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Q9CRC0 (VKOR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Vitamin K epoxide reductase complex subunit 1
EC=1.1.4.1
Alternative name(s):
Vitamin K1 2,3-epoxide reductase subunit 1
Gene names
Name:Vkorc1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (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.

Sequence similarities

Belongs to the VKOR family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Vitamin K epoxide reductase complex subunit 1
PRO_0000191669

Regions

Topological domain1 – 88Lumenal Potential
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 10071Cytoplasmic Potential
Transmembrane101 – 12323Helical; Potential
Topological domain124 – 1263Lumenal Potential
Transmembrane127 – 14923Helical; Potential
Topological domain150 – 16112Cytoplasmic Potential

Amino acid modifications

Disulfide bond132 ↔ 135Redox-active Potential

Sequences

Sequence LengthMass (Da)Tools
Q9CRC0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 044BEED047A57FD9

FASTA16117,768
        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

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head, Kidney and Small intestine.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK013996 mRNA. Translation: BAB29106.1.
AK002742 mRNA. Translation: BAB22320.1.
AK003237 mRNA. Translation: BAB22661.1.
AK008509 mRNA. Translation: BAB25708.1.
AK008578 mRNA. Translation: BAB25757.1.
BC031732 mRNA. Translation: AAH31732.1.
IPIIPI00133579.
RefSeqNP_848715.1. NM_178600.2.
UniGeneMm.29703.

3D structure databases

ProteinModelPortalQ9CRC0.
SMRQ9CRC0. Positions 6-152.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9CRC0.

Proteomic databases

PRIDEQ9CRC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033074; ENSMUSP00000033074; ENSMUSG00000030804.
GeneID27973.
KEGGmmu:27973.
UCSCuc009jxe.1. mouse.

Organism-specific databases

CTD79001.
MGIMGI:106442. Vkorc1.

Phylogenomic databases

eggNOGroNOG15877.
GeneTreeENSGT00390000002103.
HOGENOMHBG714015.
HOVERGENHBG076672.
InParanoidQ9CRC0.
OMAQGKVKGH.
OrthoDBEOG4ZGPDK.
PhylomeDBQ9CRC0.

Gene expression databases

ArrayExpressQ9CRC0.
BgeeQ9CRC0.
CleanExMM_VKORC1.
GenevestigatorQ9CRC0.
GermOnlineENSMUSG00000030804. Mus musculus.

Family and domain databases

InterProIPR012932. VKOR.
[Graphical view]
KOK05357.
PfamPF07884. VKOR. 1 hit.
[Graphical view]
SMARTSM00756. VKc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio306466.
SOURCESearch...

Entry information

Entry nameVKOR1_MOUSE
AccessionPrimary (citable) accession number: Q9CRC0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents