ID   GPX5_PIG                Reviewed;         219 AA.
AC   O18994;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 56.
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   Flags: Precursor;
GN   Name=GPX5;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-46.
RC   TISSUE=Epididymis;
RX   MEDLINE=97415456; PubMed=9271255; DOI=10.1016/S0304-4165(97)00016-0;
RA   Okamura N., Iwaki Y., Hiramoto S., Tamba M., Bannai S., Sugita Y.,
RA   Syntin P., Dacheux F., Dacheux J.-L.;
RT   "Molecular cloning and characterization of the epididymis-specific
RT   glutathione peroxidase-like protein secreted in the porcine epididymal
RT   fluid.";
RL   Biochim. Biophys. Acta 1336:99-109(1997).
CC   -!- FUNCTION: May constitute a glutathionine peroxidase-like
CC       protective system against peroxide damage in sperm membrane
CC       lipids. Since the purified porcine enzyme has very little activity
CC       towards hydrogen peroxide or organic hydroperoxides the protective
CC       effect is not likely to be exerted by its enzymatic activity.
CC       Instead, may protect sperm from premature acrosome reaction in the
CC       epididymis by binding to lipid peroxides, which might otherwise
CC       interact with phospholipase A2 and induce the acrosome reaction.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Proximal caput epididymis.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; D37916; BAA22149.1; -; mRNA.
DR   RefSeq; NP_999051.1; -.
DR   UniGene; Ssc.14513; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 3724; SscGPx05.
DR   GeneID; 396920; -.
DR   KEGG; ssc:396920; -.
DR   HOVERGEN; O18994; -.
DR   BRENDA; 1.11.1.9; 249.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Peroxidase; Secreted;
KW   Signal.
FT   SIGNAL        1     21
FT   CHAIN        22    219       Epididymal secretory glutathione
FT                                peroxidase.
FT                                /FTId=PRO_0000013079.
FT   ACT_SITE     71     71       By similarity.
SQ   SEQUENCE   219 AA;  24936 MW;  A22850A6477A262D CRC64;
     MTVQLGAFYL FPLFMAGFVQ TNSNLEKMDC YKDVTGTIYD YDAFTLNGNE HIQFKQYAGK
     HVLFVNVATY CGLTAQYPEL NTLQEELKPF GLVVLGFPCN QFGKQEPGEN SEILLGLKYV
     RPGGGYVPNF QLFEKGDVNG EKEQKVFTFL KHSCPHPSEL IGSIGYISWE PIRVHDIRWN
     FEKFLVGPDG VPVMRWVHET PISTVKSDIL AYLKQFKTE
//