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Protein

Vitamin K epoxide reductase complex subunit 1

Gene

VKORC1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

Phylloquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + 1,4-dithiothreitol.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

ReactomeiR-BTA-6806664. Metabolism of vitamin K.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K epoxide reductase complex subunit 1 (EC:1.17.4.4)
Alternative name(s):
Vitamin K1 2,3-epoxide reductase subunit 1
Gene namesi
Name:VKORC1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88LumenalSequence analysis
Transmembranei9 – 2921HelicalSequence analysisAdd
BLAST
Topological domaini30 – 8152CytoplasmicSequence analysisAdd
BLAST
Transmembranei82 – 10221HelicalSequence analysisAdd
BLAST
Topological domaini103 – 1031LumenalSequence analysis
Transmembranei104 – 12219HelicalSequence analysisAdd
BLAST
Transmembranei128 – 15023HelicalSequence analysisAdd
BLAST
Topological domaini151 – 16313CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3212.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Vitamin K epoxide reductase complex subunit 1PRO_0000191667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi132 ↔ 135Redox-activeBy similarity

Keywords - PTMi

Disulfide bond, Quinone

Proteomic databases

PaxDbiQ6B4J2.
PRIDEiQ6B4J2.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000519.

Chemistry

BindingDBiQ6B4J2.

Family & Domainsi

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the VKOR family.Curated

Keywords - Domaini

Redox-active center, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J0HT. Eukaryota.
ENOG4111UX7. LUCA.
GeneTreeiENSGT00390000002103.
HOGENOMiHOG000230752.
HOVERGENiHBG076672.
InParanoidiQ6B4J2.
KOiK05357.
OMAiRARWASI.
OrthoDBiEOG7TQV2D.
TreeFamiTF328467.

Family and domain databases

InterProiIPR012932. VKOR.
[Graphical view]
PfamiPF07884. VKOR. 1 hit.
[Graphical view]
SMARTiSM00756. VKc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6B4J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGATWRSPGW VRLALCLAGL VLSLYALHVK AARARDRDYR ALCDVGTAIS
60 70 80 90 100
CSRVFSSRWG RGFGLVEHVL GKDSILNQSN SIFGCIFYTL QLLLGCLQGR
110 120 130 140 150
WASVLLRLSC LVSLAGSVYL AWILFFVLYD FCIVCITTYA INVGLTVLSF
160
REVQGPQGKV KGH
Length:163
Mass (Da):17,967
Last modified:September 13, 2004 - v1
Checksum:i7C8A7A5057908F20
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY682746 mRNA. Translation: AAT85856.1.
BC133442 mRNA. Translation: AAI33443.1.
RefSeqiNP_001003903.1. NM_001003903.3.
UniGeneiBt.1707.

Genome annotation databases

EnsembliENSBTAT00000000519; ENSBTAP00000000519; ENSBTAG00000000405.
GeneIDi445422.
KEGGibta:445422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY682746 mRNA. Translation: AAT85856.1.
BC133442 mRNA. Translation: AAI33443.1.
RefSeqiNP_001003903.1. NM_001003903.3.
UniGeneiBt.1707.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000519.

Chemistry

BindingDBiQ6B4J2.
ChEMBLiCHEMBL3212.

Proteomic databases

PaxDbiQ6B4J2.
PRIDEiQ6B4J2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000519; ENSBTAP00000000519; ENSBTAG00000000405.
GeneIDi445422.
KEGGibta:445422.

Organism-specific databases

CTDi79001.

Phylogenomic databases

eggNOGiENOG410J0HT. Eukaryota.
ENOG4111UX7. LUCA.
GeneTreeiENSGT00390000002103.
HOGENOMiHOG000230752.
HOVERGENiHBG076672.
InParanoidiQ6B4J2.
KOiK05357.
OMAiRARWASI.
OrthoDBiEOG7TQV2D.
TreeFamiTF328467.

Enzyme and pathway databases

ReactomeiR-BTA-6806664. Metabolism of vitamin K.

Family and domain databases

InterProiIPR012932. VKOR.
[Graphical view]
PfamiPF07884. VKOR. 1 hit.
[Graphical view]
SMARTiSM00756. VKc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bovine vitamin K epoxide reductase cDNA."
    Jin D.-Y., Tie J.-K., Stafford D.W.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal liver.

Entry informationi

Entry nameiVKOR1_BOVIN
AccessioniPrimary (citable) accession number: Q6B4J2
Secondary accession number(s): A2VDX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: September 13, 2004
Last modified: June 8, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.