ID   GPX5_MOUSE              Reviewed;         221 AA.
AC   P21765;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   25-NOV-2008, entry version 74.
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=Major androgen-regulated protein;
DE   AltName: Full=arMEP24;
DE   Flags: Precursor;
GN   Name=Gpx5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Epididymis;
RX   MEDLINE=92004864; PubMed=1913244;
RA   Ghyselinck N.B., Rigaudiere N., Dufaure J.-P.;
RT   "Androgen-dependent protein secreted by mouse caput epididymis shows
RT   high homologies with different glutathione peroxidases.";
RL   C. R. Acad. Sci. III, Sci. Vie 313:1-6(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93225968; PubMed=8469239; DOI=10.1210/me.7.2.258;
RA   Ghyselinck N.B., Dufaure I., Lareyre J.J., Rigaudiere N.,
RA   Mattei M.-G., Dufaure J.-P.;
RT   "Structural organization and regulation of the gene for the androgen-
RT   dependent glutathione peroxidase-like protein specific to the mouse
RT   epididymis.";
RL   Mol. Endocrinol. 7:258-272(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 47-221.
RC   TISSUE=Epididymis;
RX   MEDLINE=91088305; PubMed=2263479; DOI=10.1093/nar/18.23.7144;
RA   Ghyselinck N.B., Dufaure J.-P.;
RT   "A mouse cDNA sequence for epididymal androgen-regulated proteins
RT   related to glutathione peroxidase.";
RL   Nucleic Acids Res. 18:7144-7144(1990).
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; M68896; AAA37729.1; -; Genomic_DNA.
DR   EMBL; X53780; CAA37796.1; -; mRNA.
DR   PIR; A47367; A47367.
DR   UniGene; Mm.1332; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 5578; MmGPx05.
DR   Ensembl; ENSMUSG00000004344; Mus musculus.
DR   MGI; MGI:104886; Gpx5.
DR   HOGENOM; P21765; -.
DR   HOVERGEN; P21765; -.
DR   ArrayExpress; P21765; -.
DR   CleanEx; MM_GPX5; -.
DR   GermOnline; ENSMUSG00000004344; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR000889; Glut_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_0000013078.
FT   ACT_SITE     73     73       By similarity.
FT   CONFLICT     53     53       D -> H (in Ref. 3; CAA37796).
FT   CONFLICT    103    103       Q -> E (in Ref. 2).
FT   CONFLICT    170    170       S -> F (in Ref. 2).
SQ   SEQUENCE   221 AA;  25382 MW;  DE5F8BD6CD22D6F9 CRC64;
     MVTELRVFYL VPLLLASYVQ TTPRPEKMKM DCYKDVKGTI YDYEALSLNG KEDIPFKQYR
     GKHVLFVNVA TYCGLTIQYP ELNALQEDLK PFGLVILGFP CNQFGKQEPG DNLEILPGLK
     YVRPGKGFLP NFQLFAKGDV NGENEQKIFT FLKRSCPHPS ETVVMSKHTS WEPIKVHDIR
     WNFEKFLVGP DGVPVMRWFH QAPVSTVKSD IMAYLSHFKT I
//