GPX5_MOUSE
ID GPX5_MOUSE Reviewed; 221 AA.
AC P21765; E9QK84;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 154.
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 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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Epididymis;
RX PubMed=1913244;
RA Ghyselinck N.B., Rigaudiere N., Dufaure J.-P.;
RT "Androgen-dependent protein secreted by mouse caput epididymis shows high
RT 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 PubMed=8469239; DOI=10.1210/mend.7.2.8469239;
RA Ghyselinck N.B., Dufaure I., Lareyre J.J., Rigaudiere N., Mattei M.-G.,
RA 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-221.
RC TISSUE=Epididymis;
RX 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 related
RT 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 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; M68896; AAA37729.1; -; Genomic_DNA.
DR EMBL; AC124460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X53780; CAA37796.1; -; mRNA.
DR CCDS; CCDS26270.1; -.
DR PIR; A47367; A47367.
DR RefSeq; NP_034473.2; NM_010343.2.
DR AlphaFoldDB; P21765; -.
DR SMR; P21765; -.
DR BioGRID; 200042; 1.
DR STRING; 10090.ENSMUSP00000106117; -.
DR PeroxiBase; 5578; MmGPx05.
DR PhosphoSitePlus; P21765; -.
DR CPTAC; non-CPTAC-4037; -.
DR jPOST; P21765; -.
DR MaxQB; P21765; -.
DR PaxDb; P21765; -.
DR PRIDE; P21765; -.
DR ProteomicsDB; 271052; -.
DR DNASU; 14780; -.
DR Ensembl; ENSMUST00000110491; ENSMUSP00000106117; ENSMUSG00000004344.
DR GeneID; 14780; -.
DR KEGG; mmu:14780; -.
DR UCSC; uc007ppz.2; mouse.
DR CTD; 2880; -.
DR MGI; MGI:104886; Gpx5.
DR VEuPathDB; HostDB:ENSMUSG00000004344; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000161098; -.
DR HOGENOM; CLU_029507_2_1_1; -.
DR InParanoid; P21765; -.
DR OMA; GHNTIST; -.
DR OrthoDB; 1483113at2759; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 14780; 0 hits in 74 CRISPR screens.
DR PRO; PR:P21765; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P21765; protein.
DR Bgee; ENSMUSG00000004344; Expressed in morula and 15 other tissues.
DR Genevisible; P21765; MM.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0097524; C:sperm plasma membrane; IDA:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
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_0000013078"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="H -> D (in Ref. 2; AAA37729)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="A -> R (in Ref. 2; AAA37729 and 4; CAA37796)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="F -> S (in Ref. 2; AAA37729 and 4; CAA37796)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="I -> V (in Ref. 2; AAA37729 and 4; CAA37796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25393 MW; 99FF8A2FECABFC9E CRC64;
MVTELRVFYL VPLLLASYVQ TTPRPEKMKM DCYKDVKGTI YDYEALSLNG KEHIPFKQYA
GKHVLFVNVA TYCGLTIQYP ELNALQEDLK PFGLVILGFP CNQFGKQEPG DNLEILPGLK
YVRPGKGFLP NFQLFAKGDV NGENEQKIFT FLKRSCPHPS ETVVMSKHTF WEPIKVHDIR
WNFEKFLVGP DGIPVMRWFH QAPVSTVKSD IMAYLSHFKT I
