VKOR1_BOVIN
ID VKOR1_BOVIN Reviewed; 163 AA.
AC Q6B4J2; A2VDX1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Vitamin K epoxide reductase complex subunit 1;
DE EC=1.17.4.4;
DE AltName: Full=Vitamin K1 2,3-epoxide reductase subunit 1;
GN Name=VKORC1;
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].
RA Jin D.-Y., Tie J.-K., Stafford D.W.;
RT "Bovine vitamin K epoxide reductase cDNA.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in vitamin K metabolism. Catalytic subunit of the
CC vitamin K epoxide reductase (VKOR) complex which reduces inactive
CC vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for
CC the gamma-carboxylation of various proteins, including clotting
CC factors, and is required for normal blood coagulation, but also for
CC normal bone development (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + H2O + phylloquinone = 2,3-
CC epoxyphylloquinone + [protein]-dithiol; Xref=Rhea:RHEA:13817,
CC Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15759, ChEBI:CHEBI:18067, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058; EC=1.17.4.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + phylloquinol = [protein]-dithiol +
CC phylloquinone; Xref=Rhea:RHEA:57744, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:18067, ChEBI:CHEBI:28433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058; EC=1.17.4.4;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The number of transmembrane domains and the membrane topology
CC are controversial; supporting evidence is available both for models
CC with three transmembrane domains and four transmembrane domains.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The location of two cysteine active-site residues within
CC a proposed transmembrane is consistent both with the known hydrophobic
CC environment of the thiol redox site of the enzyme and with the
CC lipophilicity of vitamin K and warfarin (coumadin). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VKOR family. {ECO:0000305}.
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DR EMBL; AY682746; AAT85856.1; -; mRNA.
DR EMBL; BC133442; AAI33443.1; -; mRNA.
DR RefSeq; NP_001003903.1; NM_001003903.3.
DR AlphaFoldDB; Q6B4J2; -.
DR SMR; Q6B4J2; -.
DR STRING; 9913.ENSBTAP00000000519; -.
DR BindingDB; Q6B4J2; -.
DR ChEMBL; CHEMBL3212; -.
DR PaxDb; Q6B4J2; -.
DR PRIDE; Q6B4J2; -.
DR Ensembl; ENSBTAT00000000519; ENSBTAP00000000519; ENSBTAG00000000405.
DR GeneID; 445422; -.
DR KEGG; bta:445422; -.
DR CTD; 79001; -.
DR VEuPathDB; HostDB:ENSBTAG00000000405; -.
DR eggNOG; ENOG502S4E7; Eukaryota.
DR GeneTree; ENSGT00940000157421; -.
DR HOGENOM; CLU_105471_0_0_1; -.
DR InParanoid; Q6B4J2; -.
DR OMA; YVINFAL; -.
DR OrthoDB; 1611169at2759; -.
DR TreeFam; TF328467; -.
DR Reactome; R-BTA-6806664; Metabolism of vitamin K.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000000405; Expressed in cortex of kidney and 105 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0047057; F:vitamin-K-epoxide reductase (warfarin-sensitive) activity; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; ISS:UniProtKB.
DR GO; GO:0050820; P:positive regulation of coagulation; IEA:Ensembl.
DR GO; GO:0042373; P:vitamin K metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR CDD; cd12917; VKOR_euk; 1.
DR Gene3D; 1.20.1440.130; -; 1.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR038354; VKOR_sf.
DR InterPro; IPR042406; VKORC1/VKORC1L1.
DR PANTHER; PTHR14519; PTHR14519; 1.
DR Pfam; PF07884; VKOR; 1.
DR SMART; SM00756; VKc; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Membrane; Oxidoreductase; Quinone;
KW Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..163
FT /note="Vitamin K epoxide reductase complex subunit 1"
FT /id="PRO_0000191667"
FT TOPO_DOM 1..8
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DISULFID 132..135
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 163 AA; 17967 MW; 7C8A7A5057908F20 CRC64;
MGATWRSPGW VRLALCLAGL VLSLYALHVK AARARDRDYR ALCDVGTAIS CSRVFSSRWG
RGFGLVEHVL GKDSILNQSN SIFGCIFYTL QLLLGCLQGR WASVLLRLSC LVSLAGSVYL
AWILFFVLYD FCIVCITTYA INVGLTVLSF REVQGPQGKV KGH
