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UniProtKB/Swiss-Prot P06681: Variant p.Glu318Asp

Complement C2
Gene: C2
Chromosomal location: 6p21.3
Variant information

Variant position:  318
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
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 Glutamate (E) to Aspartate (D) at position 318 (E318D, p.Glu318Asp).
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 acidic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  2
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

Polymorphism:  The variant Asp-318 is associated with a reduced risk of age-related macular degeneration (ARMD) [MIM:603075]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world.
Additional information on the polymorphism described.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  318
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  752
The length of the canonical sequence.

Location on the sequence:   FASEPKVLMSVLNDNSRDMT  E VISSLENANYKDHENGTGTN
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                         FASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTN

Gorilla                       FASKPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTN

Chimpanzee                    FASEPRVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTN

Mouse                         FASQPKTIMSILSERSQDVTEVITSLDSASYKDHENATGTN

Bovine                        FASKPKIIMSVLEDRSRDVTEVENSLRNINYKDHENGTGTN

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.

TypePositionsDescription
Chain 21 – 752 Complement C2
Chain 244 – 752 Complement C2a fragment
Domain 254 – 452 VWFA
Metal binding 337 – 337 Divalent metal cation
Glycosylation 333 – 333 N-linked (GlcNAc...) asparagine
Alternative sequence 238 – 328 Missing. In isoform 2.
Helix 316 – 324


Literature citations

Submission
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS ASP-318 AND CYS-734;

Variation in factor B (BF) and complement component 2 (C2) genes is associated with age-related macular degeneration.
Gold B.; Merriam J.E.; Zernant J.; Hancox L.S.; Taiber A.J.; Gehrs K.; Cramer K.; Neel J.; Bergeron J.; Barile G.R.; Smith R.T.; Hageman G.S.; Dean M.; Allikmets R.;
Nat. Genet. 38:458-462(2006)
Cited for: VARIANT ASP-318; INVOLVEMENT IN REDUCED RISK OF ARMD;

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.