ID   GPX2_HYLLA              Reviewed;         190 AA.
AC   Q4AEH9;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Glutathione peroxidase 2;
DE            EC=1.11.1.9;
DE   AltName: Full=GSHPx-2;
DE            Short=GPx-2;
DE   AltName: Full=Glutathione peroxidase-gastrointestinal;
DE   AltName: Full=GSHPx-GI;
GN   Name=GPX2;
OS   Hylobates lar (Common gibbon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hylobatidae; Hylobates.
OX   NCBI_TaxID=9580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15967696; DOI=10.1016/j.cbpc.2005.05.002;
RA   Fukuhara R., Kageyama T.;
RT   "Structure, gene expression, and evolution of primate glutathione
RT   peroxidases.";
RL   Comp. Biochem. Physiol. 141B:428-436(2005).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; AB121002; BAE17011.1; -; mRNA.
DR   SMR; Q4AEH9; 4-187.
DR   PeroxiBase; 3697; HlGPx02.
DR   HOVERGEN; Q4AEH9; -.
DR   BRENDA; 1.11.1.9; 285274.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EC.
DR   GO; GO:0008430; F:selenium binding; IEA:UniProtKB-KW.
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   Cytoplasm; Oxidoreductase; Peroxidase; Selenium; Selenocysteine.
FT   CHAIN         1    190       Glutathione peroxidase 2.
FT                                /FTId=PRO_0000066620.
FT   ACT_SITE     40     40       By similarity.
FT   NON_STD      40     40       Selenocysteine.
SQ   SEQUENCE   190 AA;  21954 MW;  FC8C4E69C4DE83A0 CRC64;
     MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL NELQCRFPRR
     LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK
     DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP
     DIKRLLKVAI
//