Reviewed, UniProtKB/Swiss-Prot Q9CRC0 (VKOR1_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Redox-active center Transmembrane
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of coagulation Inferred from mutant phenotype. Source: MGI vitamin K metabolic process Inferred from direct assay. Source: MGI
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	vitamin-K-epoxide reductase (warfarin-sensitive) activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 161	161	Vitamin K epoxide reductase complex subunit 1		PRO_0000191669
Regions
	Topological domain	1 – 8	8	Lumenal Potential
	Transmembrane	9 – 29	21	Potential
	Topological domain	30 – 100	71	Cytoplasmic Potential
	Transmembrane	101 – 123	23	Potential
	Topological domain	124 – 126	3	Lumenal Potential
	Transmembrane	127 – 149	23	Potential
	Topological domain	150 – 161	12	Cytoplasmic Potential
Amino acid modifications
	Disulfide bond	132 ↔ 135		Redox-active Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9CRC0-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 044BEED047A57FD9	FASTA	161	17,768
	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

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. , 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
EMBLGenBankDDBJ	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.
IPI	IPI00133579.
RefSeq	NP_848715.1.
UniGene	Mm.29703
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9CRC0.
Genome annotation databases
Ensembl	ENSMUSG00000030804. Mus musculus. [Contig view]
GeneID	27973.
KEGG	mmu:27973.
Organism-specific databases
MGI	MGI:106442. Vkorc1.
Phylogenomic databases
HOGENOM	Q9CRC0.
HOVERGEN	Q9CRC0.
OMA	Q9CRC0. QGKVKGH.
Enzyme and pathway databases
BRENDA	1.1.4.1. 244.
Gene expression databases
ArrayExpress	Q9CRC0.
Bgee	Q9CRC0.
CleanEx	MM_VKORC1.
GermOnline	ENSMUSG00000030804. Mus musculus.
Family and domain databases
InterPro	IPR012932. VKOR. [Graphical view]
Pfam	PF07884. VKOR. 1 hit. [Graphical view]
SMART	SM00756. VKc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	306466.
SOURCE	Search...

Entry information

Entry name

VKOR1_MOUSE

Accession

Primary (citable) accession number: Q9CRC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)