PRDX5_MESAU
ID PRDX5_MESAU Reviewed; 18 AA.
AC P86241;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Peroxiredoxin-5, mitochondrial {ECO:0000250|UniProtKB:P30044};
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30044};
DE AltName: Full=Peroxiredoxin V {ECO:0000250|UniProtKB:P30044};
DE Short=Prx-V {ECO:0000250|UniProtKB:P30044};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000250|UniProtKB:P30044};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000305};
DE Flags: Fragment;
GN Name=PRDX5 {ECO:0000250|UniProtKB:P30044};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + 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: 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 AlphaFoldDB; P86241; -.
DR STRING; 10036.XP_005063356.1; -.
DR eggNOG; KOG0541; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Antioxidant; Cytoplasm; Mitochondrion; Oxidoreductase; Peroxidase;
KW Peroxisome; Phosphoprotein; Redox-active center; Reference proteome.
FT CHAIN <1..>18
FT /note="Peroxiredoxin-5, mitochondrial"
FT /id="PRO_0000394425"
FT DOMAIN <1..>18
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R063"
FT NON_TER 1
FT NON_TER 18
SQ SEQUENCE 18 AA; 2063 MW; D99825F873E5178A CRC64;
ETDLLLDDSL VSLFGNRR
