UniProtKB/SwissProt variant VAR

Variant information

Variant position:

125

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

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:

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:

-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:

In FA7D.

Any additional useful information about the variant.

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                         SDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHK

Chimpanzee                    SDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETYK

Mouse                         SDGDQCASNPCQNGGTCQDHLKSYVCFCLLDFEGRNCEKSK

Rat                           SDGDQCASNPCQNGGTCQDHLKSYVCFCPLDFEGRNCEKNK

Bovine                        NDGDQCASSPCQNGGSCEDQLRSYICFCPDGFEGRNCETDK

Rabbit                        NDGDQCASNPCQNGGSCEDQIQSYICFCLADFEGRNCEKNK

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;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08709: Variant p.Leu125Pro