Total submissions: 1
Submitter | RCV | SCV | Clinical significance | Condition | Last evaluated | Review status | Method | Comment |
---|---|---|---|---|---|---|---|---|
Labcorp Genetics |
RCV000705647 | SCV000834654 | pathogenic | Ehlers-Danlos syndrome, type 4 | 2018-02-08 | criteria provided, single submitter | clinical testing | Algorithms developed to predict the effect of missense changes on protein structure and function do not agree on the potential impact of this missense change (SIFT: "Deleterious"; PolyPhen-2: "Probably Damaging"; Align-GVGD: "Class C0"). Other missense substitutions at this codon (p.Gly501Ala and p.Gly501Arg) have been reported in individuals with suspected Ehlers-Danlos syndrome, type IV (PMID:10706896 and 22038052). Glycine residues within the Gly-Xaa-Yaa repeats of the triple helix domain are required for the structure and stability of fibrillar collagens (PMID: 7695699, 8218237, 19344236). In COL3A1, missense variants at these glycine residues are significantly enriched in individuals with disease (PMID: 24922459, 25758994) compared to the general population (ExAC). For these reasons, this variant has been classified as Pathogenic. This variant has been observed to be de novo in an affected individual tested at a diagnostic lab. This variant is not present in population databases (ExAC no frequency). This sequence change replaces glycine with glutamic acid at codon 501 of the COL3A1 protein (p.Gly501Glu). The glycine residue is highly conserved and there is a moderate physicochemical difference between glycine and glutamic acid. |