ID   GPX5_CANFA              Reviewed;         221 AA.
AC   O46607;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 55.
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   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epididymis;
RX   MEDLINE=98304457; PubMed=9640275;
RA   Beiglboeck A., Pera I., Ellerbrock K., Kirchhoff C.;
RT   "Dog epididymis-specific mRNA encoding secretory glutathione
RT   peroxidase-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
CC       glutathionine peroxidase-like protective system against peroxide
CC       damage in sperm membrane lipids.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Epididymis.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; AF045185; AAC02550.1; -; mRNA.
DR   RefSeq; NP_001003213.1; -.
DR   UniGene; Cfa.3743; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 3737; CfaGPx05.
DR   Ensembl; ENSCAFG00000011947; Canis familiaris.
DR   GeneID; 403877; -.
DR   KEGG; cfa:403877; -.
DR   HOVERGEN; O46607; -.
DR   BRENDA; 1.11.1.9; 463.
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   2: Evidence at transcript level;
KW   Oxidoreductase; Peroxidase; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    221       Epididymal secretory glutathione
FT                                peroxidase.
FT                                /FTId=PRO_0000013075.
FT   ACT_SITE     73     73       By similarity.
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
//