UniProt functional annotation for P30044



	UniProt functional annotation for P30044

UniProt code: P30044.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410, ECO:0000269|PubMed:31740833}.

Catalytic activity: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]- disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA- COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:10751410};

Subunit: Monomer. {ECO:0000269|PubMed:20643143}.

Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410, ECO:0000269|PubMed:31740833}.

Subcellular location: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10751410}. Peroxisome matrix {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410}. Note=Imported into peroxisomes via peroxisomal targeting signal 1 receptor PEX5. {ECO:0000269|PubMed:10514471}.

Tissue specificity: Widely expressed. {ECO:0000269|PubMed:10521424}.

Ptm: S-palmitoylated (PubMed:31740833). Palmitoylation occurs on the active site, inhibiting its reactivity; therefore PRDX5 palmitoylation status determines its antioxidant capacity (PubMed:31740833). {ECO:0000269|PubMed:31740833}.

Ptm: [Isoform Mitochondrial]: S-palmitoylated (PubMed:31740833). Depalmitoylated by ABHD10 (PubMed:31740833). {ECO:0000269|PubMed:31740833}.

Miscellaneous: The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys Prx, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin. {ECO:0000305|PubMed:10751410, ECO:0000305|PubMed:18489898}.

Miscellaneous: [Isoform 4]: Produced by alternative splicing. {ECO:0000305}.

Similarity: Belongs to the peroxiredoxin family. Prx5 subfamily. {ECO:0000305}.

Sequence caution: Sequence=AAF17200.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. {ECO:0000269\|PubMed:10514471, ECO:0000269\|PubMed:10521424, ECO:0000269\|PubMed:10751410, ECO:0000269\|PubMed:31740833}.


Catalytic activity:		Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]- disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA- COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269\|PubMed:10751410};
Subunit:		Monomer. {ECO:0000269\|PubMed:20643143}.
Subcellular location:		[Isoform Mitochondrial]: Mitochondrion {ECO:0000269\|PubMed:10521424, ECO:0000269\|PubMed:10751410, ECO:0000269\|PubMed:31740833}.
Subcellular location:		[Isoform Cytoplasmic+peroxisomal]: Cytoplasm {ECO:0000269\|PubMed:10514471, ECO:0000269\|PubMed:10751410}. Peroxisome matrix {ECO:0000269\|PubMed:10514471, ECO:0000269\|PubMed:10521424, ECO:0000269\|PubMed:10751410}. Note=Imported into peroxisomes via peroxisomal targeting signal 1 receptor PEX5. {ECO:0000269\|PubMed:10514471}.
Tissue specificity:		Widely expressed. {ECO:0000269\|PubMed:10521424}.
Ptm:		S-palmitoylated (PubMed:31740833). Palmitoylation occurs on the active site, inhibiting its reactivity; therefore PRDX5 palmitoylation status determines its antioxidant capacity (PubMed:31740833). {ECO:0000269\|PubMed:31740833}.
Ptm:		[Isoform Mitochondrial]: S-palmitoylated (PubMed:31740833). Depalmitoylated by ABHD10 (PubMed:31740833). {ECO:0000269\|PubMed:31740833}.
Miscellaneous:		The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys Prx, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin. {ECO:0000305\|PubMed:10751410, ECO:0000305\|PubMed:18489898}.
Miscellaneous:		[Isoform 4]: Produced by alternative splicing. {ECO:0000305}.
Similarity:		Belongs to the peroxiredoxin family. Prx5 subfamily. {ECO:0000305}.
Sequence caution:		Sequence=AAF17200.1; Type=Frameshift; Evidence={ECO:0000305};