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UniProtKB/Swiss-Prot entry Q9CRC0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VKOR1_MOUSE
Primary accession number Q9CRC0
Secondary accession numbers None
Integrated into Swiss-Prot on April 12, 2005
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 39)
Name and origin of the protein
Protein name Vitamin K epoxide reductase complex subunit 1
Synonyms EC 1.1.4.1
Vitamin K1 2,3-epoxide reductase subunit 1
Gene name
Name: Vkorc1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Head, Kidney, and Small intestine;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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 (By similarity).
  • CATALYTIC ACTIVITY: 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol.
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity).
  • 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.
  • SIMILARITY: Belongs to the VKOR family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK013996; BAB29106.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002742; BAB22320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK003237; BAB22661.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008509; BAB25708.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008578; BAB25757.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031732; AAH31732.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_848715.1; -.
UniGene Mm.29703
3D structure databases
ModBase Q9CRC0.
Organism-specific databases
MGI MGI:106442; Vkorc1.
Gene expression databases
ArrayExpress Q9CRC0; -.
CleanEx MM_VKORC1; -.
GermOnline ENSMUSG00000030804; Mus musculus.
Ontologies
GO
GO:0047057; Molecular function: vitamin-K-epoxide reductase (warfarin-sensitive) activity (inferred from direct assay from MGI).
GO:0050820; Biological process: positive regulation of coagulation (inferred from mutant phenotype from MGI).
GO:0042373; Biological process: vitamin K metabolic process (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR012932; VKOR.
Graphical view of domain structure.
Pfam PF07884; VKOR; 1.
Pfam graphical view of domain structure.
SMART SM00756; VKc; 1.
SMART graphical view of domain structure.
BLOCKS Q9CRC0.
Genome annotation databases
Ensembl ENSMUSG00000030804; Mus musculus. [Contig view]
GeneID 27973; -.
KEGG mmu:27973; -.
Phylogenomic databases
HOGENOM Q9CRC0; -.
HOVERGEN Q9CRC0; -.
Other
SOURCE Vkorc1; Mus musculus.
ProtoNet Q9CRC0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Membrane; Oxidoreductase; Redox-active center; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   161  161     Vitamin K epoxide reductase complex subunit 1. PRO_0000191669
TOPO_DOM   1     8  8     Lumenal (Potential). 
TRANSMEM   9    29  21     Potential. 
TOPO_DOM   30   100  71     Cytoplasmic (Potential). 
TRANSMEM   101   123  23     Potential. 
TOPO_DOM   124   126  3     Lumenal (Potential). 
TRANSMEM   127   149  23     Potential. 
TOPO_DOM   150   161  12     Cytoplasmic (Potential). 
DISULFID   132   135        Redox-active (Potential). 
Sequence information
Length: 161 AA [This is the length of the unprocessed precursor] Molecular weight: 17768 Da [This is the MW of the unprocessed precursor] CRC64: 044BEED047A57FD9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGTTWRSPGL VRLALCLAGL ALSLYALHVK AARARDENYR ALCDVGTAIS CSRVFSSRWG 

        70         80         90        100        110        120 
RGFGLVEHML GADSVLNQSN SIFGCLFYTL QLLLGCLRGR WASILLVLSS LVSVAGSVYL 

       130        140        150        160 
AWILFFVLYD FCIVCITTYA INVGLMLLSF QKVPEHKTKK H 

Q9CRC0 in FASTA format

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