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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_HUMAN             Reviewed;         163 AA.
Q9BQB6; A6NIQ6; B2R4Z6; Q6UX90; Q7Z2R4;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
18-JUL-2018, entry version 142.
RecName: Full=Vitamin K epoxide reductase complex subunit 1;
EC=1.17.4.4 {ECO:0000269|PubMed:15879509, ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610};
AltName: Full=Vitamin K1 2,3-epoxide reductase subunit 1;
Name=VKORC1; Synonyms=VKOR; ORFNames=MSTP134, MSTP576, UNQ308/PRO351;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, VARIANTS CMRES LEU-29; ALA-45; GLY-58
AND ARG-128, AND VARIANT VKCFD2 TRP-98.
TISSUE=Kidney;
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Aorta;
Liu B., Qin B.M., Sheng H., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
Song L., Lu H., Xu H.S., Zheng W.Y., Gong J., Wang Y.B., Liu Y.Q.,
Zhang C.N., Shi Y., Wang W., Zhang Z., Yang X., Han Y., Chen J.Z.,
Liu B.H., Hui R.T.;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-163 (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[10]
POTENTIAL REDOX-ACTIVE SITE.
PubMed=15276181; DOI=10.1016/j.tibs.2004.04.004;
Goodstadt L., Ponting C.P.;
"Vitamin K epoxide reductase: homology, active site and catalytic
mechanism.";
Trends Biochem. Sci. 29:289-292(2004).
[11]
MUTAGENESIS OF ARG-35; SER-56; LEU-120; LEU-128 AND TYR-139, CATALYTIC
ACTIVITY, ENZYME 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).
[12]
TOPOLOGY, AND SUBCELLULAR LOCATION.
PubMed=15716279; DOI=10.1074/jbc.M500765200;
Tie J.-K., Nicchitta C., von Heijne G., Stafford D.W.;
"Membrane topology mapping of vitamin K epoxide reductase by in vitro
translation/cotranslocation.";
J. Biol. Chem. 280:16410-16416(2005).
[13]
FUNCTION, POTENTIAL REDOX-ACTIVE SITE, CATALYTIC ACTIVITY, ENZYME
REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-16; CYS-43;
CYS-51; SER-57; CYS-85; CYS-96; ARG-98; CYS-132; CYS-135 AND TYR-139,
AND CHARACTERIZATION OF VARIANT VKCFD2 TRP-98.
PubMed=16270630; DOI=10.1160/TH05-02-0082;
Rost S., Fregin A., Hunerberg M., Bevans C.G., Muller C.R.,
Oldenburg J.;
"Site-directed mutagenesis of coumarin-type anticoagulant-sensitive
VKORC1: evidence that highly conserved amino acids define structural
requirements for enzymatic activity and inhibition by warfarin.";
Thromb. Haemost. 94:780-786(2005).
[14]
TOPOLOGY.
PubMed=20696932; DOI=10.1073/pnas.1009972107;
Schulman S., Wang B., Li W., Rapoport T.A.;
"Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-
like redox partners.";
Proc. Natl. Acad. Sci. U.S.A. 107:15027-15032(2010).
[15]
CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND
MUTAGENESIS OF CYS-43 AND CYS-51.
PubMed=20978134; DOI=10.1074/jbc.M110.172213;
Rishavy M.A., Usubalieva A., Hallgren K.W., Berkner K.L.;
"Novel insight into the mechanism of the vitamin K oxidoreductase
(VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow
vitamin K reduction and facilitation of vitamin K-dependent protein
carboxylation.";
J. Biol. Chem. 286:7267-7278(2011).
[16]
SUBCELLULAR LOCATION, TOPOLOGY, CATALYTIC ACTIVITY, ENZYME REGULATION,
AND FUNCTION.
