GPX1_MOUSE
ID GPX1_MOUSE Reviewed; 201 AA.
AC P11352; P12079; Q544W3; Q5RJH8; Q9CR54;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Glutathione peroxidase 1 {ECO:0000305};
DE Short=GPx-1;
DE Short=GSHPx-1;
DE EC=1.11.1.9 {ECO:0000305|PubMed:9195979};
DE AltName: Full=Cellular glutathione peroxidase;
DE AltName: Full=Selenium-dependent glutathione peroxidase 1;
GN Name=Gpx1 {ECO:0000312|MGI:MGI:104887};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SELENOCYSTEINE AT SEC-47.
RC TISSUE=Erythrocyte;
RX PubMed=3015592; DOI=10.1002/j.1460-2075.1986.tb04350.x;
RA Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., Harrison P.R.;
RT "The structure of the mouse glutathione peroxidase gene: the selenocysteine
RT in the active site is encoded by the 'termination' codon, TGA.";
RL EMBO J. 5:1221-1227(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryonic liver, Kidney, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2771650; DOI=10.1093/nar/17.15.6390;
RA Dunn D.K., Howells D.D., Richardson J., Goldfarb P.S.;
RT "A human cDNA sequence for a novel glutathione peroxidase-related
RT selenopeptide, GPRP.";
RL Nucleic Acids Res. 17:6390-6390(1989).
RN [5]
RP CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9195979; DOI=10.1074/jbc.272.26.16644;
RA Ho Y.S., Magnenat J.L., Bronson R.T., Cao J., Gargano M., Sugawara M.,
RA Funk C.D.;
RT "Mice deficient in cellular glutathione peroxidase develop normally and
RT show no increased sensitivity to hyperoxia.";
RL J. Biol. Chem. 272:16644-16651(1997).
RN [6]
RP INTERACTION WITH MIEN1.
RX PubMed=17503775; DOI=10.1021/bi602462q;
RA Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A.,
RA Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.;
RT "SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the
RT functions of selenoproteins of a novel thioredoxin-like family.";
RL Biochemistry 46:6871-6882(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, SELENOCYSTEINE AT SEC-47, PARTIAL LOSS OF
RP SELENIUM IN ABSENCE OF SOD1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=21420488; DOI=10.1016/j.freeradbiomed.2011.03.018;
RA Wang S.K., Weaver J.D., Zhang S., Lei X.G.;
RT "Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine
RT in murine hepatic GPX1 protein.";
RL Free Radic. Biol. Med. 51:197-204(2011).
RN [10]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112 AND
RP LYS-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112; LYS-119 AND
RP LYS-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Protects the hemoglobin in erythrocytes from oxidative
CC breakdown. In platelets, plays a crucial role of glutathione peroxidase
CC in the arachidonic acid metabolism (PubMed:9195979).
CC {ECO:0000269|PubMed:9195979}.
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:0000305|PubMed:9195979};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC Evidence={ECO:0000305|PubMed:9195979};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2
CC glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC ChEBI:CHEBI:90680; Evidence={ECO:0000269|PubMed:9195979};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC Evidence={ECO:0000305|PubMed:9195979};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for H(2)O(2) (at 25 degrees Celsius, in 0.1 M phosphate
CC buffer, pH 7.0) {ECO:0000269|PubMed:21420488};
CC KM=29 uM for tert-butylperoxide (at 25 degrees Celsius, in 0.1 M
CC phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488};
CC Vmax=319 mM/min/mg enzyme toward H(2)O(2) (at 25 degrees Celsius, in
CC 0.1 M phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488};
CC Vmax=182 mM/min/mg enzyme toward tert-butylperoxide (at 25 degrees
CC Celsius, in 0.1 M phosphate buffer, pH 7.0)
CC {ECO:0000269|PubMed:21420488};
CC -!- SUBUNIT: Homotetramer. Interacts with MIEN1.
CC {ECO:0000269|PubMed:17503775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney and lung.
CC {ECO:0000269|PubMed:9195979}.
CC -!- PTM: During periods of oxidative stress, Sec-47 may react with a
CC superoxide radical, irreversibly lose hydroselenide and be converted to
CC dehydroalanine. {ECO:0000269|PubMed:21420488}.
CC -!- DISRUPTION PHENOTYPE: Mutants are healthy, fertile and show no
CC increased sensitivity to hyperoxia. {ECO:0000269|PubMed:9195979}.
