ID   GPX5_CANLF              Reviewed;         221 AA.
AC   O46607;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 106.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epididymis;
RX   PubMed=9640275; DOI=10.1530/jrf.0.1120357;
RA   Beiglboeck A., Pera I., Ellerbrock K., Kirchhoff C.;
RT   "Dog epididymis-specific mRNA encoding secretory glutathione peroxidase-
RT   like protein.";
RL   J. Reprod. Fertil. 112:357-367(1998).
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; AF045185; AAC02550.1; -; mRNA.
DR   RefSeq; NP_001003213.1; NM_001003213.1.
DR   AlphaFoldDB; O46607; -.
DR   SMR; O46607; -.
DR   STRING; 9612.ENSCAFP00000017573; -.
DR   PeroxiBase; 3737; CfaGPx05.
DR   PaxDb; O46607; -.
DR   GeneID; 403877; -.
DR   KEGG; cfa:403877; -.
DR   CTD; 2880; -.
DR   eggNOG; KOG1651; Eukaryota.
DR   InParanoid; O46607; -.
DR   OrthoDB; 1483113at2759; -.
DR   Proteomes; UP000002254; Unplaced.
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   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_0000013075"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  25338 MW;  C90EF0F0B88C9ACF CRC64;
     MTAWLGASYV LPILLVSFVQ TNAKPEKTKM DCYKDVKGTI YEYEALTLNG NERIQFKQYP
     RKHVLFVNVA TYCGLTAQYP ELNSLQEELK PLGLVVLGFP CNQFGKQGPG ENSEILPGLK
     YVRPGRGYVP NFQLFEKGDV NGEKEQKVFT FLKLSCPHPS EVLGSFRHIS WDPVKVHDIR
     WNFEKFLVGP DGVPVLRWFH RTPISTVKED ILVYLKQLKM K