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Protein

Vitamin K epoxide reductase complex subunit 1

Gene

Vkorc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.4 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by warfarin (coumadin).3 Publications

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: UniProtKB
  • bone development Source: UniProtKB
  • peptidyl-glutamic acid carboxylation Source: UniProtKB
  • regulation of blood coagulation Source: RGD
  • response to antibiotic Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD
  • vitamin K metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BRENDAi1.1.4.1. 5301.
ReactomeiR-RNO-6806664. Metabolism of vitamin K.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K epoxide reductase complex subunit 1 (EC:1.17.4.43 Publications)
Alternative name(s):
Vitamin K1 2,3-epoxide reductase subunit 1
Gene namesi
Name:Vkorc1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1303107. Vkorc1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010LumenalSequence analysis
Transmembranei11 – 3121HelicalSequence analysisAdd
BLAST
Topological domaini32 – 7443CytoplasmicSequence analysisAdd
BLAST
Transmembranei75 – 9420HelicalSequence analysisAdd
BLAST
Topological domaini95 – 1006LumenalSequence analysis
Transmembranei101 – 12323HelicalSequence analysisAdd
BLAST
Topological domaini124 – 1263CytoplasmicSequence analysis
Transmembranei127 – 14923HelicalSequence analysisAdd
BLAST
Topological domaini150 – 16112LumenalBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321C → S: Loss of enzyme activity. 1 Publication
Mutagenesisi135 – 1351C → S: Loss of enzyme activity. 1 Publication

Chemistry

GuidetoPHARMACOLOGYi2645.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Vitamin K epoxide reductase complex subunit 1PRO_0000191670Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Quinone

Proteomic databases

PaxDbiQ6TEK4.
PRIDEiQ6TEK4.

Expressioni

Tissue specificityi

Highly expressed in liver. Detected at lower levels in lung, kidney and testis.1 Publication

Gene expression databases

BgeeiENSRNOG00000050828.
ExpressionAtlasiQ6TEK4. baseline and differential.
GenevisibleiQ6TEK4. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4578394.
STRINGi10116.ENSRNOP00000063977.

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.
InParanoidiQ6TEK4.
KOiK05357.
OMAiRARWASI.
OrthoDBiEOG091G0QTR.
PhylomeDBiQ6TEK4.
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.

Q6TEK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTTWRSPGR LRLALCLAGL ALSLYALHVK AARARNEDYR ALCDVGTAIS
60 70 80 90 100
CSRVFSSRWG RGFGLVEHVL GADSILNQSN SIFGCMFYTI QLLLGCLRGR
110 120 130 140 150
WASILLILSS LVSVAGSLYL AWILFFVLYD FCIVCITTYA INAGLMLLSF
160
QKVPEHKVKK P
Length:161
Mass (Da):17,783
Last modified:July 5, 2004 - v1
Checksum:iBBCE9897B00807DD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201L → Q Identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin. 2 Publications
Natural varianti128 – 1281L → Q Identified in warfarin-resistant animals; moderately reduces enzyme activity; decreases inhibition by warfarin. 2 Publications
Natural varianti139 – 1391Y → C Identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin. 2 Publications
Natural varianti139 – 1391Y → F Identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin. 2 Publications
Natural varianti139 – 1391Y → S Identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin. 2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY423047 mRNA. Translation: AAR82917.1.
RefSeqiNP_976080.1. NM_203335.2.
UniGeneiRn.97942.

Genome annotation databases

EnsembliENSRNOT00000073596; ENSRNOP00000063977; ENSRNOG00000050828.
GeneIDi309004.
KEGGirno:309004.
UCSCiRGD:1303107. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY423047 mRNA. Translation: AAR82917.1.
RefSeqiNP_976080.1. NM_203335.2.
UniGeneiRn.97942.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4578394.
STRINGi10116.ENSRNOP00000063977.

Chemistry

GuidetoPHARMACOLOGYi2645.

Proteomic databases

PaxDbiQ6TEK4.
PRIDEiQ6TEK4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000073596; ENSRNOP00000063977; ENSRNOG00000050828.
GeneIDi309004.
KEGGirno:309004.
UCSCiRGD:1303107. rat.

Organism-specific databases

CTDi79001.
RGDi1303107. Vkorc1.

Phylogenomic databases

eggNOGiENOG410J0HT. Eukaryota.
ENOG4111UX7. LUCA.
GeneTreeiENSGT00390000002103.
HOGENOMiHOG000230752.
HOVERGENiHBG076672.
InParanoidiQ6TEK4.
KOiK05357.
OMAiRARWASI.
OrthoDBiEOG091G0QTR.
PhylomeDBiQ6TEK4.
TreeFamiTF328467.

Enzyme and pathway databases

BRENDAi1.1.4.1. 5301.
ReactomeiR-RNO-6806664. Metabolism of vitamin K.

Miscellaneous databases

PROiQ6TEK4.

Gene expression databases

BgeeiENSRNOG00000050828.
ExpressionAtlasiQ6TEK4. baseline and differential.
GenevisibleiQ6TEK4. RN.

Family and domain databases

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

Entry informationi

Entry nameiVKOR1_RAT
AccessioniPrimary (citable) accession number: Q6TEK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 93 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).

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.