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   16-JUN-2009, entry version 54.
DE   RecName: Full=Probable glutathione peroxidase R05H10.5;
DE            EC=1.11.1.9;
GN   ORFNames=R05H10.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: May constitute a glutathionine peroxidase-like
CC       protective system against oxidative stresses (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; Z83119; CAB05581.1; -; Genomic_DNA.
DR   PIR; T23936; T23936.
DR   RefSeq; NP_497078.1; -.
DR   UniGene; Cel.14641; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 3747; CelGPx02.
DR   Ensembl; R05H10.5; Caenorhabditis elegans.
DR   GeneID; 187630; -.
DR   KEGG; cel:R05H10.5; -.
DR   NMPDR; fig|6239.3.peg.8304; -.
DR   WormBase; WBGene00011045; R05H10.5.
DR   WormPep; R05H10.5; CE18107.
DR   OMA; O62327; SIKWNFS.
DR   BRENDA; 1.11.1.9; 672.
DR   NextBio; 935924; -.
DR   ArrayExpress; O62327; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
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   Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase.
FT   CHAIN         1    163       Probable glutathione peroxidase R05H10.5.
FT                                /FTId=PRO_0000066647.
FT   ACT_SITE     36     36       By similarity.
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
//