GPX3_CAEEL
ID GPX3_CAEEL Reviewed; 224 AA.
AC Q95003;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glutathione peroxidase 3;
DE EC=1.11.1.9;
DE Flags: Precursor;
GN Name=gpx-3; ORFNames=C11E4.2;
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 -!- 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, extracellular space {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; Z81015; CAB02655.1; -; Genomic_DNA.
DR PIR; T19190; T19190.
DR RefSeq; NP_509616.1; NM_077215.4.
DR AlphaFoldDB; Q95003; -.
DR SMR; Q95003; -.
DR STRING; 6239.C11E4.2; -.
DR PeroxiBase; 3748; CelGPx03.
DR PaxDb; Q95003; -.
DR PeptideAtlas; Q95003; -.
DR EnsemblMetazoa; C11E4.2.1; C11E4.2.1; WBGene00007517.
DR GeneID; 182513; -.
DR KEGG; cel:CELE_C11E4.2; -.
DR UCSC; C11E4.2; c. elegans.
DR CTD; 182513; -.
DR WormBase; C11E4.2; CE08102; WBGene00007517; gpx-3.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00970000196088; -.
DR HOGENOM; CLU_029507_2_1_1; -.
DR InParanoid; Q95003; -.
DR OMA; GANEHAM; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; Q95003; -.
DR Reactome; R-CEL-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR Reactome; R-CEL-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q95003; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00007517; Expressed in larva and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:WormBase.
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 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 Glycoprotein; Oxidoreductase; Peroxidase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..224
FT /note="Glutathione peroxidase 3"
FT /id="PRO_0000013090"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 224 AA; 25556 MW; F02D055246EDE2F1 CRC64;
MAPGSVLSLA VALATIIGIS CTATVDETMR WKECLNTNQS IFDFQIETLQ GEYTDLSQYR
GKVILLVNVA TFCAYTQQYT DFNPMLEKYQ AQGLTLVAFP CNQFYLQEPA ENHELMNGLT
YVRPGNGWTP HQELHIYGKI DVNGDNHHPL YEFVKESCPQ TVDKIGKTDE LMYNPVRPSD
ITWNFEKFLI DRNGQPRFRF HPTAWSHGDV VTPFIEQLLA EPAN