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   03-AUG-2022, entry version 120.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-46, AND FUNCTION.
RC   TISSUE=Epididymis;
RX   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 glutathione peroxidase-like protective
CC       system against peroxide damage in sperm membrane lipids. Since the
CC       purified porcine enzyme has very little activity towards hydrogen
CC       peroxide or organic hydroperoxides the protective effect is not likely
CC       to be exerted by its enzymatic activity. Instead, may protect sperm
CC       from premature acrosome reaction in the epididymis by binding to lipid
CC       peroxides, which might otherwise interact with phospholipase A2 and
CC       induce the acrosome reaction. {ECO:0000269|PubMed:9271255}.
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   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Proximal caput epididymis.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; D37916; BAA22149.1; -; mRNA.
DR   RefSeq; NP_999051.1; NM_213886.1.
DR   AlphaFoldDB; O18994; -.
DR   SMR; O18994; -.
DR   STRING; 9823.ENSSSCP00000001283; -.
DR   PeroxiBase; 3724; SscGPx05.
DR   PaxDb; O18994; -.
DR   PeptideAtlas; O18994; -.
DR   PRIDE; O18994; -.
DR   Ensembl; ENSSSCT00000001312; ENSSSCP00000001283; ENSSSCG00000001214.
DR   Ensembl; ENSSSCT00005004486; ENSSSCP00005002630; ENSSSCG00005002918.
DR   Ensembl; ENSSSCT00015072658; ENSSSCP00015029151; ENSSSCG00015054484.
DR   Ensembl; ENSSSCT00025101265; ENSSSCP00025044755; ENSSSCG00025073518.
DR   Ensembl; ENSSSCT00030036072; ENSSSCP00030016480; ENSSSCG00030025829.
DR   Ensembl; ENSSSCT00035038593; ENSSSCP00035015405; ENSSSCG00035029146.
DR   Ensembl; ENSSSCT00040007052; ENSSSCP00040002797; ENSSSCG00040005331.
DR   Ensembl; ENSSSCT00045012696; ENSSSCP00045008711; ENSSSCG00045007605.
DR   Ensembl; ENSSSCT00050042167; ENSSSCP00050017455; ENSSSCG00050031364.
DR   Ensembl; ENSSSCT00055012184; ENSSSCP00055009620; ENSSSCG00055006273.
DR   Ensembl; ENSSSCT00060040554; ENSSSCP00060017176; ENSSSCG00060030030.
DR   Ensembl; ENSSSCT00065028217; ENSSSCP00065011566; ENSSSCG00065021191.
DR   Ensembl; ENSSSCT00070049697; ENSSSCP00070041954; ENSSSCG00070024870.
DR   GeneID; 396920; -.
DR   KEGG; ssc:396920; -.
DR   CTD; 2880; -.
DR   eggNOG; KOG1651; Eukaryota.
DR   GeneTree; ENSGT00940000163329; -.
DR   HOGENOM; CLU_029507_2_1_1; -.
DR   InParanoid; O18994; -.
DR   OMA; YTFLKVR; -.
DR   OrthoDB; 1483113at2759; -.
DR   TreeFam; TF105318; -.
DR   Reactome; R-SSC-3299685; Detoxification of Reactive Oxygen Species.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Proteomes; UP000314985; Chromosome 7.
DR   Bgee; ENSSSCG00000001214; Expressed in epididymis.
DR   ExpressionAtlas; O18994; baseline.
DR   Genevisible; O18994; SS.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Peroxidase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:9271255"
FT   CHAIN           22..219
FT                   /note="Epididymal secretory glutathione peroxidase"
FT                   /id="PRO_0000013079"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000250"
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