ClinVar Miner

Submissions for variant NM_000090.4(COL3A1):c.1745G>A (p.Gly582Asp)

dbSNP: rs1688322272
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Total submissions: 1
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Submitter RCV SCV Clinical significance Condition Last evaluated Review status Method Comment
Labcorp Genetics (formerly Invitae), Labcorp RCV001056189 SCV001220616 likely pathogenic Ehlers-Danlos syndrome, type 4 2019-03-03 criteria provided, single submitter clinical testing 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, variants that affect these glycine residues are significantly enriched in individuals with disease (PMID: 24922459, 25758994) compared to the general population (ExAC). In summary, the currently available evidence indicates that the variant is pathogenic, but additional data are needed to prove that conclusively. Therefore, this variant has been classified as Likely Pathogenic. This variant has not been reported in the literature in individuals with COL3A1-related conditions. This variant is not present in population databases (ExAC no frequency). This sequence change replaces glycine with aspartic acid at codon 582 of the COL3A1 protein (p.Gly582Asp). The glycine residue is highly conserved and there is a moderate physicochemical difference between glycine and aspartic acid.

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