Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08709: Variant p.Leu125Pro

Coagulation factor VII
Gene: F7
Feedback?
Variant information Variant position: help 125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Leucine (L) to Proline (P) at position 125 (L125P, p.Leu125Pro). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In FA7D. Any additional useful information about the variant.


Sequence information Variant position: help 125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 466 The length of the canonical sequence.
Location on the sequence: help 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         SDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHK

Chimpanzee                    SDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETYK

Mouse                         SDGDQCASNPCQNGGTCQDHLKSYVCFCLLDFEGRNCEKSK

Rat                           SDGDQCASNPCQNGGTCQDHLKSYVCFCPLDFEGRNCEKNK

Bovine                        NDGDQCASSPCQNGGSCEDQLRSYICFCPDGFEGRNCETDK

Rabbit                        NDGDQCASNPCQNGGSCEDQIQSYICFCLADFEGRNCEKNK
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
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.