ID U4PB05_CAEEL Unreviewed; 179 AA.
AC U4PB05;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=gpx-2 {ECO:0000313|EMBL:CDH93042.1,
GN ECO:0000313|WormBase:R05H10.5b};
GN ORFNames=CELE_R05H10.5 {ECO:0000313|EMBL:CDH93042.1}, R05H10.5
GN {ECO:0000313|WormBase:R05H10.5b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CDH93042.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CDH93042.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CDH93042.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; BX284602; CDH93042.1; -; Genomic_DNA.
DR RefSeq; NP_001293547.1; NM_001306618.1.
DR AlphaFoldDB; U4PB05; -.
DR SMR; U4PB05; -.
DR EPD; U4PB05; -.
DR PeptideAtlas; U4PB05; -.
DR EnsemblMetazoa; R05H10.5b.1; R05H10.5b.1; WBGene00011045.
DR AGR; WB:WBGene00011045; -.
DR WormBase; R05H10.5b; CE48951; WBGene00011045; gpx-2.
DR GeneTree; ENSGT00940000175241; -.
DR OMA; HMMKDID; -.
DR OrthoDB; 67394at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011045; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; U4PB05; baseline.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF2; GLUTATHIONE PEROXIDASE 2; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Proteomics identification {ECO:0007829|EPD:U4PB05,
KW ECO:0007829|PeptideAtlas:U4PB05};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT ACT_SITE 52
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 179 AA; 19816 MW; 11743520D6D30D6D CRC64;
MLSAARRFIS LSTASAMASV HGITVKNAQG EDTPLSNYQG KVLIIVNVAS QCGLTNSNYN
QFKELLDVYK KDGLEVLAFP CNQFGGQEPS CEIDIAAFVA DKFKFEPTLF QKIDVNGDNT
APLYKFLKQE KGGFLVDAIK WNFTKFLVGR DGHVIKRFSP TTEPKDMKKD IEAALQAKL
//
