Sequence information
Variant position: 125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 466 The length of the canonical sequence.
Location on the sequence:
SDGDQCASSPCQNGGSCKDQ
L QSYICFCLPAFEGRNCETHK
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 SDGDQCASSPCQNGGSCKDQL QSYICFCLPAFEGRNCETHK
Chimpanzee SDGDQCASSPCQNGGSCKDQL QSYICFCLPAFEGRNCETYK
Mouse SDGDQCASNPCQNGGTCQDHL KSYVCFCLLDFEGRNCEKSK
Rat SDGDQCASNPCQNGGTCQDHL KSYVCFCPLDFEGRNCEKNK
Bovine NDGDQCASSPCQNGGSCEDQL RSYICFCPDGFEGRNCETDK
Rabbit NDGDQCASNPCQNGGSCEDQI QSYICFCLADFEGRNCEKNK
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
Chain
61 – 212
Factor VII light chain
Domain
106 – 142
EGF-like 1; calcium-binding
Site
113 – 113
Important for S-112 for O-xylosylation
Modified residue
123 – 123
(3R)-3-hydroxyaspartate
Glycosylation
112 – 112
O-linked (Glc...) serine; alternate
Glycosylation
112 – 112
O-linked (Xyl...) serine; alternate
Glycosylation
120 – 120
O-linked (Fuc) serine
Disulfide bond
115 – 130
Mutagenesis
112 – 112
S -> A. Complete loss of O-glycosylation and O-xylosylation by POGLUT1.
Mutagenesis
113 – 113
S -> A. No effect on O-glycosylation by POGLUT1. Drastic decrease in O-xylosylation.
Literature citations
Molecular analysis of the genotype-phenotype relationship in factor VII deficiency.
Millar D.S.; Kemball-Cook G.; McVey J.H.; Tuddenham E.G.D.; Mumford A.D.; Attock G.B.; Reverter J.C.; Lanir N.; Parapia L.A.; Reynaud J.; Meili E.; von Felton A.; Martinowitz U.; Prangnell D.R.; Krawczak M.; Cooper D.N.;
Hum. Genet. 107:327-342(2000)
Cited for: VARIANTS FA7D GLN-73; GLN-79; PHE-121; PRO-125; CYS-128; TRP-139; SER-151; VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302; THR-304; VAL-304; CYS-307; MET-332; VAL-354; ILE-358; PHE-370; GLY-389; SER-391 AND GLU-435;
Disclaimer:
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.