PubMed=22923610; DOI=10.1074/jbc.M112.402941;
Tie J.K., Jin D.Y., Stafford D.W.;
"Human vitamin K epoxide reductase and its bacterial homologue have
different membrane topologies and reaction mechanisms.";
J. Biol. Chem. 287:33945-33955(2012).
[17]
3D-STRUCTURE MODELING.
PubMed=24406068; DOI=10.1111/jth.12450;
Wu S., Tie J.K., Stafford D.W., Pedersen L.G.;
"Membrane topology for human vitamin K epoxide reductase.";
J. Thromb. Haemost. 12:112-114(2014).
[18]
VARIANTS CMRES THR-26; LEU-29; GLY-36; TYR-36; TRP-52; PHE-56; LEU-59;
CYS-59; GLY-66; MET-66; ALA-71; SER-77; TYR-77; ASN-123 AND HIS-139.
PubMed=20946155; DOI=10.1111/j.1538-7836.2010.04095.x;
Watzka M., Geisen C., Bevans C.G., Sittinger K., Spohn G., Rost S.,
Seifried E., Muller C.R., Oldenburg J.;
"Thirteen novel VKORC1 mutations associated with oral anticoagulant
resistance: insights into improved patient diagnosis and treatment.";
J. Thromb. Haemost. 9:109-118(2011).
-!- 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:14765194, ECO:0000269|PubMed:14765195,
ECO:0000269|PubMed:15879509, ECO:0000269|PubMed:16270630,
ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610}.
-!- CATALYTIC ACTIVITY: Phylloquinone + oxidized dithiothreitol +
H(2)O = 2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone
+ 1,4-dithiothreitol. {ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134,
ECO:0000269|PubMed:22923610}.
-!- ENZYME REGULATION: Inhibited by warfarin (coumadin).
{ECO:0000269|PubMed:15879509, ECO:0000269|PubMed:16270630,
ECO:0000269|PubMed:22923610}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:15716279,
ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134,
ECO:0000269|PubMed:22923610}; Multi-pass membrane protein
{ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:15716279,
ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134,
ECO:0000269|PubMed:22923610}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=MST576;
IsoId=Q9BQB6-1; Sequence=Displayed;
Name=2; Synonyms=MST134;
IsoId=Q9BQB6-2; Sequence=VSP_013363;
Name=3;
IsoId=Q9BQB6-3; Sequence=VSP_043407;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at highest levels in fetal and adult
liver, followed by fetal heart, kidney, and lung, adult heart, and
pancreas. {ECO:0000269|PubMed:14765194}.
-!- DOMAIN: The number of transmembrane domains and the membrane
topology are controversial; supporting evidence is available both
for models with three transmembrane domains (PubMed:15716279 and
PubMed:22923610) and four transmembrane domains (PubMed:20696932
and PubMed:20978134). According to PubMed:15716279 and
PubMed:22923610 the N-terminus of the protein is in the
endoplasmic reticulum lumen, while the C-terminus is in the
cytosol, which is in favor of three transmembrane domains.
According to PubMed:20696932, both N-terminus and C-terminus are
in the cytosol, indicating the presence of four transmembrane
domains. Besides, the 3D-structure of a bacterial ortholog shows
four transmembrane domains. Moreover, proteins that reside in the
endoplasmic reticulum lumen can catalyze the reduction of the
active site cysteines, possibly via Cys-43 and Cys-51
(PubMed:20696932 and PubMed:20978134), but less efficiently than
the synthetic compound dithiothreitol (in vitro). Location of Cys-
43 and Cys-51 in the endoplasmic reticulum lumen would be in
agreement with four transmembrane domains. Again, these data are
controversial, and papers do not agree on the effects of mutating
Cys-43 and Cys-51, probably because of differences in the assay
systems.
