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Glutathione peroxidase 1 (GPx-1) (GSHPx-1) (EC 1.11.1.9) (Cellular glutathione peroxidase) (Selenium-dependent glutathione peroxidase 1)

 GPX1_MOUSE              Reviewed;         201 AA.
P11352; P12079; Q544W3; Q5RJH8; Q9CR54;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
25-OCT-2017, entry version 177.
RecName: Full=Glutathione peroxidase 1;
Short=GPx-1;
Short=GSHPx-1;
EC=1.11.1.9;
AltName: Full=Cellular glutathione peroxidase;
AltName: Full=Selenium-dependent glutathione peroxidase 1;
Name=Gpx1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SELENOCYSTEINE AT SEC-47.
TISSUE=Erythrocyte;
PubMed=3015592;
Chambers I., Frampton J., Goldfarb P., Affara N., McBain W.,
Harrison P.R.;
"The structure of the mouse glutathione peroxidase gene: the
selenocysteine in the active site is encoded by the 'termination'
codon, TGA.";
EMBO J. 5:1221-1227(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow, Embryonic liver, Kidney, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2771650; DOI=10.1093/nar/17.15.6390;
Dunn D.K., Howells D.D., Richardson J., Goldfarb P.S.;
"A human cDNA sequence for a novel glutathione peroxidase-related
selenopeptide, GPRP.";
Nucleic Acids Res. 17:6390-6390(1989).
[5]
INTERACTION WITH MIEN1.
PubMed=17503775; DOI=10.1021/bi602462q;
Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A.,
Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.;
"SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the
functions of selenoproteins of a novel thioredoxin-like family.";
Biochemistry 46:6871-6882(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
BIOPHYSICOCHEMICAL PROPERTIES, SELENOCYSTEINE AT SEC-47, PARTIAL LOSS
OF SELENIUM IN ABSENCE OF SOD1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Liver;
PubMed=21420488; DOI=10.1016/j.freeradbiomed.2011.03.018;
Wang S.K., Weaver J.D., Zhang S., Lei X.G.;
"Knockout of SOD1 promotes conversion of selenocysteine to
dehydroalanine in murine hepatic GPX1 protein.";
Free Radic. Biol. Med. 51:197-204(2011).
[9]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112 AND
LYS-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112; LYS-119
AND LYS-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Protects the hemoglobin in erythrocytes from oxidative
breakdown.
-!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
disulfide + 2 H(2)O.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 uM for H(2)O(2) (at 25 degrees Celsius, in 0.1 M phosphate
buffer, pH 7.0) {ECO:0000269|PubMed:21420488};
KM=29 uM for tert-butylperoxide (at 25 degrees Celsius, in 0.1 M
phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488};
Vmax=319 mM/min/mg enzyme toward H(2)O(2) (at 25 degrees
Celsius, in 0.1 M phosphate buffer, pH 7.0)
{ECO:0000269|PubMed:21420488};
Vmax=182 mM/min/mg enzyme toward tert-butylperoxide (at 25
degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)
{ECO:0000269|PubMed:21420488};
-!- SUBUNIT: Homotetramer. Interacts with MIEN1.
{ECO:0000269|PubMed:17503775}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: During periods of oxidative stress, Sec-47 may react with a
superoxide radical, irreversibly lose hydroselenide and be
converted to dehydroalanine. {ECO:0000269|PubMed:21420488}.
-!- MISCELLANEOUS: In the absence of Sod1, Gpx1 in the liver undergoes
a 40% reduction in catalytic activity as a result of the
decomposition of Sec-47 to dehydroalanine.
{ECO:0000305|PubMed:21420488}.
-!- SIMILARITY: Belongs to the glutathione peroxidase family.
{ECO:0000305}.
-!- CAUTION: PubMed:2771650 sequence was originally thought to
originate from human. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB43535.1; Type=Miscellaneous discrepancy; Note=Number of sequencing artifacts.; Evidence={ECO:0000305};
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EMBL; X03920; CAA27558.1; -; Genomic_DNA.
EMBL; AK002245; BAC55244.1; -; mRNA.
EMBL; AK010999; BAC55252.1; -; mRNA.
EMBL; AK011019; BAC55253.1; -; mRNA.
EMBL; AK028171; BAC55257.1; -; mRNA.
EMBL; AK150548; BAE29650.1; -; mRNA.
EMBL; AK154833; BAE32862.1; -; mRNA.
EMBL; AK160388; BAE35760.1; -; mRNA.
EMBL; BC086649; AAH86649.1; -; mRNA.
EMBL; X15667; CAB43535.1; ALT_SEQ; mRNA.
CCDS; CCDS23522.1; -.
PIR; A25106; OPMSE.
PIR; S05317; S05317.
RefSeq; NP_001316456.1; NM_001329527.1.
