GPX1_RAT
ID GPX1_RAT Reviewed; 201 AA.
AC P04041; O08946; Q4PIY2; Q91WZ5;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Glutathione peroxidase 1 {ECO:0000305};
DE Short=GPx-1;
DE Short=GSHPx-1;
DE EC=1.11.1.9 {ECO:0000250|UniProtKB:P07203};
DE AltName: Full=Cellular glutathione peroxidase;
GN Name=Gpx1 {ECO:0000312|RGD:2729};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3408482; DOI=10.1016/0006-291x(88)90242-2;
RA Yoshimura S., Takekoshi S., Watanabe K., Fujii-Kuriyama Y.;
RT "Determination of nucleotide sequence of cDNA coding rat glutathione
RT peroxidase and diminished expression of the mRNA in selenium deficient rat
RT liver.";
RL Biochem. Biophys. Res. Commun. 154:1024-1028(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3387231; DOI=10.1093/nar/16.11.5207;
RA Ho Y.S., Howard A.J., Crapo J.D.;
RT "Nucleotide sequence of a rat glutathione peroxidase cDNA.";
RL Nucleic Acids Res. 16:5207-5207(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2838821; DOI=10.1093/nar/16.12.5557;
RA Reddy A.P., Hsu B.L., Reddy P.S., Li N.Q., Thyagaraju K., Reddy C.C.,
RA Tam M.F., Tu C.P.D.;
RT "Expression of glutathione peroxidase I gene in selenium-deficient rats.";
RL Nucleic Acids Res. 16:5557-5568(1988).
RN [4]
RP SEQUENCE REVISION TO 47.
RA Reddy A.P., Hsu B.L., Reddy P.S., Li N.Q., Thyagaraju K., Reddy C.C.,
RA Tam M.F., Tu C.P.D.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=1451786; DOI=10.1016/0014-5793(92)80198-p;
RA Ho Y.-S., Howard A.J.;
RT "Cloning and characterization of the rat glutathione peroxidase gene.";
RL FEBS Lett. 301:5-9(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1640255; DOI=10.1093/jn/122.8.1620;
RA Christensen M.J., Burgener K.W.;
RT "Dietary selenium stabilizes glutathione peroxidase mRNA in rat liver.";
RL J. Nutr. 122:1620-1626(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
RC STRAIN=Sprague-Dawley;
RA Suemizu H.;
RT "Functional analysis of the 5'-flanking region of the rat glutathione
RT peroxidase gene.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 7-52, AND SELENOCYSTEINE AT SEC-47.
RC TISSUE=Liver;
RX PubMed=6217842; DOI=10.1016/0167-4838(82)90472-1;
RA Condell R.A., Tappel A.L.;
RT "Amino acid sequence around the active-site selenocysteine of rat liver
RT glutathione peroxidase.";
RL Biochim. Biophys. Acta 709:304-309(1982).
RN [9]
RP PROTEIN SEQUENCE OF 96-112 AND 165-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-195, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000250|UniProtKB:P11352}.
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:P11352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC Evidence={ECO:0000250|UniProtKB:P11352};
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:0000250|UniProtKB:P11352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC Evidence={ECO:0000250|UniProtKB:P11352};
CC -!- SUBUNIT: Homotetramer. Interacts with MIEN1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in liver and lung.
CC {ECO:0000269|PubMed:1451786}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; M21210; AAB95647.2; -; mRNA.
DR EMBL; X07365; CAB43593.1; -; mRNA.
DR EMBL; X12367; CAA30928.2; -; mRNA.
DR EMBL; S50336; AAA12407.2; -; Genomic_DNA.
DR EMBL; S41066; AAK72702.1; -; mRNA.
DR EMBL; AB004231; BAA20399.2; -; Genomic_DNA.
DR PIR; A30793; OPRTE.
DR RefSeq; NP_110453.3; NM_030826.4.
DR BioGRID; 246569; 2.
DR IntAct; P04041; 1.
DR STRING; 10116.ENSRNOP00000066577; -.
DR PeroxiBase; 3730; RnoGPx01.
DR iPTMnet; P04041; -.
DR PhosphoSitePlus; P04041; -.
DR SwissPalm; P04041; -.
DR jPOST; P04041; -.
DR PaxDb; P04041; -.
DR PRIDE; P04041; -.
DR Ensembl; ENSRNOT00000073247; ENSRNOP00000066577; ENSRNOG00000048812.
DR GeneID; 24404; -.
DR KEGG; rno:24404; -.
DR CTD; 2876; -.
DR RGD; 2729; Gpx1.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000156150; -.
DR InParanoid; P04041; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; P04041; -.
DR BRENDA; 1.11.1.9; 5301.
DR Reactome; R-RNO-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR Reactome; R-RNO-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR SABIO-RK; P04041; -.
DR PRO; PR:P04041; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0097413; C:Lewy body; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
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:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; ISO:RGD.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:RGD.
DR GO; GO:0001885; P:endothelial cell development; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:RGD.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:RGD.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0051450; P:myoblast proliferation; ISO:RGD.
DR GO; GO:0014902; P:myotube differentiation; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0018158; P:protein oxidation; ISO:RGD.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:RGD.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; ISO:RGD.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0051593; P:response to folic acid; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0033194; P:response to hydroperoxide; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0000302; P:response to reactive oxygen species; ISO:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0009609; P:response to symbiotic bacterium; ISO:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; ISO:RGD.
DR GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0009650; P:UV protection; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; ISO:RGD.
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; Direct protein sequencing; Lipid metabolism;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW Selenocysteine.
FT CHAIN 1..201
FT /note="Glutathione peroxidase 1"
FT /id="PRO_0000066617"
FT ACT_SITE 47
FT SITE 47
FT /note="Subject to oxidation and hydroselenide loss to
FT dehydroalanine"
FT /evidence="ECO:0000250"
FT NON_STD 47
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:6217842"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 86
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 112
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 112
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 146
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 146
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07203"
FT CONFLICT 24..25
FT /note="GG -> RE (in Ref. 1; AAB95647)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="C -> S (in Ref. 1; AAB95647)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> T (in Ref. 1; AAB95647)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="P -> S (in Ref. 1; AAB95647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22305 MW; 093528A214615A11 CRC64;
MSAARLSAVA QSTVYAFSAR PLAGGEPVSL GSLRGKVLLI ENVASLUGTT TRDYTEMNDL
QKRLGPRGLV VLGFPCNQFG HQENGKNEEI LNSLKYVRPG GGFEPNFTLF EKCEVNGEKA
HPLFTFLRNA LPAPSDDPTA LMTDPKYIIW SPVCRNDISW NFEKFLVGPD GVPVRRYSRR
FRTIDIEPDI EALLSKQPSN P
