Aliases for ATP6V0A2 Gene
- ATPase, H+ Transporting, Lysosomal V0 Subunit A2 2 3
- Lysosomal H(+)-Transporting ATPase V0 Subunit A2 3 4
- Infantile Malignant Osteopetrosis 2 2
- ARCL2A 3 6
- WSS 3 6
- TJ6 3 4
- Vacuolar Proton Translocating ATPase 116 KDa Subunit A Isoform 2 4
- ATPase, H+ Transporting, Lysosomal V0 Subunit A Isoform 2 2
- Vacuolar Proton Translocating ATPase 116 KDa Subunit A 3
- V-Type Proton ATPase 116 KDa Subunit A Isoform 2 3
- V-Type Proton ATPase 116 KDa Subunit A 3
- Regeneration And Tolerance Factor 3
- V-ATPase 116 KDa Isoform A2 4
External Ids for ATP6V0A2 Gene
The protein encoded by this gene is a subunit of the vacuolar ATPase (v-ATPase), an heteromultimeric enzyme that is present in intracellular vesicles and in the plasma membrane of specialized cells, and which is essential for the acidification of diverse cellular components. V-ATPase is comprised of a membrane peripheral V(1) domain for ATP hydrolysis, and an integral membrane V(0) domain for proton translocation. The subunit encoded by this gene is a component of the V(0) domain. Mutations in this gene are a cause of both cutis laxa type II and wrinkly skin syndrome. [provided by RefSeq, Jul 2009]
GeneCards Summary for ATP6V0A2 Gene
ATP6V0A2 (ATPase, H+ Transporting, Lysosomal V0 Subunit A2) is a Protein Coding gene. Diseases associated with ATP6V0A2 include wrinkly skin syndrome and atp6v0a2-related cutis laxa. Among its related pathways are Signaling by GPCR and Insulin receptor signalling cascade. GO annotations related to this gene include hydrogen ion transmembrane transporter activity. An important paralog of this gene is ATP6V0A1.
UniProtKB/Swiss-Prot for ATP6V0A2 Gene
Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH.
H+-ATPase (also known as vacuolar ATPase, V-ATPase) is a enzyme transporter that functions to acidify intracellular compartments in eukaryotic cells. It is ubiquitously expressed and is present in endomembrane organelles such as vacuoles, lysosomes, endosomes, the Golgi apparatus, chromaffin granules and coated vesicles, as well as in the plasma membrane. H+-ATPase is a multisubunit complex composed of two domains. The V1 domain is responsible for ATP hydrolysis and the V0 domain is responsible for protein translocation. There are two main mechanisms of regulating H+-ATPase activity; recycling of H+-ATPase-containing vesicles to and from the plasma membrane and glucose-sensitive assembly/disassembly of the holoenzyme complex. These transporters play an important role in processes such as receptor-mediated endocytosis, protein degradation and coupled transport. They have a function in bone reabsorption and mutations in the A3 gene cause recessive osteopetrosis. Furthermore, H+-ATPases have been implicated in tumor metastasis and regulation of sperm motility and maturation.