GPX1_HUMAN
ID GPX1_HUMAN Reviewed; 203 AA.
AC P07203; E9PAS1; Q7Z5H1; Q9BW12;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Glutathione peroxidase 1 {ECO:0000305};
DE Short=GPx-1 {ECO:0000303|PubMed:11115402};
DE Short=GSHPx-1;
DE EC=1.11.1.9 {ECO:0000305|PubMed:11115402};
DE AltName: Full=Cellular glutathione peroxidase;
GN Name=GPX1 {ECO:0000312|HGNC:HGNC:4553};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 7-ALA-ALA-8 DEL.
RX PubMed=3658677; DOI=10.1093/nar/15.17.7178;
RA Sukenaga Y., Ishida K., Takeda T., Takagi K.;
RT "cDNA sequence coding for human glutathione peroxidase.";
RL Nucleic Acids Res. 15:7178-7178(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT 7-ALA-ALA-8 DEL.
RX PubMed=3697069; DOI=10.1093/nar/15.23.10051;
RA Ishida K., Morino T., Takagi K., Sukenaga Y.;
RT "Nucleotide sequence of a human gene for glutathione peroxidase.";
RL Nucleic Acids Res. 15:10051-10051(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 7-ALA-ALA-8 DEL.
RC TISSUE=Kidney;
RX PubMed=2955287; DOI=10.1093/nar/15.13.5484;
RA Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Hallewell R.A.;
RT "Sequence of a cDNA coding for human glutathione peroxidase confirms TGA
RT encodes active site selenocysteine.";
RL Nucleic Acids Res. 15:5484-5484(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 7-ALA-ALA-8 DEL.
RX PubMed=2307470; DOI=10.1016/0888-7543(90)90566-d;
RA Chada S., le Beau M.M., Casey L., Newburger P.E.;
RT "Isolation and chromosomal localization of the human glutathione peroxidase
RT gene.";
RL Genomics 6:268-271(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ALA-8 DEL.
RX PubMed=1556108; DOI=10.1016/s0021-9258(18)42647-6;
RA Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.;
RT "Structure and function of the 5'-flanking sequence of the human cytosolic
RT selenium-dependent glutathione peroxidase gene (hgpx1).";
RL J. Biol. Chem. 267:5949-5958(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS PRO-5; THR-194
RP AND LEU-200.
RG NIEHS SNPs program;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=11115402;
RA Sutherland M., Shankaranarayanan P., Schewe T., Nigam S.;
RT "Evidence for the presence of phospholipid hydroperoxide glutathione
RT peroxidase in human platelets: implications for its involvement in the
RT regulatory network of the 12-lipoxygenase pathway of arachidonic acid
RT metabolism.";
RL Biochem. J. 353:91-100(2001).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 14-198.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the selenocysteine to glycine mutant of human
RT glutathione peroxidase 1.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [14]
RP VARIANT LEU-200.
RX PubMed=10220143;
RX DOI=10.1002/(sici)1098-1004(1999)13:4<294::aid-humu6>3.0.co;2-5;
RA Forsberg L., de Faire U., Morgenstern R.;
RT "Low yield of polymorphisms from EST blast searching: analysis of genes
RT related to oxidative stress and verification of the P197L polymorphism in
RT GPX1.";
RL Hum. Mutat. 13:294-300(1999).
RN [15]
RP VARIANTS ALA-8 DEL AND 7-ALA-ALA-8 DEL.
RX PubMed=12496980; DOI=10.1038/sj.pcan.4500569;
RA Kote-Jarai Z., Durocher F., Edwards S.M., Hamoudi R., Jackson R.A.,
RA Ardern-Jones A., Murkin A., Dearnaley D.P., Kirby R., Houlston R.,
RA Easton D.F., Eeles R.;
RT "Association between the GCG polymorphism of the selenium dependent GPX1
RT gene and the risk of young onset prostate cancer.";
RL Prostate Cancer Prostatic Dis. 5:189-192(2002).
RN [16]
RP VARIANTS ALA-8 DEL AND LEU-200.
RX PubMed=15331559; DOI=10.2337/diabetes.53.9.2455;
RA Hamanishi T., Furuta H., Kato H., Doi A., Tamai M., Shimomura H.,
RA Sakagashira S., Nishi M., Sasaki H., Sanke T., Nanjo K.;
RT "Functional variants in the glutathione peroxidase-1 (GPx-1) gene are
RT associated with increased intima-media thickness of carotid arteries and
RT risk of macrovascular diseases in Japanese type 2 diabetic patients.";
RL Diabetes 53:2455-2460(2004).
