GenomeNet

Database: UniProt
Entry: Q95003
LinkDB: Q95003
Original site: Q95003 
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   11-JUN-2014, entry version 95.
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   Rhabditoidea; Rhabditidae; Peloderinae; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; Z81015; CAB02655.1; -; Genomic_DNA.
DR   PIR; T19190; T19190.
DR   RefSeq; NP_509616.1; NM_077215.4.
DR   UniGene; Cel.33165; -.
DR   ProteinModelPortal; Q95003; -.
DR   SMR; Q95003; 39-200.
DR   STRING; 6239.C11E4.2; -.
DR   PeroxiBase; 3748; CelGPx03.
DR   PaxDb; Q95003; -.
DR   PRIDE; Q95003; -.
DR   EnsemblMetazoa; C11E4.2; C11E4.2; 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; COG0386; -.
DR   GeneTree; ENSGT00740000115371; -.
DR   HOGENOM; HOG000277055; -.
DR   InParanoid; Q95003; -.
DR   KO; K00432; -.
DR   OMA; ACPHPSE; -.
DR   OrthoDB; EOG7KQ23C; -.
DR   PhylomeDB; Q95003; -.
DR   NextBio; 917856; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
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   Complete proteome; Glycoprotein; Oxidoreductase; Peroxidase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    224       Glutathione peroxidase 3.
FT                                /FTId=PRO_0000013090.
FT   ACT_SITE     73     73       By similarity.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
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
//
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