ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   18-JUN-2025, entry version 170.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://www.proteinspotlight.org/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   RefSeq; XP_028701781.1; XM_028845948.1.
DR   RefSeq; XP_028701782.1; XM_028845949.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   FunCoup; P00002; 2331.
DR   STRING; 9544.ENSMMUP00000073390; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   GeneID; 100425223; -.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; DKGIIWD; -.
DR   OrthoDB; 9508248at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other cell types or tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   FunFam; 1.10.760.10:FF:000008; Cytochrome c; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   09-APR-2025, entry version 169.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://www.proteinspotlight.org/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   RefSeq; XP_028701781.1; XM_028845948.1.
DR   RefSeq; XP_028701782.1; XM_028845949.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000073390; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   GeneID; 100425223; -.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; DKGIIWD; -.
DR   OrthoDB; 9508248at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other cell types or tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0043293; C:apoptosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   FunFam; 1.10.760.10:FF:000008; Cytochrome c; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-FEB-2025, entry version 168.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000073390; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; DKGIIWD; -.
DR   OrthoDB; 9508248at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other cell types or tissues.
DR   GO; GO:0043293; C:apoptosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   FunFam; 1.10.760.10:FF:000008; Cytochrome c; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-NOV-2024, entry version 167.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000073390; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; MPAPYKK; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   FunFam; 1.10.760.10:FF:000008; Cytochrome c; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-OCT-2024, entry version 166.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000073390; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; MPAPYKK; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000073390; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; MPAPYKK; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other cell types or tissues.
DR   ExpressionAtlas; P00002; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000073390; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; CHTITEG; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other cell types or tissues.
DR   ExpressionAtlas; P00002; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-NOV-2023, entry version 163.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PaxDb; 9544-ENSMMUP00000035167; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; CHTITEG; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other tissues.
DR   ExpressionAtlas; P00002; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   28-JUN-2023, entry version 162.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; CHTITEG; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-MAY-2023, entry version 161.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; CHTITEG; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   22-FEB-2023, entry version 160.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   Ensembl; ENSMMUT00000081058.1; ENSMMUP00000073390.1; ENSMMUG00000051205.1.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF29; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   14-DEC-2022, entry version 159.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   12-OCT-2022, entry version 158.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000051205; Expressed in colon and 21 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 156.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366; DOI=10.1016/s0021-9258(18)97056-0;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   AlphaFoldDB; P00002; -.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in heart and 24 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme c axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme c axial ligand)"
FT   BINDING         15
FT                   /note="Heme c; covalent"
FT   BINDING         18
FT                   /note="Heme c; covalent"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-FEB-2022, entry version 155.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in heart and 24 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme; covalent"
FT   BINDING         18
FT                   /note="Heme; covalent"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   29-SEP-2021, entry version 154.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   VEuPathDB; HostDB:ENSMMUG00000051205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in heart and 24 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme; covalent"
FT   BINDING         18
FT                   /note="Heme; covalent"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-JUN-2021, entry version 153.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   BMRB; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in heart and 24 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme; covalent"
FT   BINDING         18
FT                   /note="Heme; covalent"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-APR-2021, entry version 152.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   BMRB; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in heart and 23 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme; covalent"
FT   BINDING         18
FT                   /note="Heme; covalent"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-OCT-2020, entry version 151.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   BMRB; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in heart and 23 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme (covalent)"
FT   BINDING         18
FT                   /note="Heme (covalent)"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   12-AUG-2020, entry version 150.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in heart and 23 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme (covalent)"
FT   BINDING         18
FT                   /note="Heme (covalent)"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   17-JUN-2020, entry version 149.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in colon and 13 other tissues.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme (covalent)"
FT   BINDING         18
FT                   /note="Heme (covalent)"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   26-FEB-2020, entry version 148.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; Expressed in colon and 13 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme (covalent)"
FT   BINDING         18
FT                   /note="Heme (covalent)"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 147.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND PROTEIN
RP   SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000081058; ENSMMUP00000073390; ENSMMUG00000051205.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108221"
FT   METAL           19
FT                   /note="Iron (heme axial ligand)"
FT   METAL           81
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         15
FT                   /note="Heme (covalent)"
FT   BINDING         18
FT                   /note="Heme (covalent)"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:4954366"
FT   MOD_RES         49
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         56
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62894"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62897"
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-OCT-2019, entry version 146.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   InParanoid; P00002; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   18-SEP-2019, entry version 145.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   InParanoid; P00002; -.
