ID GPX2_PONPY Reviewed; 190 AA. AC Q4AEI0; Q5RDD1; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 16-JUN-2009, entry version 28. 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 Pongo pygmaeus (Bornean orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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. CC -!- SEQUENCE CAUTION: CC Sequence=CAH90226.1; Type=Erroneous termination; Positions=40; Note=Translated as Sec; CC Sequence=CAH90226.1; Type=Frameshift; Positions=183; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB121001; BAE17010.1; -; mRNA. DR EMBL; CR857983; CAH90226.1; ALT_SEQ; mRNA. DR UniGene; Pab.11118; -. DR SMR; Q4AEI0; 4-187. DR PeroxiBase; 3726; PpyGPx02. DR HOVERGEN; Q4AEI0; -. DR BRENDA; 1.11.1.9; 269192. 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_0000066623. FT ACT_SITE 40 40 By similarity. FT NON_STD 40 40 Selenocysteine. SQ SEQUENCE 190 AA; 21984 MW; 48904FB5D91F5FA1 CRC64; MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL NELQCRFPRR LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGSGYQPTFT LVQKCEVNGQ NEHPVFAYLK DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP DIKRLLKVAI //