TCDB is operated by the Saier Lab Bioinformatics Group
TRANSPORTERS FROM HUMANS:
Transporter Information:
Name: ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D
Symbol: ATP6V1D
TC: 3.A.2.2.3
Locations: 14q23-q24.2
Aliases: VATD, VMA8
GenBank: AF145316
Swiss-Prot: Q9Y5K8
Accession Number: NM_015994
Old Name: ATPase, H+ transporting, lysosomal (vacuolar proton pump)
GDBGDB:11505653
LocusLink51382
PubMed (9442887): Stevens TH, Forgac M. Structure, function and regulation of the vacuolar (H+)-ATPase.Annu Rev Cell Dev Biol. 1997;13:779-808. Review. PMID: 9442887 [PubMed - indexed for MEDLINE]

The vacuolar (H+)-ATPases (or V-ATPases) function in the acidification of intracellular compartments in eukaryotic cells. The V-ATPases are multisubunit complexes composed of two functional domains. The peripheral V1 domain, a 500-kDa complex responsible for ATP hydrolysis, contains at least eight different subunits of molecular weight 70-13 (subunits A-H). The integral V0 domain, a 250-kDa complex, functions in proton translocation and contains at least five different subunits of molecular weight 100-17 (subunits a-d). Biochemical and genetic analysis has been used to identify subunits and residues involved in nucleotide binding and hydrolysis, proton translocation, and coupling of these activities. Several mechanisms have been implicated in the regulation of vacuolar acidification in vivo, including control of pump density, regulation of assembly of V1 and V0 domains, disulfide bond formation, activator or inhibitor proteins, and regulation of counterion conductance. Recent information concerning targeting and regulation of V-ATPases has also been obtained.