RefSeq; NP_001316457.1; NM_001329528.1.
RefSeq; NP_032186.2; NM_008160.6.
UniGene; Mm.1090; -.
ProteinModelPortal; P11352; -.
BioGrid; 200037; 2.
IntAct; P11352; 8.
MINT; MINT-1855025; -.
STRING; 10090.ENSMUSP00000081010; -.
SwissLipids; SLP:000001635; -.
PeroxiBase; 3709; MmGPx01.
iPTMnet; P11352; -.
PhosphoSitePlus; P11352; -.
SwissPalm; P11352; -.
REPRODUCTION-2DPAGE; IPI00319652; -.
REPRODUCTION-2DPAGE; P11352; -.
SWISS-2DPAGE; P11352; -.
EPD; P11352; -.
MaxQB; P11352; -.
PaxDb; P11352; -.
PeptideAtlas; P11352; -.
PRIDE; P11352; -.
Ensembl; ENSMUST00000082429; ENSMUSP00000081010; ENSMUSG00000063856.
GeneID; 14775; -.
KEGG; mmu:14775; -.
UCSC; uc009rpf.3; mouse.
CTD; 2876; -.
MGI; MGI:104887; Gpx1.
eggNOG; KOG1651; Eukaryota.
eggNOG; COG0386; LUCA.
GeneTree; ENSGT00760000119230; -.
HOGENOM; HOG000277055; -.
HOVERGEN; HBG004333; -.
InParanoid; P11352; -.
KO; K00432; -.
OMA; VDRYYPT; -.
OrthoDB; EOG091G10LN; -.
PhylomeDB; P11352; -.
TreeFam; TF105318; -.
Reactome; R-MMU-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-MMU-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-MMU-74259; Purine catabolism.
SABIO-RK; P11352; -.
ChiTaRS; Gpx1; mouse.
PRO; PR:P11352; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000063856; -.
CleanEx; MM_GPX1; -.
ExpressionAtlas; P11352; baseline and differential.
Genevisible; P11352; MM.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0097413; C:Lewy body; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:MGI.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0045454; P:cell redox homeostasis; ISO:MGI.
GO; GO:0001885; P:endothelial cell development; IMP:MGI.
GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
GO; GO:0060047; P:heart contraction; IMP:MGI.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:MGI.
GO; GO:0051702; P:interaction with symbiont; IGI:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
GO; GO:0051450; P:myoblast proliferation; IMP:MGI.
GO; GO:0014902; P:myotube differentiation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IGI:MGI.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0018158; P:protein oxidation; IMP:MGI.
GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; ISO:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:MGI.
GO; GO:0010332; P:response to gamma radiation; IGI:MGI.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
GO; GO:0033194; P:response to hydroperoxide; IMP:MGI.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
GO; GO:0010269; P:response to selenium ion; ISO:MGI.
GO; GO:0009609; P:response to symbiotic bacterium; IGI:MGI.
GO; GO:0009636; P:response to toxic substance; IMP:MGI.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
GO; GO:0001659; P:temperature homeostasis; IGI:MGI.
GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
GO; GO:0009650; P:UV protection; ISO:MGI.
GO; GO:0042311; P:vasodilation; IMP:MGI.
CDD; cd00340; GSH_Peroxidase; 1.
InterPro; IPR000889; Glutathione_peroxidase.
InterPro; IPR029759; GPX_AS.
InterPro; IPR029760; GPX_CS.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR11592; PTHR11592; 1.
Pfam; PF00255; GSHPx; 1.
PIRSF; PIRSF000303; Glutathion_perox; 1.
PRINTS; PR01011; GLUTPROXDASE.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase;
Phosphoprotein; Reference proteome; Selenocysteine.
CHAIN 1 201 Glutathione peroxidase 1.
/FTId=PRO_0000066613.
ACT_SITE 47 47
SITE 47 47 Subject to oxidation and hydroselenide
loss to dehydroalanine.
NON_STD 47 47 Selenocysteine.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000250|UniProtKB:P04041}.
MOD_RES 62 62 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 62 62 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 86 86 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 86 86 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 112 112 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 112 112 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 119 119 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 146 146 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 146 146 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:P04041}.
SEQUENCE 201 AA; 22329 MW; 401D065165D8AF5C CRC64;
MCAARLSAAA QSTVYAFSAR PLTGGEPVSL GSLRGKVLLI ENVASLUGTT IRDYTEMNDL
QKRLGPRGLV VLGFPCNQFG HQENGKNEEI LNSLKYVRPG GGFEPNFTLF EKCEVNGEKA
HPLFTFLRNA LPTPSDDPTA LMTDPKYIIW SPVCRNDIAW NFEKFLVGPD GVPVRRYSRR
FRTIDIEPDI ETLLSQQSGN S


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