ID GPX4_GOSHI Reviewed; 170 AA. AC O49069; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 54. DE RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase; DE Short=PHGPx; DE EC=1.11.1.12; OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Malvales; Malvaceae; Malvoideae; Gossypium. OX NCBI_TaxID=3635; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Coker 312; RA Jaradat T.T., Allen R.; RT "Glutathione peroxidase from cotton, partial cDNA."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protects cells and enzymes from oxidative damage, by CC catalyzing the reduction of hydrogen peroxide, lipid peroxides and CC organic hydroperoxide, by glutathione (By similarity). CC -!- CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = CC glutathione disulfide + lipid + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). 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; AF037051; AAB94892.1; -; mRNA. DR HSSP; P00435; 1GP1. DR PeroxiBase; 2648; GhGPx06-1. DR BRENDA; 1.11.1.12; 1857. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro. DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione pero...; 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 Cytoplasm; Oxidoreductase; Peroxidase. FT CHAIN 1 170 Probable phospholipid hydroperoxide FT glutathione peroxidase. FT /FTId=PRO_0000066628. FT ACT_SITE 43 43 By similarity. SQ SEQUENCE 170 AA; 18854 MW; 32FE5856B9B40F82 CRC64; MASQSSKPQS IYDFTVKDAK GNDVDLSIYK GKVLIIVNVA SQCGLTNSNY TDLTEIYKKY KDQGLEILAF PCNQFGGQEP GSIEESIQNM VCTRFKAEYP IFDKVDVNGD NAAPLYKFLK SSKGGFFGDS IKWNFSKFLV DKEGNVVDRY SPTTTPASME KDIKKLLGVA //