GPX1_BOVIN
ID GPX1_BOVIN Reviewed; 205 AA.
AC P00435; A6QPG3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 157.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=2976939; DOI=10.1093/protein/2.3.239;
RA Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Tainer J.A.,
RA Hallewell R.A.;
RT "Selenocysteine's mechanism of incorporation and evolution revealed in
RT cDNAs of three glutathione peroxidases.";
RL Protein Eng. 2:239-246(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 8-205.
RC TISSUE=Erythrocyte;
RX PubMed=6714945; DOI=10.1515/bchm2.1984.365.1.195;
RA Gunzler W.A., Steffens G.J., Grossmann A., Kim S.-M.A., Otting F.,
RA Wendel A., Flohe L.;
RT "The amino-acid sequence of bovine glutathione peroxidase.";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:195-212(1984).
RN [4]
RP GLYCATION AT LYS-117, AND LACK OF GLYCATION AT LYS-41; LYS-91; LYS-100;
RP LYS-124; LYS-151; LYS-169.
RX PubMed=7873592; DOI=10.1016/0167-4838(94)00202-r;
RA Baldwin J.S., Lee L., Leung T.K., Muruganandam A., Mutus B.;
RT "Identification of the site of non-enzymatic glycation of glutathione
RT peroxidase: rationalization of the glycation-related catalytic alterations
RT on the basis of three-dimensional protein structure.";
RL Biochim. Biophys. Acta 1247:60-64(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=6852035; DOI=10.1111/j.1432-1033.1983.tb07429.x;
RA Epp O., Ladenstein R., Wendel A.;
RT "The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm
RT resolution.";
RL Eur. J. Biochem. 133:51-69(1983).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: During periods of oxidative stress, Sec-52 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; X13684; CAB40806.1; -; mRNA.
DR EMBL; BC149308; AAI49309.1; -; mRNA.
DR PIR; S04872; OPBOE.
DR RefSeq; NP_776501.1; NM_174076.3.
DR PDB; 1GP1; X-ray; 2.00 A; A/B=8-205.
DR PDBsum; 1GP1; -.
DR SMR; P00435; -.
DR BioGRID; 158568; 2.
DR PeroxiBase; 3635; BtGPx01.
DR CarbonylDB; P00435; -.
DR PeptideAtlas; P00435; -.
DR PRIDE; P00435; -.
DR Ensembl; ENSBTAT00000080370; ENSBTAP00000061122; ENSBTAG00000054195.
DR GeneID; 281209; -.
DR KEGG; bta:281209; -.
DR CTD; 2876; -.
DR VEuPathDB; HostDB:ENSBTAG00000054195; -.
DR VGNC; VGNC:109407; GPX1.
DR GeneTree; ENSGT00940000156150; -.
DR InParanoid; P00435; -.
DR OMA; RDYTEMN; -.
DR OrthoDB; 1483113at2759; -.
DR BRENDA; 1.11.1.9; 908.
DR EvolutionaryTrace; P00435; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000054195; Expressed in granulosa cell and 107 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097413; C:Lewy body; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:ParkinsonsUK-UCL.
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; IEA:Ensembl.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS: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; IEA:Ensembl.
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:ParkinsonsUK-UCL.
DR GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
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; IEA:Ensembl.
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; IDA:ParkinsonsUK-UCL.
DR GO; GO:0018158; P:protein oxidation; IEA:Ensembl.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IEA:Ensembl.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
DR GO; GO:0010269; P:response to selenium ion; IBA:GO_Central.
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; IEA:Ensembl.
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; Cytoplasm; Direct protein sequencing; Glycation;
KW Glycoprotein; Lipid metabolism; Oxidoreductase; Peroxidase; Phosphoprotein;
KW Reference proteome; Selenocysteine.
FT CHAIN 1..205
FT /note="Glutathione peroxidase 1"
FT /id="PRO_0000066608"
FT ACT_SITE 52
FT SITE 41
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7873592"
FT SITE 52
FT /note="Subject to oxidation and hydroselenide loss to
FT dehydroalanine"
FT /evidence="ECO:0000250"
FT SITE 91
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7873592"
FT SITE 100
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7873592"
FT SITE 124
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7873592"
FT SITE 151
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7873592"
FT SITE 169
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7873592"
FT NON_STD 52
FT /note="Selenocysteine"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 91
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 91
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 151
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 151
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07203"
FT CARBOHYD 117
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:7873592"
FT CONFLICT 96
FT /note="L -> P (in Ref. 2; AAI49309)"
FT /evidence="ECO:0000305"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1GP1"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1GP1"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1GP1"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:1GP1"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1GP1"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1GP1"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1GP1"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1GP1"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1GP1"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:1GP1"
SQ SEQUENCE 205 AA; 22659 MW; 7CBDF736CAAA92F6 CRC64;
MCAAQRSAAA LAAAAPRTVY AFSARPLAGG EPFNLSSLRG KVLLIENVAS LUGTTVRDYT
QMNDLQRRLG PRGLVVLGFP CNQFGHQENA KNEEILNCLK YVRPGGGFEP NFMLFEKCEV
NGEKAHPLFA FLREVLPTPS DDATALMTDP KFITWSPVCR NDVSWNFEKF LVGPDGVPVR
RYSRRFLTID IEPDIETLLS QGASA