DR   OMA; QGPNLYG; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   31-JUL-2019, entry version 144.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   InParanoid; P00002; -.
DR   OMA; QGPNLYG; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-JUL-2019, entry version 143.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   InParanoid; P00002; -.
DR   OMA; QGPNLYG; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAY-2019, entry version 142.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; QGPNLYG; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JAN-2019, entry version 141.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; GLFKTRC; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-NOV-2018, entry version 140.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; GLFKTRC; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   12-SEP-2018, entry version 139.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; GLFKTRC; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; Expressed in 14 organ(s), highest expression level in colon.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   22-NOV-2017, entry version 138.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; GLFKTRC; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-OCT-2017, entry version 137.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   iPTMnet; P00002; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; GLFKTRC; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-JUN-2017, entry version 136.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; GLFKTRC; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   15-MAR-2017, entry version 135.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; DLITWLK; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   15-FEB-2017, entry version 134.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; DLITWLK; -.
DR   OrthoDB; EOG090A0F2E; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   18-JAN-2017, entry version 133.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; DLITWLK; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; -.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   30-NOV-2016, entry version 132.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; DLITWLK; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Unplaced.
DR   Bgee; ENSMMUG00000030295; -.
DR   ExpressionAtlas; P00002; differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-OCT-2016, entry version 131.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; DLITWLK; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; -.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-SEP-2016, entry version 130.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; DLITWLK; -.
DR   OrthoDB; EOG091G0UQY; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000030295; -.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   06-JUL-2016, entry version 129.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HTVGAGE; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-JUN-2016, entry version 128.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:106992390; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; HTVGAGE; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAR-2016, entry version 127.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2, AND
RP   PROTEIN SEQUENCE OF 56-62 AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_014992345.1; XM_015136859.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 106992390; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HTVGAGE; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4954366}.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   17-FEB-2016, entry version 126.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HTVGAGE; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      56     56       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      73     73       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P62897}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES     100    100       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62897}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-JAN-2016, entry version 125.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HTVGAGE; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   09-DEC-2015, entry version 124.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HTVGAGE; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-NOV-2015, entry version 123.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   eggNOG; COG3474; LUCA.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HTVGAGE; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Unplaced.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   14-OCT-2015, entry version 122.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HGLWGRK; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Unplaced.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-SEP-2015, entry version 121.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HGLWGRK; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   22-JUL-2015, entry version 120.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; HGLWGRK; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JUN-2015, entry version 119.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; TWLKEST; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-MAR-2015, entry version 118.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; TWLKEST; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
FT   MOD_RES      98     98       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62894}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-FEB-2015, entry version 117.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; TWLKEST; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES      98     98       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-JAN-2015, entry version 116.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; TWLKEST; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES      98     98       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   29-OCT-2014, entry version 115.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; CHNLKEG; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   ExpressionAtlas; P00002; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES      98     98       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   01-OCT-2014, entry version 114.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; CHNLKEG; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT                                {ECO:0000269|PubMed:4954366}.
FT   MOD_RES      49     49       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES      98     98       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   14-MAY-2014, entry version 113.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; CHNLKEG; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-APR-2014, entry version 112.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KQKGIEW; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   19-FEB-2014, entry version 111.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/076";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KQKGIEW; -.
DR   OrthoDB; EOG761BWX; -.
DR   TreeFam; TF300226; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-NOV-2013, entry version 110.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KQKGIEW; -.