RN [17]
RP VARIANT LEU-200.
RX PubMed=15247771; DOI=10.1097/01.ju.0000130942.40597.9d;
RA Ichimura Y., Habuchi T., Tsuchiya N., Wang L., Oyama C., Sato K.,
RA Nishiyama H., Ogawa O., Kato T.;
RT "Increased risk of bladder cancer associated with a glutathione peroxidase
RT 1 codon 198 variant.";
RL J. Urol. 172:728-732(2004).
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:11115402).
CC {ECO:0000269|PubMed:11115402}.
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:11115402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC Evidence={ECO:0000305|PubMed:11115402};
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:11115402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC Evidence={ECO:0000305|PubMed:11115402};
CC -!- SUBUNIT: Homotetramer. Interacts with MIEN1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07203-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07203-2; Sequence=VSP_047369, VSP_047370;
CC -!- TISSUE SPECIFICITY: Expressed in platelets (at protein level).
CC {ECO:0000269|PubMed:11115402}.
CC -!- PTM: During periods of oxidative stress, Sec-49 may react with a
CC superoxide radical, irreversibly lose hydroselenide and be converted to
CC dehydroalanine. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gpx1/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Glutathione peroxidase entry;
CC URL="https://en.wikipedia.org/wiki/Glutathione_peroxidase";
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DR EMBL; Y00433; CAA68491.1; -; mRNA.
DR EMBL; Y00483; CAB37833.1; -; Genomic_DNA.
DR EMBL; X13709; CAA31992.1; -; mRNA.
DR EMBL; X13710; CAA31993.1; -; mRNA.
DR EMBL; M21304; AAA75389.2; -; mRNA.
DR EMBL; M83094; AAA67540.2; -; Genomic_DNA.
DR EMBL; AY327818; AAP80181.1; -; Genomic_DNA.
DR EMBL; AC121247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000742; AAH00742.3; -; mRNA.
DR CCDS; CCDS43091.1; -. [P07203-1]
DR CCDS; CCDS54582.1; -. [P07203-2]
DR PIR; A42152; OPHUE.
DR RefSeq; NP_000572.2; NM_000581.3. [P07203-1]
DR PDB; 2F8A; X-ray; 1.50 A; A/B=14-198.
DR PDBsum; 2F8A; -.
DR SMR; P07203; -.
DR BioGRID; 109134; 101.
DR CORUM; P07203; -.
DR IntAct; P07203; 18.
DR MINT; P07203; -.
DR STRING; 9606.ENSP00000407375; -.
DR BindingDB; P07203; -.
DR ChEMBL; CHEMBL2163186; -.
DR DrugBank; DB09096; Benzoyl peroxide.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR DrugBank; DB11091; Hydrogen peroxide.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB09221; Polaprezinc.
DR DrugBank; DB11127; Selenious acid.
DR DrugBank; DB11590; Thimerosal.
DR SwissLipids; SLP:000001632; -.
DR PeroxiBase; 3600; HsGPx01-A.
DR GlyGen; P07203; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07203; -.
DR MetOSite; P07203; -.
DR PhosphoSitePlus; P07203; -.
DR SwissPalm; P07203; -.
DR BioMuta; GPX1; -.
DR DMDM; 311033481; -.
DR OGP; P07203; -.
DR SWISS-2DPAGE; P07203; -.
DR EPD; P07203; -.
DR jPOST; P07203; -.
DR MassIVE; P07203; -.
DR PaxDb; P07203; -.
DR PeptideAtlas; P07203; -.
DR PRIDE; P07203; -.
DR ProteomicsDB; 19069; -.
DR ProteomicsDB; 51972; -. [P07203-1]
DR Antibodypedia; 39716; 543 antibodies from 40 providers.
DR DNASU; 2876; -.
DR Ensembl; ENST00000419349.2; ENSP00000391316.1; ENSG00000233276.8. [P07203-2]
DR Ensembl; ENST00000419783.3; ENSP00000407375.1; ENSG00000233276.8. [P07203-1]
DR GeneID; 2876; -.
DR KEGG; hsa:2876; -.
DR MANE-Select; ENST00000419783.3; ENSP00000407375.1; NM_000581.4; NP_000572.2.
DR UCSC; uc021wxw.2; human. [P07203-1]
DR CTD; 2876; -.
DR DisGeNET; 2876; -.
DR GeneCards; GPX1; -.
DR HGNC; HGNC:4553; GPX1.
DR HPA; ENSG00000233276; Low tissue specificity.
DR MalaCards; GPX1; -.
DR MIM; 138320; gene+phenotype.
