This target displays homology in the following species: Cow: 100%; Dog: 100%; Guinea Pig: 100%; Horse: 100%; Human: 100%; Mouse: 100%; Rabbit: 100%; Rat: 100%; Zebrafish: 93%
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.
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Protein Aliases: ATPase, H+ transporting V0 subunit e2; H+-ATPase e2 subunit; Lysosomal 9 kDa H(+)-transporting ATPase V0 subunit e2; V-ATPase subunit e 2; V-type proton ATPase subunit e 2; Vacuolar proton pump subunit e 2; vacuolar proton-ATPase subunit
Gene Aliases: ATP6V0E2; ATP6V0E2L; C7orf32
UniProt ID: (Human) Q8NHE4
Entrez Gene ID: (Human) 155066