-!- DISEASE: Combined deficiency of vitamin K-dependent clotting
factors 2 (VKCFD2) [MIM:607473]: VKCFD leads to a bleeding
tendency that is usually reversed by oral administration of
vitamin K. {ECO:0000269|PubMed:14765194,
ECO:0000269|PubMed:16270630}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Coumarin resistance (CMRES) [MIM:122700]: A condition
characterized by partial or complete resistance to warfarin or
other 4-hydroxycoumarin derivatives. These drugs are used as anti-
coagulants for the prevention of thromboembolic diseases in
subjects with deep vein thrombosis, atrial fibrillation, or
mechanical heart valve replacement. {ECO:0000269|PubMed:14765194,
ECO:0000269|PubMed:20946155}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAQ88821.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/vkorc1/";
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EMBL; AY423044; AAR82914.1; -; mRNA.
EMBL; AY521634; AAS01052.1; -; mRNA.
EMBL; AF176924; AAQ13668.1; -; mRNA.
EMBL; AY466113; AAR28759.1; -; mRNA.
EMBL; AY587020; AAS83106.1; -; Genomic_DNA.
EMBL; AK289790; BAF82479.1; -; mRNA.
EMBL; AK312005; BAG34943.1; -; mRNA.
EMBL; AC135050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471192; EAW52167.1; -; Genomic_DNA.
EMBL; CH471192; EAW52168.1; -; Genomic_DNA.
EMBL; BC002911; AAH02911.1; -; mRNA.
EMBL; AY358456; AAQ88821.1; ALT_INIT; mRNA.
CCDS; CCDS10703.1; -. [Q9BQB6-1]
CCDS; CCDS10704.1; -. [Q9BQB6-3]
RefSeq; NP_001298240.1; NM_001311311.1.
RefSeq; NP_076869.1; NM_024006.5. [Q9BQB6-1]
RefSeq; NP_996560.1; NM_206824.2. [Q9BQB6-3]
UniGene; Hs.324844; -.
ProteinModelPortal; Q9BQB6; -.
BioGrid; 122472; 100.
IntAct; Q9BQB6; 46.
MINT; Q9BQB6; -.
STRING; 9606.ENSP00000378426; -.
BindingDB; Q9BQB6; -.
ChEMBL; CHEMBL1930; -.
DrugBank; DB01418; Acenocoumarol.
DrugBank; DB00266; Dicoumarol.
DrugBank; DB00170; Menadione.
DrugBank; DB00498; Phenindione.
DrugBank; DB00946; Phenprocoumon.
DrugBank; DB00682; Warfarin.
GuidetoPHARMACOLOGY; 2645; -.
MoonDB; Q9BQB6; Predicted.
iPTMnet; Q9BQB6; -.
PhosphoSitePlus; Q9BQB6; -.
SwissPalm; Q9BQB6; -.
BioMuta; VKORC1; -.
DMDM; 62511226; -.
EPD; Q9BQB6; -.
MaxQB; Q9BQB6; -.
PaxDb; Q9BQB6; -.
PeptideAtlas; Q9BQB6; -.
PRIDE; Q9BQB6; -.
ProteomicsDB; 78652; -.
ProteomicsDB; 78653; -. [Q9BQB6-2]
ProteomicsDB; 78654; -. [Q9BQB6-3]
DNASU; 79001; -.
Ensembl; ENST00000319788; ENSP00000326135; ENSG00000167397. [Q9BQB6-2]
Ensembl; ENST00000354895; ENSP00000346969; ENSG00000167397. [Q9BQB6-3]
Ensembl; ENST00000394975; ENSP00000378426; ENSG00000167397. [Q9BQB6-1]
GeneID; 79001; -.
KEGG; hsa:79001; -.
UCSC; uc002eas.4; human. [Q9BQB6-1]
CTD; 79001; -.
DisGeNET; 79001; -.
EuPathDB; HostDB:ENSG00000167397.14; -.
GeneCards; VKORC1; -.
H-InvDB; HIX0079837; -.
HGNC; HGNC:23663; VKORC1.
HPA; HPA042720; -.
MalaCards; VKORC1; -.
MIM; 122700; phenotype.
MIM; 607473; phenotype.
