ID   GPX5_RAT                Reviewed;         221 AA.
AC   P30710;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 114.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; 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; X62404; CAA44274.1; -; mRNA.
DR   PIR; S24328; S24328.
DR   RefSeq; NP_001099208.1; NM_001105738.1.
DR   AlphaFoldDB; P30710; -.
DR   SMR; P30710; -.
DR   PeroxiBase; 3735; RnoGPx05.
DR   GeneID; 113919; -.
DR   KEGG; rno:113919; -.
DR   CTD; 2880; -.
DR   RGD; 69227; Gpx5.
DR   InParanoid; P30710; -.
DR   OrthoDB; 1483113at2759; -.
DR   PhylomeDB; P30710; -.
DR   Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:P30710; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0097524; C:sperm plasma membrane; ISO:RGD.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
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_0000013080"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  25385 MW;  0D9D3FAAC9F12D16 CRC64;
     MAIQLRVFYL VPLLLASYVQ TTPRLEKMKM DCYKDVKGTI YNYEALSLNG KERIPFKQYA
     GKHVLFVNVA TYCGLTIQYP ELNALQDDLK QFGLVILGFP CNQFGKQEPG DNTEILPGLK
     YVRPGKGFLP NFQLFAKGDV NGEKEQEIFT FLKRSCPHPS ETVVTSKHTF WEPIKVHDIR
     WNFEKFLVGP NGVPVMRWFH QAPVSTVKSD ILAYLNQFKT I