DR   OrthoDB; EOG761BWX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-OCT-2013, entry version 109.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KQKGIEW; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   18-SEP-2013, entry version 108.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_dom.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-APR-2013, entry version 107.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; 9544.ENSMMUP00000035167; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   06-MAR-2013, entry version 106.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   28-NOV-2012, entry version 105.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome_c_R; 1.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-OCT-2012, entry version 104.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-SEP-2012, entry version 103.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-JUL-2012, entry version 102.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Note=Loosely associated with the inner membrane.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 101.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOGENOM; HOG000009762; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   18-APR-2012, entry version 100.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   NextBio; 19960629; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   22-FEB-2012, entry version 99.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; COG3474; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   KO; K08738; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-NOV-2011, entry version 98.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; prNOG20206; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   KO; K08738; -.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   19-OCT-2011, entry version 97.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   PRIDE; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; prNOG20206; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   21-SEP-2011, entry version 96.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; prNOG20206; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; KMIYAGL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Complete proteome; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-JUL-2011, entry version 95.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; prNOG20206; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   28-JUN-2011, entry version 94.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 54205; -.
DR   eggNOG; prNOG20206; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 100425223; -.
DR   eggNOG; prNOG20206; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-FEB-2011, entry version 92.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 100425223; -.
DR   eggNOG; prNOG20206; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-JAN-2011, entry version 91.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 100425223; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   30-NOV-2010, entry version 90.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; XM_002803349.1.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   CTD; 100425223; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuc...; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-NOV-2010, entry version 89.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; -.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:100425223; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuc...; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-OCT-2010, entry version 88.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; -.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295.
DR   GeneID; 100425223; -.
DR   CTD; 703093; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuc...; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-AUG-2010, entry version 87.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_002803395.1; -.
DR   UniGene; Mmu.1466; -.
DR   ProteinModelPortal; P00002; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 100425223; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuc...; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUL-2010, entry version 86.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; ANLKEWL; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-APR-2010, entry version 85.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; SACHAIG; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-MAR-2010, entry version 84.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P00002; -.
DR   OMA; SACHAIG; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   09-FEB-2010, entry version 83.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; P00002; -.
DR   InParanoid; P00002; -.
DR   OMA; SACHAIG; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   19-JAN-2010, entry version 82.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   eggNOG; prNOG20206; -.
DR   HOVERGEN; P00002; -.
DR   InParanoid; P00002; -.
DR   OMA; SACHAIG; -.
DR   OrthoDB; EOG9TF34R; -.
DR   PhylomeDB; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   15-DEC-2009, entry version 81.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   HOVERGEN; P00002; -.
DR   InParanoid; P00002; -.
DR   OMA; SACHAIG; -.
DR   OrthoDB; EOG9TF34R; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-NOV-2009, entry version 80.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   HOVERGEN; P00002; -.
DR   OMA; SACHAIG; -.
DR   OrthoDB; EOG9TF34R; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-NOV-2009, entry version 79.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   HOVERGEN; P00002; -.
DR   OMA; TMSDYLE; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   01-SEP-2009, entry version 78.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   STRING; P00002; -.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   CTD; 703093; -.
DR   HOVERGEN; P00002; -.
DR   OMA; P00002; TMSDYLE.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   28-JUL-2009, entry version 77.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUT00000042168; ENSMMUP00000035167; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   OMA; P00002; TMSDYLE.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   OMA; P00002; TMSDYLE.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-MAY-2009, entry version 75.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   OMA; P00002; QGADIES.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   14-APR-2009, entry version 74.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-MAR-2009, entry version 73.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-MAR-2009, entry version 72.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 71.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   22-JUL-2008, entry version 70.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-JUN-2008, entry version 69.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   HOVERGEN; P00002; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAY-2008, entry version 68.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   KEGG; mcc:703093; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   26-FEB-2008, entry version 67.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-DEC-2007, entry version 66.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
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CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-OCT-2007, entry version 65.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight;
CC       Note=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   RefSeq; XP_001095344.1; -.
DR   RefSeq; XP_001095458.1; -.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   GeneID; 703093; -.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-SEP-2007, entry version 64.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight;
CC       Note=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JUL-2007, entry version 63.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-JUL-2007, entry version 62.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   12-JUN-2007, entry version 61.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   01-MAY-2007, entry version 60.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF500152; Cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   17-APR-2007, entry version 59.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   UniGene; Mmu.1466; -.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc/c2.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 58.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   Ensembl; ENSMMUG00000030295; Macaca mulatta.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc/c2.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         105 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 57.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 56-62
RP   AND 69-71.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 2-105.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc/c2.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11737 MW;  B590589E01024BE1 CRC64;
     MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//
ID   CYC_MACMU               Reviewed;         104 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   12-DEC-2006, entry version 56.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Life shuttle - Issue 76 of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc/c2.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      0      0
FT   CHAIN         1    104       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU               Reviewed;         104 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   28-NOV-2006, entry version 55.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc/c2.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   CHAIN         1    104       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU               Reviewed;         104 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   31-OCT-2006, entry version 54.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS:UniProtKB.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc/c2.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   CHAIN         1    104       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   17-OCT-2006, entry version 53.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc/c2.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   CHAIN         1    104       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   18-APR-2006, entry version 52.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   CHAIN         1    104       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   07-FEB-2006, entry version 51.