MIM; 608547; gene.
neXtProt; NX_Q9BQB6; -.
OpenTargets; ENSG00000167397; -.
Orphanet; 98434; Hereditary combined deficiency of vitamin K-dependent clotting factors.
Orphanet; 413684; Resistance to vitamin K antagonists.
Orphanet; 413674; Vitamin K antagonists toxicity or dose selection.
PharmGKB; PA133787052; -.
eggNOG; ENOG410J0HT; Eukaryota.
eggNOG; ENOG4111UX7; LUCA.
GeneTree; ENSGT00390000002103; -.
HOGENOM; HOG000230752; -.
HOVERGEN; HBG076672; -.
InParanoid; Q9BQB6; -.
KO; K05357; -.
OMA; QGKVKGH; -.
OrthoDB; EOG091G0QTR; -.
PhylomeDB; Q9BQB6; -.
TreeFam; TF328467; -.
BioCyc; MetaCyc:HS15548-MONOMER; -.
BRENDA; 1.1.4.1; 2681.
Reactome; R-HSA-6806664; Metabolism of vitamin K.
GeneWiki; VKORC1; -.
GenomeRNAi; 79001; -.
PRO; PR:Q9BQB6; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167397; -.
CleanEx; HS_VKORC1; -.
ExpressionAtlas; Q9BQB6; baseline and differential.
Genevisible; Q9BQB6; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
GO; GO:0047057; F:vitamin-K-epoxide reductase (warfarin-sensitive) activity; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; IMP:UniProtKB.
GO; GO:0060348; P:bone development; ISS:UniProtKB.
GO; GO:0017144; P:drug metabolic process; IMP:UniProtKB.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; IMP:UniProtKB.
GO; GO:0042373; P:vitamin K metabolic process; IDA: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;
Alternative splicing; Complete proteome; Disease mutation;
Disulfide bond; Endoplasmic reticulum; Membrane; Oxidoreductase;
Quinone; Redox-active center; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 163 Vitamin K epoxide reductase complex
subunit 1.
/FTId=PRO_0000191668.
TOPO_DOM 1 8 Lumenal. {ECO:0000255}.
TRANSMEM 9 29 Helical. {ECO:0000305}.
TOPO_DOM 30 74 Cytoplasmic. {ECO:0000255}.
TRANSMEM 75 95 Helical. {ECO:0000255}.
TRANSMEM 101 123 Helical. {ECO:0000305}.
TOPO_DOM 124 126 Lumenal. {ECO:0000305}.
TRANSMEM 127 149 Helical. {ECO:0000305}.
TOPO_DOM 150 163 Cytoplasmic. {ECO:0000305}.
DISULFID 132 135 Redox-active.
VAR_SEQ 59 163 WGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRT
RWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYA
INVSLMWLSFRKVQEPQGKAKRH -> LPADTLGLCPDAAE
LPGVSRWFCLPGLDPVLRAL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043407.
VAR_SEQ 95 163 GCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVC
ITTYAINVSLMWLSFRKVQEPQGKAKRH -> DGVSPCCPG
WSQAICLPQPPKVLGGLQALPADTLGLCPDAAELPGVSRWF
CLPGLDPVLRAL (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_013363.
VARIANT 26 26 A -> T (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065785.
VARIANT 29 29 V -> L (in CMRES; dbSNP:rs104894539).
{ECO:0000269|PubMed:14765194,
ECO:0000269|PubMed:20946155}.
/FTId=VAR_021821.
VARIANT 36 36 D -> G (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065786.
VARIANT 36 36 D -> Y (in CMRES; dbSNP:rs61742245).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065787.
VARIANT 45 45 V -> A (in CMRES; dbSNP:rs104894540).
{ECO:0000269|PubMed:14765194}.
/FTId=VAR_021822.
VARIANT 52 52 S -> W (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065788.
VARIANT 56 56 S -> F (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065789.
VARIANT 58 58 R -> G (in CMRES; dbSNP:rs104894541).
