Sequence Detail

ID/Version

P11352 Q5RJH8 Q9CR54 P12079 Q544W3 (UniProt | EBI)

Last sequence update: 2008-02-26
Last annotation update: 2024-07-24

Sequence description from provider

RecName: Full=Glutathione peroxidase 1 {ECO:0000305}; Short=GPx-1; Short=GSHPx-1; EC=1.11.1.9 {ECO:0000269|PubMed:10754271, ECO:0000269|PubMed:21420488, ECO:0000269|PubMed:36608588, ECO:0000269|PubMed:9126277, ECO:0000269|PubMed:97

Provider

SWISS-PROT

Sequence

Polypeptide 201 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Gpx1	glutathione peroxidase 1	108	123	4	50

Sequence references in MGI

J:8354 Chambers I, et al., The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J. 1986 Jun;5(6):1221-7
J:39714 Esworthy RS, et al., The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver. Arch Biochem Biophys. 1997 Apr 1;340(1):59-63
J:41169 Ho YS, et al., Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J Biol Chem. 1997 Jun 27;272(26):16644-51
J:49644 de Haan JB, et al., Mice with a homozygous null mutation for the most abundant glutathione peroxidase, Gpx1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J Biol Chem. 1998 Aug 28;273(35):22528-36
J:62395 Esposito LA, et al., Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene. Free Radic Biol Med. 2000 Mar 1;28(5):754-66
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563
J:122294 Dikiy A, et al., SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family. Biochemistry. 2007 Jun 12;46(23):6871-82
J:173797 Wang SK, et al., Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein. Free Radic Biol Med. 2011 Jul 1;51(1):197-204
J:196142 Rardin MJ, et al., Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways. Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6
J:203468 Park J, et al., SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol Cell. 2013 Jun 27;50(6):919-30
J:289141 Jedrychowski MP, et al., Facultative protein selenation regulates redox sensitivity, adipose tissue thermogenesis, and obesity. Proc Natl Acad Sci U S A. 2020 May 19;117(20):10789-10796
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89
J:344506 Schwarz M, et al., Side-by-side comparison of recombinant human glutathione peroxidases identifies overlapping substrate specificities for soluble hydroperoxides. Redox Biol. 2023 Feb;59:102593