Family

ATPase, V1 complex, subunit D (IPR002699)

Short name: V_ATPase_D

Family relationships

None.

Description

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [PMID: 15473999, PMID: 15078220]. The different types include:

  • F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [PMID: 20450191]. They are also found in bacteria [PMID: 9741106].
  • A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [PMID: 18937357, PMID: 1385979].
  • P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

The V-ATPases (or V1V0-ATPase) and A-ATPases (or A1A0-ATPase) are each composed of two linked complexes: the V1 or A1 complex contains the catalytic core that hydrolyses/synthesizes ATP, and the V0 or A0 complex that forms the membrane-spanning pore. The V- and A-ATPases both contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [PMID: 11309608, PMID: 15629643, PMID: 15168615]. The V- and A-ATPases more closely resemble one another in subunit structure than they do the F-ATPases, although the function of A-ATPases is closer to that of F-ATPases.

This is a family of D subunits from various ATP synthases, including V-type H+ transporting and Na+ transporting [PMID: 8157629]. This family is found in eukaryota, bacteria and archaea [PMID: 10788522, PMID: 9177272]. The V-type ATPase can use a proton gradient to synthesize ATP, but the primary biological role is to acidify some compartment, such as yeast vacuole (a lysosomal homologous) or the interior of a prokaryote. Subunit D is suggested to be an integral part of the catalytic sector of the V-ATPase [PMID: 7831318].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0042626 ATPase activity, coupled to transmembrane movement of substances

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam
HAMAP
TIGRFAMs
PANTHER