Aliases for ATP6V1H Gene
- ATPase, H+ Transporting, Lysosomal 50/57kDa, V1 Subunit H 2 3
- Vacuolar Proton Pump Subunit SFD 3 4
- Vacuolar ATP Synthase Subunit H 2 3
- Vacuolar Proton Pump Subunit H 3 4
- V-ATPase 50/57 KDa Subunits 3 4
- Nef-Binding Protein 1 3 4
- Protein VMA13 Homolog 3 4
- V-ATPase Subunit H 3 4
- NBP1 3 4
- ATPase, H+ Transporting, Lysosomal 50/57kD, V1 Subunit H 2
External Ids for ATP6V1H Gene
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular organelles. V-ATPase-dependent organelle acidification is necessary for multiple processes including protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. The encoded protein is the regulatory H subunit of the V1 domain of V-ATPase, which is required for catalysis of ATP but not the assembly of V-ATPase. Decreased expression of this gene may play a role in the development of type 2 diabetes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 2012]
GeneCards Summary for ATP6V1H Gene
ATP6V1H (ATPase, H+ Transporting, Lysosomal 50/57kDa, V1 Subunit H) is a Protein Coding gene. Among its related pathways are Signaling by GPCR and Insulin receptor signalling cascade. GO annotations related to this gene include ATPase activity and enzyme regulator activity.
UniProtKB/Swiss-Prot for ATP6V1H Gene
Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes.
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.