Variant position: 98 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 163 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human QSNSIFGCIFYTLQLLLGCL RTRWASVLMLLSSLVSLAGSV
Mouse QSNSIFGCLFYTLQLLLGCL RGRWASILLVLSSLVSVAGSV
Rat QSNSIFGCMFYTIQLLLGCL RGRWASILLILSSLVSVAGSL
Bovine QSNSIFGCIFYTLQLLLGCL QGRWASVLLRLSCLVSLAGSV
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 163 Vitamin K epoxide reductase complex subunit 1
59 – 163 WGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH -> LPADTLGLCPDAAELPGVSRWFCLPGLDPVLRAL. In isoform 3.
95 – 163 GCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH -> DGVSPCCPGWSQAICLPQPPKVLGGLQALPADTLGLCPDAAELPGVSRWFCLPGLDPVLRAL. In isoform 2.
85 – 85 C -> A. Reduces enzyme activity by about 25%.
85 – 85 C -> S. Reduces enzyme activity by about 75%.
96 – 96 C -> AS. Reduces enzyme activity by about 70%.
98 – 98 R -> DE. Reduces enzyme activity by about 80%. Decreases inhibition by warfarin.
98 – 98 R -> K. No effect on enzyme activity. Decreases inhibition by warfarin.
Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2.
Rost S.; Fregin A.; Ivaskevicius V.; Conzelmann E.; Hoertnagel K.; Pelz H.-J.; Lappegard K.; Seifried E.; Scharrer I.; Tuddenham E.G.D.; Mueller C.R.; Strom T.M.; Oldenburg J.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; VARIANTS CMRES LEU-29; ALA-45; GLY-58 AND ARG-128; VARIANT VKCFD2 TRP-98;
Site-directed mutagenesis of coumarin-type anticoagulant-sensitive VKORC1: evidence that highly conserved amino acids define structural requirements for enzymatic activity and inhibition by warfarin.
Rost S.; Fregin A.; Hunerberg M.; Bevans C.G.; Muller C.R.; Oldenburg J.;
Thromb. Haemost. 94:780-786(2005)
Cited for: FUNCTION; POTENTIAL REDOX-ACTIVE SITE; CATALYTIC ACTIVITY; ACTIVITY REGULATION; SUBCELLULAR LOCATION; MUTAGENESIS OF CYS-16; CYS-43; CYS-51; SER-57; CYS-85; CYS-96; ARG-98; CYS-132; CYS-135 AND TYR-139; CHARACTERIZATION OF VARIANT VKCFD2 TRP-98;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.