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Vitamin K epoxide reductase complex subunit 1 (EC 1.17.4.4) (Vitamin K1 2,3-epoxide reductase subunit 1)

 VKOR1_RAT               Reviewed;         161 AA.
Q6TEK4;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
13-FEB-2019, entry version 108.
RecName: Full=Vitamin K epoxide reductase complex subunit 1;
EC=1.17.4.4 {ECO:0000269|PubMed:15640149, ECO:0000269|PubMed:23772386, ECO:0000269|PubMed:23928358};
AltName: Full=Vitamin K1 2,3-epoxide reductase subunit 1;
Name=Vkorc1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=14765194; DOI=10.1038/nature02214;
Rost S., Fregin A., Ivaskevicius V., Conzelmann E., Hoertnagel K.,
Pelz H.-J., Lappegard K., Seifried E., Scharrer I., Tuddenham E.G.D.,
Mueller C.R., Strom T.M., Oldenburg J.;
"Mutations in VKORC1 cause warfarin resistance and multiple
coagulation factor deficiency type 2.";
Nature 427:537-541(2004).
[2]
IDENTIFICATION.
PubMed=14765195; DOI=10.1038/nature02254;
Li T., Chang C.-Y., Jin D.-Y., Lin P.-J., Khvorova A., Stafford D.W.;
"Identification of the gene for vitamin K epoxide reductase.";
Nature 427:541-544(2004).
[3]
MUTAGENESIS OF CYS-132 AND CYS-135, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=15640149; DOI=10.1074/jbc.M413982200;
Wajih N., Sane D.C., Hutson S.M., Wallin R.;
"Engineering of a recombinant vitamin K-dependent (gamma)-
carboxylation system with enhanced (gamma)-carboxyglutamic acid
forming capacity: evidence for a functional CxxC redox center in the
system.";
J. Biol. Chem. 280:10540-10547(2005).
[4]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR
LOCATION, AND CHARACTERIZATION OF VARIANTS GLN-120; GLN-128; CYS-139;
PHE-139 AND SER-139.
PubMed=23772386; DOI=10.1016/j.fob.2013.02.001;
Matagrin B., Hodroge A., Montagut-Romans A., Andru J., Fourel I.,
Besse S., Benoit E., Lattard V.;
"New insights into the catalytic mechanism of vitamin K epoxide
reductase (VKORC1) - The catalytic properties of the major mutations
of rVKORC1 explain the biological cost associated to mutations.";
FEBS Open Bio 3:144-150(2013).
[5]
TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=23928358; DOI=10.1074/jbc.M113.457119;
Hammed A., Matagrin B., Spohn G., Prouillac C., Benoit E., Lattard V.;
"VKORC1L1, an enzyme rescuing the vitamin K 2,3-epoxide reductase
activity in some extrahepatic tissues during anticoagulation
therapy.";
J. Biol. Chem. 288:28733-28742(2013).
[6]
VARIANTS GLN-120; GLN-128; CYS-139; PHE-139 AND SER-139, ACTIVITY
REGULATION, AND FUNCTION.
PubMed=15879509; DOI=10.1534/genetics.104.040360;
Pelz H.J., Rost S., Hunerberg M., Fregin A., Heiberg A.C., Baert K.,
MacNicoll A.D., Prescott C.V., Walker A.S., Oldenburg J., Muller C.R.;
"The genetic basis of resistance to anticoagulants in rodents.";
Genetics 170:1839-1847(2005).
-!- FUNCTION: Involved in vitamin K metabolism. Catalytic subunit of
the vitamin K epoxide reductase (VKOR) complex which reduces
inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is
required for the gamma-carboxylation of various proteins,
including clotting factors, and is required for normal blood
coagulation, but also for normal bone development.
{ECO:0000269|PubMed:15640149, ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:23772386, ECO:0000269|PubMed:23928358}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-disulfide + H2O + phylloquinone = 2,3-
epoxyphylloquinone + [protein]-dithiol; Xref=Rhea:RHEA:13817,
Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15759, ChEBI:CHEBI:18067, ChEBI:CHEBI:29950,
ChEBI:CHEBI:50058; EC=1.17.4.4;
Evidence={ECO:0000269|PubMed:15640149,
ECO:0000269|PubMed:23772386, ECO:0000269|PubMed:23928358};
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-disulfide + phylloquinol = [protein]-dithiol +
phylloquinone; Xref=Rhea:RHEA:57744, Rhea:RHEA-COMP:10593,
Rhea:RHEA-COMP:10594, ChEBI:CHEBI:18067, ChEBI:CHEBI:28433,
ChEBI:CHEBI:29950, ChEBI:CHEBI:50058; EC=1.17.4.4;
Evidence={ECO:0000269|PubMed:15640149,
ECO:0000269|PubMed:23772386, ECO:0000269|PubMed:23928358};
-!- ACTIVITY REGULATION: Inhibited by warfarin (coumadin).
{ECO:0000269|PubMed:15879509, ECO:0000269|PubMed:23772386,
ECO:0000269|PubMed:23928358}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:23772386, ECO:0000269|PubMed:23928358}; Multi-
pass membrane protein {ECO:0000269|PubMed:23772386,
ECO:0000269|PubMed:23928358}.
