ID   PRDX5_VULVU             Reviewed;          16 AA.
AC   P83200;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   02-SEP-2026, entry version 33.
DE   RecName: Full=Peroxiredoxin-5;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P30044};
DE   AltName: Full=Autoantigenic sperm protein 5;
DE   AltName: Full=Peroxiredoxin V;
DE            Short=Prx-V;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000305};
DE   AltName: Full=fSP5;
DE   Flags: Fragment;
GN   Name=PRDX5;
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Sperm {ECO:0000269|Ref.1};
RA   Verdier Y., Rouet N., Artois M., Boue F.;
RT   "Partial characterisation of antigenic sperm proteins in foxes (Vulpes
RT   vulpes).";
RL   Submitted (DEC-2001) to UniProtKB.
RN   [2]
RP   IDENTIFICATION BY 2D-PAGE.
RX   PubMed=12065460; DOI=10.1002/j.1939-4640.2002.tb02275.x;
RA   Verdier Y., Rouet N., Artois M., Boue F.;
RT   "Partial characterization of antigenic sperm proteins in foxes (Vulpes
RT   vulpes).";
RL   J. Androl. 23:529-536(2002).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000250|UniProtKB:P30044}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol +
CC         [thioredoxin]-disulfide + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000250|UniProtKB:P30044};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30044}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P30044}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix
CC       {ECO:0000250|UniProtKB:P30044}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.8,
CC       its MW is: 16.9 kDa. {ECO:0000269|PubMed:12065460}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC       Prx, C(R) is present in the same subunit to form an intramolecular
CC       disulfide. The disulfide is subsequently reduced by thioredoxin.
CC       {ECO:0000250|UniProtKB:P30044}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000305}.
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DR   Proteomes; UP001652641; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Antioxidant; Cytoplasm; Direct protein sequencing; Mitochondrion;
KW   Oxidoreductase; Peroxidase; Peroxisome; Redox-active center;
KW   Reference proteome.
FT   CHAIN           1..>16
FT                   /note="Peroxiredoxin-5"
FT                   /id="PRO_0000312688"
FT   NON_TER         16
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   16 AA;  1677 MW;  1138D10324279F20 CRC64;
     APIKVGDAIP XVXVFE
//