ID G3CE67_MOUSE Unreviewed; 58 AA. AC G3CE67; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-OCT-2022, entry version 16. DE RecName: Full=Vitamin-K-epoxide reductase (warfarin-sensitive) {ECO:0000256|ARBA:ARBA00012278}; DE EC=1.17.4.4 {ECO:0000256|ARBA:ARBA00012278}; DE Flags: Fragment; GN Name=Vkorc1 {ECO:0000313|EMBL:ADN33368.1}; OS Mus musculus domesticus (western European house mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10092 {ECO:0000313|EMBL:ADN33368.1}; RN [1] {ECO:0000313|EMBL:ADN33368.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21782438; DOI=10.1016/j.cub.2011.06.043; RA Song Y., Endepols S., Klemann N., Richter D., Matuschka F.R., Shih C.H., RA Nachman M.W., Kohn M.H.; RT "Adaptive Introgression of Anticoagulant Rodent Poison Resistance by RT Hybridization between Old World Mice."; RL Curr. Biol. 21:1296-1301(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-disulfide + H2O + phylloquinone = 2,3- CC epoxyphylloquinone + [protein]-dithiol; Xref=Rhea:RHEA:13817, CC Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15759, ChEBI:CHEBI:18067, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:50058; EC=1.17.4.4; CC Evidence={ECO:0000256|ARBA:ARBA00000266}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-disulfide + phylloquinol = [protein]-dithiol + CC phylloquinone; Xref=Rhea:RHEA:57744, Rhea:RHEA-COMP:10593, Rhea:RHEA- CC COMP:10594, ChEBI:CHEBI:18067, ChEBI:CHEBI:28433, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:50058; EC=1.17.4.4; CC Evidence={ECO:0000256|ARBA:ARBA00001488}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the VKOR family. CC {ECO:0000256|ARBA:ARBA00006214}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HM027476; ADN33368.1; -; Genomic_DNA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016900; F:oxidoreductase activity, acting on the CH-OH group of donors, disulfide as acceptor; IEA:UniProt. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0047057; F:vitamin-K-epoxide reductase (warfarin-sensitive) activity; IEA:InterPro. DR GO; GO:0042373; P:vitamin K metabolic process; IEA:InterPro. DR Gene3D; 1.20.1440.130; -; 1. DR InterPro; IPR012932; VKOR. DR InterPro; IPR038354; VKOR_sf. DR InterPro; IPR042406; VKORC1/VKORC1L1. DR PANTHER; PTHR14519; PTHR14519; 1. DR Pfam; PF07884; VKOR; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Quinone {ECO:0000256|ARBA:ARBA00022719}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT DOMAIN 11..58 FT /note="VKc" FT /evidence="ECO:0000259|Pfam:PF07884" FT NON_TER 58 FT /evidence="ECO:0000313|EMBL:ADN33368.1" SQ SEQUENCE 58 AA; 6326 MW; 16234F3489735D58 CRC64; MGTTWRSPGL VRLALCLAGL ALSLYSLHVK AARARDENYR ALCDVGTXIS CSRVFSSR //