{ECO:0000269|PubMed:14765194}.
/FTId=VAR_021823.
VARIANT 59 59 W -> C (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065790.
VARIANT 59 59 W -> L (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065791.
VARIANT 66 66 V -> G (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065792.
VARIANT 66 66 V -> M (in CMRES; dbSNP:rs72547529).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065793.
VARIANT 71 71 G -> A (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065794.
VARIANT 77 77 N -> S (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065795.
VARIANT 77 77 N -> Y (in CMRES; dbSNP:rs755767348).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065796.
VARIANT 98 98 R -> W (in VKCFD2; strongly reduced
enzyme activity; dbSNP:rs72547528).
{ECO:0000269|PubMed:14765194,
ECO:0000269|PubMed:16270630}.
/FTId=VAR_021824.
VARIANT 123 123 I -> N (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065797.
VARIANT 128 128 L -> R (in CMRES; dbSNP:rs104894542).
{ECO:0000269|PubMed:14765194}.
/FTId=VAR_021825.
VARIANT 139 139 Y -> H (in CMRES).
{ECO:0000269|PubMed:20946155}.
/FTId=VAR_065798.
MUTAGEN 16 16 C->A,S: Reduces enzyme activity by about
80%. {ECO:0000269|PubMed:16270630}.
MUTAGEN 35 35 R->P: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:15879509}.
MUTAGEN 43 43 C->A,S: Reduces enzyme activity.
{ECO:0000269|PubMed:16270630,
ECO:0000269|PubMed:20978134}.
MUTAGEN 51 51 C->A,S: Reduces enzyme activity.
{ECO:0000269|PubMed:16270630,
ECO:0000269|PubMed:20978134}.
MUTAGEN 56 56 S->P: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:15879509}.
MUTAGEN 57 57 S->A: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:16270630}.
MUTAGEN 85 85 C->A: Reduces enzyme activity by about
25%. {ECO:0000269|PubMed:16270630}.
MUTAGEN 85 85 C->S: Reduces enzyme activity by about
75%. {ECO:0000269|PubMed:16270630}.
MUTAGEN 96 96 C->A,S: Reduces enzyme activity by about
70%. {ECO:0000269|PubMed:16270630}.
MUTAGEN 98 98 R->D,E: Reduces enzyme activity by about
80%. Decreases inhibition by warfarin.
{ECO:0000269|PubMed:16270630}.
MUTAGEN 98 98 R->K: No effect on enzyme activity.
Decreases inhibition by warfarin.
{ECO:0000269|PubMed:16270630}.
MUTAGEN 120 120 L->Q: Decreases enzyme activity
moderately. Decreases inhibition by
warfarin. {ECO:0000269|PubMed:15879509}.
MUTAGEN 128 128 L->Q,S: Decreases enzyme activity by
about 80%. Decreases inhibition by
warfarin. {ECO:0000269|PubMed:15879509}.
MUTAGEN 132 132 C->S: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:16270630}.
MUTAGEN 135 135 C->S: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:16270630}.
MUTAGEN 139 139 Y->C,G,S: Decreases enzyme activity
moderately. Strongly decreases inhibition
by warfarin.
{ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:16270630}.
MUTAGEN 139 139 Y->F: No effect on enzyme activity.
Strongly decreases inhibition by
warfarin. {ECO:0000269|PubMed:15879509,
ECO:0000269|PubMed:16270630}.
SEQUENCE 163 AA; 18235 MW; 2F00526A6C561D5A CRC64;
MGSTWGSPGW VRLALCLTGL VLSLYALHVK AARARDRDYR ALCDVGTAIS CSRVFSSRWG
RGFGLVEHVL GQDSILNQSN SIFGCIFYTL QLLLGCLRTR WASVLMLLSS LVSLAGSVYL
AWILFFVLYD FCIVCITTYA INVSLMWLSF RKVQEPQGKA KRH


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