ID   GPX2_CAEEL              Reviewed;         163 AA.
AC   O62327;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Glutathione peroxidase 2;
DE            EC=1.11.1.9;
GN   Name=gpx-2; ORFNames=R05H10.5;
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; Z83119; CAB05581.1; -; Genomic_DNA.
DR   PIR; T23936; T23936.
DR   RefSeq; NP_497078.1; NM_064677.4.
DR   AlphaFoldDB; O62327; -.
DR   SMR; O62327; -.
DR   BioGRID; 52317; 1.
DR   STRING; 6239.R05H10.5b.1; -.
DR   PeroxiBase; 3747; CelGPx02.
DR   EPD; O62327; -.
DR   PaxDb; O62327; -.
DR   PeptideAtlas; O62327; -.
DR   EnsemblMetazoa; R05H10.5a.1; R05H10.5a.1; WBGene00011045.
DR   UCSC; R05H10.5; c. elegans.
DR   WormBase; R05H10.5a; CE18107; WBGene00011045; gpx-2.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_0_1_1; -.
DR   InParanoid; O62327; -.
DR   PhylomeDB; O62327; -.
DR   PRO; PR:O62327; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011045; Expressed in larva and 3 other tissues.
DR   ExpressionAtlas; O62327; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
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   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 2"
FT                   /id="PRO_0000066647"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   163 AA;  18152 MW;  8D5FE6DF96D212CA CRC64;
     MASVHGITVK NAQGEDTPLS NYQGKVLIIV NVASQCGLTN SNYNQFKELL DVYKKDGLEV
     LAFPCNQFGG QEPSCEIDIA AFVADKFKFE PTLFQKIDVN GDNTAPLYKF LKQEKGGFLV
     DAIKWNFTKF LVGRDGHVIK RFSPTTEPKD MKKDIEAALQ AKL