ID GPX1_PIG Reviewed; 206 AA. AC Q8MJ14; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 25-NOV-2008, entry version 41. DE RecName: Full=Glutathione peroxidase 1; DE EC=1.11.1.9; DE AltName: Full=GSHPx-1; DE Short=GPx-1; DE AltName: Full=Cellular glutathione peroxidase; GN Name=GPX1; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hostetler C.E., Robison M.R., Kincaid R.L., Ott T.L.; RT "Sus scrofa selenium-containing enzyme cytosolic glutathione RT peroxidase 1 (cGPX1) from the day 13 embryo."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protects the hemoglobin in erythrocytes from oxidative CC breakdown (By similarity). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF532927; AAM94630.1; -; mRNA. DR RefSeq; NP_999366.1; -. DR UniGene; Ssc.6352; -. DR SMR; Q8MJ14; 17-200. DR PeroxiBase; 3722; SscGPx01. DR GeneID; 397403; -. DR KEGG; ssc:397403; -. DR HOVERGEN; Q8MJ14; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro. 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; Glut_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 Acetylation; Cytoplasm; Oxidoreductase; Peroxidase; Selenium; KW Selenocysteine. FT CHAIN 1 206 Glutathione peroxidase 1. FT /FTId=PRO_0000066614. FT ACT_SITE 52 52 By similarity. FT NON_STD 52 52 Selenocysteine. FT MOD_RES 151 151 N6-acetyllysine (By similarity). SQ SEQUENCE 206 AA; 22591 MW; 4431BECD35A797A0 CRC64; MCAAQRSAAA LAAVAPRSVY AFSARPLAGG EPISLGSLRG KVLLIENVAS LUGTTVRDYT QMNELQRRLG PRGLVVLGFP CNQFGHQENA KNGEILNCLK YVRPGGGFEP NFMLFEKCEV NGANAHPLFA FLREALPTPS DDATALMTDP KFITWSPVCR NDIAWNFEKF LVGPDGVPLR RYSRRFLTID IEPDIEALLS QEPSSA //