Total submissions: 3
| Submitter | RCV | SCV | Clinical significance | Condition | Last evaluated | Review status | Method | Comment |
|---|---|---|---|---|---|---|---|---|
| Ce |
RCV000585246 | SCV000693056 | uncertain significance | not provided | 2017-08-01 | criteria provided, single submitter | clinical testing | |
| Invitae | RCV001853162 | SCV002187431 | pathogenic | Arterial tortuosity syndrome | 2023-05-05 | criteria provided, single submitter | clinical testing | For these reasons, this variant has been classified as Pathogenic. This variant disrupts the p.Arg105 amino acid residue in SLC2A10. Other variant(s) that disrupt this residue have been determined to be pathogenic (PMID: 18774132, 29323665; Invitae). This suggests that this residue is clinically significant, and that variants that disrupt this residue are likely to be disease-causing. Advanced modeling of protein sequence and biophysical properties (such as structural, functional, and spatial information, amino acid conservation, physicochemical variation, residue mobility, and thermodynamic stability) performed at Invitae indicates that this missense variant is expected to disrupt SLC2A10 protein function. ClinVar contains an entry for this variant (Variation ID: 213726). This missense change has been observed in individuals with arterial tortuosity syndrome (PMID: 28726533, 29323665). This variant is present in population databases (rs753280877, gnomAD 0.01%), including at least one homozygous and/or hemizygous individual. This sequence change replaces arginine, which is basic and polar, with histidine, which is basic and polar, at codon 105 of the SLC2A10 protein (p.Arg105His). |
| Ambry Genetics | RCV002321792 | SCV002608601 | uncertain significance | Familial thoracic aortic aneurysm and aortic dissection | 2022-02-22 | criteria provided, single submitter | clinical testing | The p.R105H variant (also known as c.314G>A), located in coding exon 2 of the SLC2A10 gene, results from a G to A substitution at nucleotide position 314. The arginine at codon 105 is replaced by histidine, an amino acid with highly similar properties. This variant was reported in two individuals from an arterial tortuosity cohort, both of whom had a second SLCC2A10 variant detected (Beyens A et al. Genet Med, 2018 10;20:1236-1245; Hardin JS et al. Ophthalmic Genet Jul;39:29-34). This amino acid position is highly conserved in available vertebrate species. In addition, this alteration is predicted to be deleterious by in silico analysis. Since supporting evidence is limited at this time, the clinical significance of this alteration remains unclear. |