ID A0A7T0LYL8_MOUSE Unreviewed; 90 AA. AC A0A7T0LYL8; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-MAY-2024, entry version 8. 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:QPL12615.1}; 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:QPL12615.1}; RN [1] {ECO:0000313|EMBL:QPL12615.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=32970676; RA Duncan B.J.M.L., Koenders A., Burnham Q., Lohr M.T.; RT "Mus musculus populations in Western Australia lack VKORC1 mutations RT conferring resistance to first generation anticoagulant rodenticides: RT Implications for conservation and biosecurity."; RL PLoS ONE 15:0-e0236234(2020). 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; MT956896; QPL12611.1; -; Genomic_DNA. DR EMBL; MT956898; QPL12613.1; -; Genomic_DNA. DR EMBL; MT956900; QPL12615.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7T0LYL8; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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:0007596; P:blood coagulation; IEA:TreeGrafter. DR GO; GO:0042373; P:vitamin K metabolic process; IEA:InterPro. DR CDD; cd12917; VKOR_euk; 1. DR Gene3D; 1.20.1440.130; VKOR domain; 1. DR InterPro; IPR012932; VKOR. DR InterPro; IPR038354; VKOR_sf. DR InterPro; IPR042406; VKORC1/VKORC1L1. DR PANTHER; PTHR14519:SF0; VITAMIN K EPOXIDE REDUCTASE COMPLEX SUBUNIT 1; 1. DR PANTHER; PTHR14519; VITAMIN K EPOXIDE REDUCTASE COMPLEX, SUBUNIT 1; 1. DR Pfam; PF07884; VKOR; 1. DR SMART; SM00756; VKc; 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 Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..90 FT /note="vitamin-K-epoxide reductase (warfarin-sensitive)" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5033598802" FT DOMAIN 1..90 FT /note="Vitamin K epoxide reductase" FT /evidence="ECO:0000259|SMART:SM00756" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QPL12615.1" FT NON_TER 90 FT /evidence="ECO:0000313|EMBL:QPL12615.1" SQ SEQUENCE 90 AA; 9862 MW; 67DEF2700E17B198 CRC64; WRSPGLVRLA LCLAGLALSL YALHVKAARA RDENYRALCD VGTAISCSRV FSSRWGRGFG LVEHMLGADS VLNQSNSIFG CLFYTLQLLL //