ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q6B4J2


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name VKOR1_BOVIN
Primary accession number Q6B4J2
Secondary accession number A2VDX1
Integrated into Swiss-Prot on April 12, 2005
Sequence was last modified on September 13, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 26)
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
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Jin D.-Y., Tie J.-K., Stafford D.W.;
"Bovine vitamin K epoxide reductase cDNA.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Fetal liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
  • 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
AY682746; AAT85856.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC133442; AAI33443.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001003903.1; -.
UniGene Bt.1707
3D structure databases
ModBase Q6B4J2.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
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 Q6B4J2.
Genome annotation databases
Ensembl ENSBTAG00000000405; Bos taurus. [Contig view]
GeneID 445422; -.
KEGG bta:445422; -.
Phylogenomic databases
HOVERGEN Q6B4J2; -.
Other
ProtoNet Q6B4J2.
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   163  163     Vitamin K epoxide reductase complex subunit 1. PRO_0000191667
TOPO_DOM   1     8  8     Lumenal (Potential). 
TRANSMEM   9    29  21     Potential. 
TOPO_DOM   30    81  52     Cytoplasmic (Potential). 
TRANSMEM   82   102  21     Potential. 
TOPO_DOM   103   113  11     Lumenal (Potential). 
TRANSMEM   114   134  21     Potential. 
TOPO_DOM   135   163  29     Cytoplasmic (Potential). 
DISULFID   132   135        Redox-active (Potential). 
Sequence information
Length: 163 AA [This is the length of the unprocessed precursor] Molecular weight: 17967 Da [This is the MW of the unprocessed precursor] CRC64: 7C8A7A5057908F20 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGATWRSPGW VRLALCLAGL VLSLYALHVK AARARDRDYR ALCDVGTAIS CSRVFSSRWG 

        70         80         90        100        110        120 
RGFGLVEHVL GKDSILNQSN SIFGCIFYTL QLLLGCLQGR WASVLLRLSC LVSLAGSVYL 

       130        140        150        160 
AWILFFVLYD FCIVCITTYA INVGLTVLSF REVQGPQGKV KGH 

Q6B4J2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!