The domain within your query sequence starts at position 4 and ends at position 427; the E-value for the V-ATPase_C domain shown below is 3.9e-156.



PFAM accession number:PF03223
Interpro abstract (IPR004907):




V-ATPases (also known as V1V0-ATPase or vacuolar ATPase) (EC are found in the eukaryotic endomembrane system, and in the plasma membrane of prokaryotes and certain specialised eukaryotic cells. V-ATPases hydrolyse ATP to drive a proton pump, and are involved in a variety of vital intra- and inter-cellular processes such as receptor mediated endocytosis, protein trafficking, active transport of metabolites, homeostasis and neurotransmitter release [(PUBMED:15629643)]. V-ATPases are composed of two linked complexes: the V1 complex (subunits A-H) contains the catalytic core that hydrolyses ATP, while the V0 complex (subunits a, c, c', c'', d) forms the membrane-spanning pore. V-ATPases may have an additional role in membrane fusion through binding to t-SNARE proteins [(PUBMED:15907459)].

This entry represents the C subunit that is part of the V1 complex, and is localised to the interface between the V1 and V0 complexes [(PUBMED:15951435)]. This subunit does not show any homology with F-ATPase subunits. The C subunit plays an essential role in controlling the assembly of V-ATPase, acting as a flexible stator that holds together the catalytic (V1) and membrane (V0) sectors of the enzyme [(PUBMED:15540116)]. The release of subunit C from the ATPase complex results in the dissociation of the V1 and V0 subcomplexes, which is an important mechanism in controlling V-ATPase activity in cells.

GO process:ATP hydrolysis coupled proton transport (GO:0015991)
GO component:proton-transporting V-type ATPase, V1 domain (GO:0033180)
GO function:proton transmembrane transporter activity (GO:0015078)
