ID GPX3_PONPY Reviewed; 226 AA. AC Q5RFG3; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 24-JUL-2007, entry version 23. DE Glutathione peroxidase 3 precursor (EC 1.11.1.9) (GSHPx-3) (GPx-3) DE (Plasma glutathione peroxidase) (GSHPx-P). GN Name=GPX3; OS Pongo pygmaeus (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 PeroxiBase; 3727; PpyGPx03. 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 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 PRINTS; PR01011; GLUTPROXDASE. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. PE 2: Evidence at transcript level; KW Oxidoreductase; Peroxidase; Secreted; Selenium; Selenocysteine; KW 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 SE_CYS 73 73 SQ SEQUENCE 226 AA; 25515 MW; 8C0BF083533F3D8F CRC64; MARLLQASCL LSLLLAGFVP QSRGQEKSKM DCHGGISGTI YEYGALTIDG EEYIPFKQYA GKYVLFVNVA SYCGLTGQYI ELNALQEELA PFGLVILGFP CNQFGKQEPG ENSEILPTLK YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR WNFEKFLVGP DGIPIMRWHH RTTVSNVKMD ILSYMRRQAA LGVKRK //