Aliases for ATP6V1D Gene
- ATPase, H+ Transporting, Lysosomal 34kDa, V1 Subunit D 2 3
- ATPase, H+ Transporting, Lysosomal (Vacuolar Proton Pump) 2 3
- V-ATPase 28 KDa Accessory Protein 3 4
- Vacuolar Proton Pump Subunit D 3 4
- V-ATPase Subunit D 3 4
- ATP6M 3 4
- VATD 3 4
- H(+)-Transporting Two-Sector ATPase, Subunit M 3
- ATPase, H+ Transporting Lysosomal, Member M 3
External Ids for ATP6V1D Gene
Previous Symbols for ATP6V1D Gene
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes the V1 domain D subunit protein. [provided by RefSeq, Jul 2008]
GeneCards Summary for ATP6V1D Gene
ATP6V1D (ATPase, H+ Transporting, Lysosomal 34kDa, V1 Subunit D) 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, coupled to transmembrane movement of substances.
UniProtKB/Swiss-Prot for ATP6V1D Gene
Subunit of the peripheral V1 complex of vacuolar ATPase. 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). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium.
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.