DR neXtProt; NX_P07203; -.
DR OpenTargets; ENSG00000233276; -.
DR PharmGKB; PA28949; -.
DR VEuPathDB; HostDB:ENSG00000233276; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000156150; -.
DR HOGENOM; CLU_029507_2_0_1; -.
DR InParanoid; P07203; -.
DR OMA; RDYTEMN; -.
DR PhylomeDB; P07203; -.
DR TreeFam; TF105318; -.
DR BioCyc; MetaCyc:HS00019-MON; -.
DR BRENDA; 1.11.1.9; 2681.
DR PathwayCommons; P07203; -.
DR Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids.
DR Reactome; R-HSA-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR SignaLink; P07203; -.
DR SIGNOR; P07203; -.
DR BioGRID-ORCS; 2876; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; GPX1; human.
DR EvolutionaryTrace; P07203; -.
DR GeneWiki; GPX1; -.
DR GenomeRNAi; 2876; -.
DR Pharos; P07203; Tbio.
DR PRO; PR:P07203; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P07203; protein.
DR Bgee; ENSG00000233276; Expressed in monocyte and 94 other tissues.
DR ExpressionAtlas; P07203; baseline and differential.
DR Genevisible; P07203; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:BHF-UCL.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; NAS:ParkinsonsUK-UCL.
DR GO; GO:0001885; P:endothelial cell development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:BHF-UCL.
DR GO; GO:0060047; P:heart contraction; IMP:BHF-UCL.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
DR GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:BHF-UCL.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:1902905; P:positive regulation of supramolecular fiber organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0018158; P:protein oxidation; IEA:Ensembl.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IDA:BHF-UCL.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:BHF-UCL.
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; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:BHF-UCL.
DR GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0010269; P:response to selenium ion; IMP:BHF-UCL.
DR GO; GO:0009609; P:response to symbiotic bacterium; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR GO; GO:0009650; P:UV protection; IMP:BHF-UCL.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Lipid metabolism; Oxidoreductase; Peroxidase; Phosphoprotein;
KW Reference proteome; Selenocysteine.
FT CHAIN 1..203
FT /note="Glutathione peroxidase 1"
FT /id="PRO_0000066610"
FT ACT_SITE 49
FT SITE 49
FT /note="Subject to oxidation and hydroselenide loss to
FT dehydroalanine"
FT /evidence="ECO:0000250"
FT NON_STD 49
FT /note="Selenocysteine"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 114
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 114
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 148
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 148
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 85..98
FT /note="ENAKNEEILNSLKY -> VRRAERGGAGADVQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047369"
FT VAR_SEQ 99..203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047370"
FT VARIANT 5
FT /note="R -> P (in dbSNP:rs8179169)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_020912"
FT VARIANT 7..8
FT /note="Missing (in dbSNP:rs17838762)"
FT /evidence="ECO:0000269|PubMed:12496980,
FT ECO:0000269|PubMed:2307470, ECO:0000269|PubMed:2955287,
FT ECO:0000269|PubMed:3658677, ECO:0000269|PubMed:3697069"
FT /id="VAR_020913"
FT VARIANT 8
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:12496980,
FT ECO:0000269|PubMed:15331559, ECO:0000269|PubMed:1556108"
FT /id="VAR_020914"
FT VARIANT 194
FT /note="A -> T (in dbSNP:rs6446261)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_020915"
FT VARIANT 200
FT /note="P -> L (in dbSNP:rs1050450)"
FT /evidence="ECO:0000269|PubMed:10220143,
FT ECO:0000269|PubMed:15247771, ECO:0000269|PubMed:15331559,
FT ECO:0000269|Ref.6"
FT /id="VAR_007904"
FT CONFLICT 93
FT /note="L -> Q (in Ref. 3; CAA31992)"
FT /evidence="ECO:0000305"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:2F8A"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:2F8A"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2F8A"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2F8A"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:2F8A"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2F8A"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2F8A"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2F8A"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:2F8A"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:2F8A"
SQ SEQUENCE 203 AA; 22088 MW; 5DB11579C66FE8E5 CRC64;
MCAARLAAAA AAAQSVYAFS ARPLAGGEPV SLGSLRGKVL LIENVASLUG TTVRDYTQMN
ELQRRLGPRG LVVLGFPCNQ FGHQENAKNE EILNSLKYVR PGGGFEPNFM LFEKCEVNGA
GAHPLFAFLR EALPAPSDDA TALMTDPKLI TWSPVCRNDV AWNFEKFLVG PDGVPLRRYS
RRFQTIDIEP DIEALLSQGP SCA
