ID GPX3_PONPY Reviewed; 226 AA. AC Q5RFG3; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 19-OCT-2011, entry version 45. DE RecName: Full=Glutathione peroxidase 3; DE Short=GPx-3; DE Short=GSHPx-3; DE EC=1.11.1.9; DE AltName: Full=Plasma glutathione peroxidase; DE Short=GPx-P; DE Short=GSHPx-P; DE Flags: Precursor; GN Name=GPX3; 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=Kidney; RG The German cDNA consortium; RL Submitted (MAR-2005) 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 + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Secreted in plasma. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB121006; BAE17014.1; -; mRNA. DR EMBL; CR857195; CAH89494.2; -; mRNA. DR UniGene; Pab.18214; -. DR PeroxiBase; 3727; PpyGPx03. DR GeneTree; ENSGT00550000074312; -. DR HOVERGEN; HBG004333; -. DR InParanoid; Q5RFG3; -. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB. DR GO; GO:0008430; F:selenium binding; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_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 SUPFAM; SSF52833; Thiordxn-like_fd; 1. 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 Oxidoreductase; Peroxidase; Secreted; Selenocysteine; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 226 Glutathione peroxidase 3. FT /FTId=PRO_0000042615. FT ACT_SITE 73 73 By similarity. FT NON_STD 73 73 Selenocysteine. SQ SEQUENCE 226 AA; 25562 MW; D7F77A1692493D98 CRC64; MARLLQASCL LSLLLAGFVP QSRGQEKSKM DCHGGISGTI YEYGALTIDG EEYIPFKQYA GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP CNQFGKQEPG ENSEILPTLK YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR WNFEKFLVGP DGIPIMRWHH RTTVSNVKMD ILSYMRRQAA LGVKRK //