UniProt functional annotation for P08067



	UniProt functional annotation for P08067

UniProt code: P08067.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544). It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed:1657998, PubMed:2538628) (Probable). {ECO:0000269|PubMed:1657998, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:2538628, ECO:0000305|PubMed:11880631, ECO:0000305|PubMed:30598556}.

Catalytic activity: Reaction=2 [Fe(III)cytochrome c](out) + a quinol = 2 [Fe(II)cytochrome c](out) + a quinone + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA- COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:1657998, ECO:0000269|PubMed:2538628};

Cofactor: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; Evidence={ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};

Subunit: Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:1657998, PubMed:2538628, PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). RIP1 interacts with QCR10 on the intermembrane space (IMS) side, and with QCR9 (PubMed:30598556, PubMed:30598554). {ECO:0000269|PubMed:10764779, ECO:0000269|PubMed:10775262, ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:1657998, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:2538628, ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:30598556}.

Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.

Ptm: Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized RIP1. {ECO:0000269|PubMed:6309810, ECO:0000269|PubMed:8206223}.

Miscellaneous: The Rieske protein is a high potential 2Fe-2S protein. {ECO:0000305|PubMed:18390544}.

Similarity: Belongs to the Rieske iron-sulfur protein family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544). It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed:1657998, PubMed:2538628) (Probable). {ECO:0000269\|PubMed:1657998, ECO:0000269\|PubMed:18390544, ECO:0000269\|PubMed:2538628, ECO:0000305\|PubMed:11880631, ECO:0000305\|PubMed:30598556}.


Catalytic activity:		Reaction=2 [Fe(III)cytochrome c](out) + a quinol = 2 [Fe(II)cytochrome c](out) + a quinone + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA- COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269\|PubMed:1657998, ECO:0000269\|PubMed:2538628};
Cofactor:		Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; Evidence={ECO:0000269\|PubMed:10873857, ECO:0000269\|PubMed:11880631, ECO:0000269\|PubMed:18390544, ECO:0000269\|PubMed:30598554}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269\|PubMed:10873857, ECO:0000269\|PubMed:11880631, ECO:0000269\|PubMed:18390544, ECO:0000269\|PubMed:30598554};
Subunit:		Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:1657998, PubMed:2538628, PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). RIP1 interacts with QCR10 on the intermembrane space (IMS) side, and with QCR9 (PubMed:30598556, PubMed:30598554). {ECO:0000269\|PubMed:10764779, ECO:0000269\|PubMed:10775262, ECO:0000269\|PubMed:10873857, ECO:0000269\|PubMed:11880631, ECO:0000269\|PubMed:1657998, ECO:0000269\|PubMed:18390544, ECO:0000269\|PubMed:2538628, ECO:0000269\|PubMed:30598554, ECO:0000269\|PubMed:30598556}.
Subcellular location:		Mitochondrion inner membrane {ECO:0000269\|PubMed:18390544, ECO:0000269\|PubMed:30598554}; Single-pass membrane protein {ECO:0000269\|PubMed:18390544, ECO:0000269\|PubMed:30598554}.
Ptm:		Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized RIP1. {ECO:0000269\|PubMed:6309810, ECO:0000269\|PubMed:8206223}.
Miscellaneous:		The Rieske protein is a high potential 2Fe-2S protein. {ECO:0000305\|PubMed:18390544}.
Similarity:		Belongs to the Rieske iron-sulfur protein family. {ECO:0000305}.