GPX1_CAEEL
ID GPX1_CAEEL Reviewed; 163 AA.
AC O02621;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glutathione peroxidase 1;
DE EC=1.11.1.9;
GN Name=gpx-1; ORFNames=F26E4.12;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: May constitute a glutathione peroxidase-like protective
CC system against oxidative stresses. {ECO:0000250}.
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: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; Z81070; CAB03004.1; -; Genomic_DNA.
DR PIR; T21418; T21418.
DR RefSeq; NP_492598.1; NM_060197.1.
DR AlphaFoldDB; O02621; -.
DR SMR; O02621; -.
DR BioGRID; 49762; 13.
DR STRING; 6239.F26E4.12; -.
DR PeroxiBase; 3746; CelGPx01.
DR EPD; O02621; -.
DR PaxDb; O02621; -.
DR PeptideAtlas; O02621; -.
DR EnsemblMetazoa; F26E4.12.1; F26E4.12.1; WBGene00009165.
DR GeneID; 184981; -.
DR KEGG; cel:CELE_F26E4.12; -.
DR UCSC; F26E4.12; c. elegans.
DR CTD; 184981; -.
DR WormBase; F26E4.12; CE09696; WBGene00009165; gpx-1.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_0_1_1; -.
DR InParanoid; O02621; -.
DR OMA; GFMFDAI; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; O02621; -.
DR PRO; PR:O02621; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009165; Expressed in embryo and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IMP:WormBase.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; HEP:WormBase.
DR GO; GO:0090087; P:regulation of peptide transport; IMP:WormBase.
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 InterPro; IPR013766; Thioredoxin_domain.
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 3: Inferred from homology;
KW Cytoplasm; Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..163
FT /note="Glutathione peroxidase 1"
FT /id="PRO_0000066646"
FT ACT_SITE 36
FT /evidence="ECO:0000250"
SQ SEQUENCE 163 AA; 18424 MW; 441535A92DC4330F CRC64;
MSSVYDFNVK NANGDDVSLS DYKGKVLIIV NVASQCGLTN KNYTQLKELL DVYKKDGLEV
LAFPCNQFAG QEPSCEIDIQ AFVADKFKFE PTLFQKIDVN GDKQSPLFKF LKNEKGGFMF
DAIKWNFTKF LVGRDGKIIK RFGPTTDPKD MEKDIKEALG EKL