Aliases for ATP6V0E2 Gene
External Ids for ATP6V0E2 Gene
Previous HGNC Symbols for ATP6V0E2 Gene
Previous GeneCards Identifiers for ATP6V0E2 Gene
Multisubunit vacuolar-type proton pumps, or H(+)-ATPases, acidify various intracellular compartments, such as vacuoles, clathrin-coated and synaptic vesicles, endosomes, lysosomes, and chromaffin granules. H(+)-ATPases are also found in plasma membranes of specialized cells, where they play roles in urinary acidification, bone resorption, and sperm maturation. Multiple subunits form H(+)-ATPases, with proteins of the V1 class hydrolyzing ATP for energy to transport H+, and proteins of the V0 class forming an integral membrane domain through which H+ is transported. ATP6V0E2 encodes an isoform of the H(+)-ATPase V0 e subunit, an essential proton pump component (Blake-Palmer et al., 2007 [PubMed 17350184]).[supplied by OMIM, Mar 2008]
GeneCards Summary for ATP6V0E2 Gene
ATP6V0E2 (ATPase, H+ Transporting V0 Subunit E2) is a Protein Coding gene. Diseases associated with ATP6V0E2 include osteopetrosis. 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 and ATPase activity, coupled to transmembrane movement of ions. An important paralog of this gene is ATP6V0E1.
UniProtKB/Swiss-Prot for ATP6V0E2 Gene
Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
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.