GPX5_MACFA
ID GPX5_MACFA Reviewed; 221 AA.
AC P28714;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Epididymal secretory glutathione peroxidase;
DE EC=1.11.1.9;
DE AltName: Full=Epididymis-specific glutathione peroxidase-like protein;
DE Short=EGLP;
DE AltName: Full=Glutathione peroxidase 5;
DE Short=GPx-5;
DE Short=GSHPx-5;
DE Flags: Precursor;
GN Name=GPX5;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RX PubMed=1386734; DOI=10.1042/bj2850863;
RA Perry A.C.F., Jones R., Niang L.S.P., Jackson R.M., Hall L.;
RT "Genetic evidence for an androgen-regulated epididymal secretory
RT glutathione peroxidase whose transcript does not contain a selenocysteine
RT codon.";
RL Biochem. J. 285:863-870(1992).
CC -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC organic hydroperoxide, by glutathione. May constitute a glutathione
CC peroxidase-like protective system against peroxide damage in sperm
CC membrane lipids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Epididymis.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; X62403; CAA44273.1; -; mRNA.
DR PIR; S24327; S24327.
DR RefSeq; NP_001274571.1; NM_001287642.1.
DR AlphaFoldDB; P28714; -.
DR SMR; P28714; -.
DR STRING; 9541.XP_005553769.1; -.
DR PeroxiBase; 3738; MfaGPx05.
DR Ensembl; ENSMFAT00000009347; ENSMFAP00000035112; ENSMFAG00000004017.
DR GeneID; 102137743; -.
DR CTD; 2880; -.
DR VEuPathDB; HostDB:ENSMFAG00000004017; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000164550; -.
DR OMA; HELMNGI; -.
DR OrthoDB; 1483113at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase; Peroxidase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..221
FT /note="Epididymal secretory glutathione peroxidase"
FT /id="PRO_0000013077"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 25212 MW; 32AE912ED6C73D93 CRC64;
MTTQLRVVHL LPLLLACFVQ TSPKQETMKM DCHKDEKGTI YDYEAIALNK NEYVPFKQYV
GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP CNQFGKQEPG DNKEILPGLK
YVRPGGGFVP NFQLFEKGDV NGEKEQKVFS FLKHSCPHPS EILGTFKSIS WDPVKVHDIR
WNFEKFLVGP DGIPVMRWSH RATVSSVKTD ILAYLKQFKT K
