DefinitionThis section has been translated automatically.
The ATP6VOA2 gene, also called ATPase H+ Transporting V0 Subunit A2 (see synonym) is a subunit of vacuolar ATPase (v-ATPase), a heteromultimeric enzyme present in intracellular vesicles and in the plasma membrane of specialized cells and essential for the pH gradient (acidification) and glycolysis of various cellular components (Guillard M et al. (2009). V-ATPases are ATP-dependent proton pumps with several subunits located in membranes of cells and organelles. The gene encodes the a2 subunit of the vacuolar H (+) - ATPase (V-ATPase). mutations in the ATP6V0A2 gene. The glycosylation of proteins is one of the most important posttranslational modifications. Mutations in this gene Functional processes related to this gene include ATPase binding and proton transport ATPase activity, rotation mechanism (Miles AL et al. 2017). An important paralogue of this gene is ATP6V0A1.
Clinical pictureThis section has been translated automatically.
Defects in glycan biosynthesis lead to congenital malformation syndromes, also known as congenital glycosylation disorders (CDG). In patients with autosomal recessive cutis laxa type 2A (ARCL 2A), also known as wrinkly skin syndrome, a combined defect of N- and O-glycosylation has been identified. (Guillard M et al. 2009).
LiteratureThis section has been translated automatically.
- Guillard M et al (2009) Vacuolar H+-ATPase meets glycosylation in patients with cutis laxa. Biochim Biophys Acta 1792:903-914.
- Miles AL et al (2017) The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1α prolyl hydroxylation by regulating cellular iron levels. Elife pii: e22693. doi: 10.7554/eLife.22693.