CC -!- MISCELLANEOUS: In the absence of Sod1, Gpx1 in the liver undergoes a
CC 40% reduction in catalytic activity as a result of the decomposition of
CC Sec-47 to dehydroalanine. {ECO:0000305|PubMed:21420488}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:2771650 sequence was originally thought to originate
CC from human. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43535.1; Type=Miscellaneous discrepancy; Note=Number of sequencing artifacts.; Evidence={ECO:0000305};
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DR EMBL; X03920; CAA27558.1; -; Genomic_DNA.
DR EMBL; AK002245; BAC55244.1; -; mRNA.
DR EMBL; AK010999; BAC55252.1; -; mRNA.
DR EMBL; AK011019; BAC55253.1; -; mRNA.
DR EMBL; AK028171; BAC55257.1; -; mRNA.
DR EMBL; AK150548; BAE29650.1; -; mRNA.
DR EMBL; AK154833; BAE32862.1; -; mRNA.
DR EMBL; AK160388; BAE35760.1; -; mRNA.
DR EMBL; BC086649; AAH86649.1; -; mRNA.
DR EMBL; X15667; CAB43535.1; ALT_SEQ; mRNA.
DR CCDS; CCDS23522.1; -.
DR PIR; A25106; OPMSE.
DR PIR; S05317; S05317.
DR RefSeq; NP_001316456.1; NM_001329527.1.
DR RefSeq; NP_001316457.1; NM_001329528.1.
DR RefSeq; NP_032186.2; NM_008160.6.
DR BioGRID; 200037; 8.
DR IntAct; P11352; 4.
DR STRING; 10090.ENSMUSP00000081010; -.
DR SwissLipids; SLP:000001635; -.
DR PeroxiBase; 3709; MmGPx01.
DR iPTMnet; P11352; -.
DR PhosphoSitePlus; P11352; -.
DR SwissPalm; P11352; -.
DR REPRODUCTION-2DPAGE; IPI00319652; -.
DR REPRODUCTION-2DPAGE; P11352; -.
DR SWISS-2DPAGE; P11352; -.
DR CPTAC; non-CPTAC-3983; -.
DR EPD; P11352; -.
DR jPOST; P11352; -.
DR MaxQB; P11352; -.
DR PaxDb; P11352; -.
DR PeptideAtlas; P11352; -.
DR PRIDE; P11352; -.
DR ProteomicsDB; 269627; -.
DR Antibodypedia; 39716; 543 antibodies from 40 providers.
DR DNASU; 14775; -.
DR Ensembl; ENSMUST00000082429; ENSMUSP00000081010; ENSMUSG00000063856.
DR GeneID; 14775; -.
DR KEGG; mmu:14775; -.
DR UCSC; uc009rpf.3; mouse.
DR CTD; 2876; -.
DR MGI; MGI:104887; Gpx1.
DR VEuPathDB; HostDB:ENSMUSG00000063856; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000156150; -.
DR InParanoid; P11352; -.
DR OMA; RDYTEMN; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; P11352; -.
DR TreeFam; TF105318; -.
DR Reactome; R-MMU-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR Reactome; R-MMU-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR SABIO-RK; P11352; -.
DR BioGRID-ORCS; 14775; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Gpx1; mouse.
DR PRO; PR:P11352; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P11352; protein.
DR Bgee; ENSMUSG00000063856; Expressed in fetal liver hematopoietic progenitor cell and 256 other tissues.
DR ExpressionAtlas; P11352; baseline and differential.
DR Genevisible; P11352; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097413; C:Lewy body; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:MGI.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IMP:UniProtKB.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IGI:MGI.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0001885; P:endothelial cell development; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0060047; P:heart contraction; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:MGI.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; IMP:MGI.
DR GO; GO:0051450; P:myoblast proliferation; IMP:MGI.
DR GO; GO:0014902; P:myotube differentiation; IMP:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IGI:MGI.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI.
DR GO; GO:0018158; P:protein oxidation; IMP:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; ISO:MGI.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IGI:MGI.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:MGI.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR GO; GO:0010269; P:response to selenium ion; ISO:MGI.
DR GO; GO:0009609; P:response to symbiotic bacterium; IGI:MGI.
DR GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR GO; GO:0001659; P:temperature homeostasis; IGI:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR GO; GO:0009650; P:UV protection; ISO:MGI.
DR GO; GO:0042311; P:vasodilation; IMP:MGI.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Lipid metabolism; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Reference proteome; Selenocysteine.
FT CHAIN 1..201
FT /note="Glutathione peroxidase 1"
FT /id="PRO_0000066613"
FT ACT_SITE 47
FT SITE 47
FT /note="Subject to oxidation and hydroselenide loss to
FT dehydroalanine"
FT NON_STD 47
FT /note="Selenocysteine"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 62
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 62
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 86
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 112
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 112
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 146
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 146
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
SQ 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
