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 23-FEB-2022, entry version 73. DE RecName: Full=Glutathione peroxidase 3 {ECO:0000250|UniProtKB:P22352}; DE Short=GPx-3; DE Short=GSHPx-3; DE EC=1.11.1.9 {ECO:0000250|UniProtKB:P22352}; DE AltName: Full=Plasma glutathione peroxidase; DE Short=GPx-P; DE Short=GSHPx-P; DE Flags: Precursor; GN Name=GPX3 {ECO:0000250|UniProtKB:P22352}; OS Pongo pygmaeus (Bornean orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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. {ECO:0000250|UniProtKB:P22352}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; CC Evidence={ECO:0000250|UniProtKB:P22352}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione CC disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:58297, ChEBI:CHEBI:64090; CC Evidence={ECO:0000250|UniProtKB:P22352}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Secreted in plasma. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC {ECO:0000305}. 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:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0008430; F:selenium binding; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR CDD; cd00340; GSH_Peroxidase; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR029759; GPX_AS. DR InterPro; IPR029760; GPX_CS. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 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 FT /evidence="ECO:0000255" FT CHAIN 25..226 FT /note="Glutathione peroxidase 3" FT /id="PRO_0000042615" FT ACT_SITE 73 FT /evidence="ECO:0000250" FT NON_STD 73 FT /note="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 //