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   CHAIN         1    104       Cytochrome c.
FT                                /FTId=PRO_0000108221.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   07-FEB-2006 (Rel. 49, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   24-JAN-2006 (Rel. 49, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   LinkHub; P00002; -.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c_c2; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR012125; Cytc.
DR   InterPro; IPR012282; Cytochrome_c_R.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00002; 1-104.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain; Transport.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000001; Cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain; Transport.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain; Transport.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain; Transport.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND PROTEIN SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   GO; GO:0005829; C:cytosol; ISS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS.
DR   GO; GO:0008635; P:caspase activation via cytochrome c; ISS.
DR   GO; GO:0045333; P:cellular respiration; ISS.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY SEQUENCE, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY SEQUENCE, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY SEQUENCE, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Mitochondrion; Respiratory chain.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Cytochrome c.
GN   Name=CYCS; Synonyms=CYC;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PRELIMINARY SEQUENCE, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation; Direct protein sequencing.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUN-2004 (Rel. 44, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation; Direct protein sequencing.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUN-2004 (Rel. 44, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       N-acetylglycine.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-OCT-2003 (Rel. 42, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 2PCB.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-OCT-2003 (Rel. 42, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-OCT-2003 (Rel. 42, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        80     80       Iron (heme axial ligand).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   10-OCT-2003 (Rel. 42, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-SEP-2003 (Rel. 42, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds 1 heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   28-FEB-2003 (Rel. 41, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds one heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   28-FEB-2003 (Rel. 41, Last annotation update)
DE   Cytochrome c.
GN   CYCS OR CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds one heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Cytochrome c.
GN   CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds one heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAR-2002 (Rel. 41, Last annotation update)
DE   Cytochrome c.
GN   CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds one heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1WEJ.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAR-2002 (Rel. 41, Last annotation update)
DE   Cytochrome c.
GN   CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: Binds one heme group per molecule.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1HRC.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-MAR-2002 (Rel. 41, Last annotation update)
DE   Cytochrome c.
GN   CYC.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1HRC.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   Cytochrome c.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1HRC.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   Cytochrome c.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1HRC.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   Cytochrome c.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   Cytochrome C.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   CYTOCHROME C.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   CYTOCHROME C.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   InterPro; IPR000345; CytC_heme_bind.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; -; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   CYTOCHROME C.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   InterPro; IPR000345; -.
DR   InterPro; IPR002327; -.
DR   InterPro; IPR003088; -.
DR   Pfam; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   CYTOCHROME C.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE=66045191; PubMed=4954366;
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   INTERPRO; IPR000345; -.
DR   INTERPRO; IPR002327; -.
DR   INTERPRO; IPR003088; -.
DR   PFAM; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   CYTOCHROME C.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae;
OC   Cercopithecinae; Macaca.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE; 66045191.
RA   Rothfus J.A., Smith E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   INTERPRO; IPR000345; -.
DR   INTERPRO; IPR002327; -.
DR   INTERPRO; IPR003088; -.
DR   PFAM; PF00034; cytochrome_c; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  EF05AB513DF1DE48 CRC64;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   CYTOCHROME C.
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC   Eutheria; Primates; Catarrhini; Cercopithecidae; Cercopithecinae;
OC   Macaca.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE; 66045191.
RA   ROTHFUS J.A., SMITH E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. Biol. Chem. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   HSSP; P00004; 1OCD.
DR   PFAM; PF00034; cytochrome_c; 1.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   Mitochondrion; Electron transport; Respiratory chain; Heme;
KW   Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  F099A8BF CRC32;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA;
OC   PRIMATES; CATARRHINI; CERCOPITHECIDAE; CERCOPITHECINAE; MACACA.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE; 66045191.