-!- TISSUE SPECIFICITY: Highly expressed in liver. Detected at lower
levels in lung, kidney and testis. {ECO:0000269|PubMed:23928358}.
-!- DOMAIN: The number of transmembrane domains and the membrane
topology are controversial; supporting evidence is available both
for models with three transmembrane domains and four transmembrane
domains. {ECO:0000250}.
-!- MISCELLANEOUS: The location of two cysteine active-site residues
within a proposed transmembrane is consistent both with the known
hydrophobic environment of the thiol redox site of the enzyme and
with the lipophilicity of vitamin K and warfarin (coumadin).
-!- SIMILARITY: Belongs to the VKOR family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY423047; AAR82917.1; -; mRNA.
RefSeq; NP_976080.1; NM_203335.2.
UniGene; Rn.97942; -.
STRING; 10116.ENSRNOP00000063977; -.
BindingDB; Q6TEK4; -.
GuidetoPHARMACOLOGY; 2645; -.
PaxDb; Q6TEK4; -.
PRIDE; Q6TEK4; -.
Ensembl; ENSRNOT00000073596; ENSRNOP00000063977; ENSRNOG00000050828.
GeneID; 309004; -.
KEGG; rno:309004; -.
UCSC; RGD:1303107; rat.
CTD; 79001; -.
RGD; 1303107; Vkorc1.
eggNOG; ENOG410J0HT; Eukaryota.
eggNOG; ENOG4111UX7; LUCA.
GeneTree; ENSGT00940000157421; -.
HOGENOM; HOG000230752; -.
HOVERGEN; HBG076672; -.
InParanoid; Q6TEK4; -.
KO; K05357; -.
OMA; MCDLGES; -.
OrthoDB; 1611169at2759; -.
PhylomeDB; Q6TEK4; -.
TreeFam; TF328467; -.
BRENDA; 1.1.4.1; 5301.
PRO; PR:Q6TEK4; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000050828; Expressed in 9 organ(s), highest expression level in liver.
ExpressionAtlas; Q6TEK4; baseline and differential.
Genevisible; Q6TEK4; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
GO; GO:0047058; F:vitamin-K-epoxide reductase (warfarin-insensitive) activity; IDA:RGD.
GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
GO; GO:0060348; P:bone development; ISS:UniProtKB.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; ISS:UniProtKB.
GO; GO:0030193; P:regulation of blood coagulation; IMP:RGD.
GO; GO:0046677; P:response to antibiotic; IDA:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
GO; GO:0042373; P:vitamin K metabolic process; ISS:UniProtKB.
Gene3D; 1.20.1440.130; -; 1.
InterPro; IPR012932; VKOR.
InterPro; IPR038354; VKOR_sf.
Pfam; PF07884; VKOR; 1.
SMART; SM00756; VKc; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Endoplasmic reticulum; Membrane;
Oxidoreductase; Polymorphism; Quinone; Redox-active center;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 161 Vitamin K epoxide reductase complex
subunit 1.
/FTId=PRO_0000191670.
TOPO_DOM 1 10 Lumenal. {ECO:0000255}.
TRANSMEM 11 31 Helical. {ECO:0000255}.
TOPO_DOM 32 74 Cytoplasmic. {ECO:0000255}.
TRANSMEM 75 94 Helical. {ECO:0000255}.
TOPO_DOM 95 100 Lumenal. {ECO:0000255}.
TRANSMEM 101 123 Helical. {ECO:0000255}.
TOPO_DOM 124 126 Cytoplasmic. {ECO:0000255}.
TRANSMEM 127 149 Helical. {ECO:0000255}.
TOPO_DOM 150 161 Lumenal. {ECO:0000250}.
DISULFID 132 135 Redox-active.
VARIANT 120 120 L -> Q (identified in warfarin-resistant
animals; strongly reduces enzyme
activity; abolishes inhibition by
warfarin). {ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:23772386}.
VARIANT 128 128 L -> Q (identified in warfarin-resistant
animals; moderately reduces enzyme
activity; decreases inhibition by
warfarin). {ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:23772386}.
VARIANT 139 139 Y -> C (identified in warfarin-resistant
animals; strongly reduces enzyme
activity; abolishes inhibition by
warfarin). {ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:23772386}.
VARIANT 139 139 Y -> F (identified in warfarin-resistant
animals; strongly reduces enzyme
activity; abolishes inhibition by
warfarin). {ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:23772386}.
VARIANT 139 139 Y -> S (identified in warfarin-resistant
animals; strongly reduces enzyme
activity; abolishes inhibition by
warfarin). {ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:23772386}.
MUTAGEN 132 132 C->S: Loss of enzyme activity.
{ECO:0000269|PubMed:15640149}.
MUTAGEN 135 135 C->S: Loss of enzyme activity.
{ECO:0000269|PubMed:15640149}.
SEQUENCE 161 AA; 17783 MW; BBCE9897B00807DD CRC64;
MGTTWRSPGR LRLALCLAGL ALSLYALHVK AARARNEDYR ALCDVGTAIS CSRVFSSRWG
RGFGLVEHVL GADSILNQSN SIFGCMFYTI QLLLGCLRGR WASILLILSS LVSVAGSLYL
AWILFFVLYD FCIVCITTYA INAGLMLLSF QKVPEHKVKK P


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