RA   ROTHFUS J.A., SMITH E.L.;
RT   "Amino acid sequence of rhesus monkey heart cytochrome c.";
RL   J. BIOL. CHEM. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
DR   PFAM; PF00034; cytochrome_c; 1.
DR   HSSP; P00004; 1OCD.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN; HEME;
KW   ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  F099A8BF CRC32;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE)
DT   01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE; 66045191.
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- PTM: BINDS ONE HEME GROUP PER MOLECULE.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00025; 2FRC.
DR   PROSITE; PS00190; CYTOCHROME_C; 1.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN; HEME;
KW   ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  F099A8BF CRC32;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987 (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE; 66045191.
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00025; 1FRC.
DR   PROSITE; PS00190; CYTOCHROME_C.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  F099A8BF CRC32;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987 (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RX   MEDLINE; 66045191.
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00025; 1FRC.
DR   PROSITE; PS00190; CYTOCHROME_C.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987 (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RM   66045191
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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DR   PIR; A00003; CCMQR.
DR   HSSP; P00025; 1FRC.
DR   PROSITE; PS00190; CYTOCHROME_C.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC_MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987 (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RM   66045191
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR   PIR; A00003; CCMQR.
DR   PROSITE; PS00190; CYTOCHROME_C.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC$MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987 (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   COMPOSITION OF CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF 55-61 AND 68-70.
RC   MEDLINE=66045191;
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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DR   PIR; A00003; CCMQR.
DR   PROSITE; PS00190; CYTOCHROME_C.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC$MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986  (REL. 01, CREATED)
DT   21-JUL-1986  (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987  (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   MACACA MULATTA (RHESUS MACAQUE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1] (COMP. OF CHYMOTRYPTIC PEPTIDES AND SEQ. OF 55-61 AND 68-70)
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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DR   PIR; A00003; CCMQR.
DR   PROSITE; PS00190; CYTOCHROME_C.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC$MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986  (REL. 01, CREATED)
DT   21-JUL-1986  (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987  (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   RHESUS MACAQUE (MACACA MULATTA).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1] (COMP. OF CHYMOTRYPTIC PEPTIDES AND SEQ. OF 55-61 AND 68-70)
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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DR   PIR; A00003; CCMQR.
DR   PROSITE; PS00190; CYTOCHROME_C.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC$MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   21-JUL-1986  (REL. 01, CREATED)
DT   21-JUL-1986  (REL. 01, LAST SEQUENCE UPDATE)
DT   13-AUG-1987  (REL. 05, LAST ANNOTATION UPDATE)
DE   CYTOCHROME C.
OS   RHESUS MACAQUE (MACACA MULATTA).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1] (COMP. OF CHYMOTRYPTIC PEPTIDES AND SEQ. OF 55-61 AND 68-70)
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//
ID   CYC$MACMU      STANDARD;      PRT;   104 AA.
AC   P00002;
DT   13-AUG-1987  (DR LINES EDITED)
DT   21-JUL-1986  (ADAPTED FROM A PIR ENTRY)
DE   CYTOCHROME C.
OS   RHESUS MACAQUE (MACACA MULATTA).
OC   EUKARYOTA.
RN   [1] (COMP. OF CHYMOTRYPTIC PEPTIDES AND SEQ. OF 55-61 AND 68-70)
RA   ROTHFUS J.A., SMITH E.L.;
RL   J. BIOL. CHEM. 240:4277-4283(1965).
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   PIR; A00003; CCMQR.
KW   MITOCHONDRION; ELECTRON TRANSPORT; RESPIRATORY CHAIN;
KW   OXIDATIVE PHOSPHORYLATION; HEME; ACETYLATION.
FT   MOD_RES       1      1       ACETYLATION.
FT   BINDING      14     14       HEME (COVALENT).
FT   BINDING      17     17       HEME (COVALENT).
FT   METAL        18     18       IRON (HEME AXIAL LIGAND).
FT   METAL        80     80       IRON (HEME AXIAL LIGAND).
SQ   SEQUENCE   104 AA;  11605 MW;  55855 CN;
     GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGITWG
     EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE
//