InterPro : IPR016727

Name  ATPase, V0 complex, subunit d Short Name  ATPase_V0-cplx_dsu
Type  Family 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 [, ]. The different types include:F-ATPases (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 eukaryotic and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane []. They are also found in bacteria [].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 [, ].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.V-ATPases (also known as V1V0-ATPase or vacuolar ATPase) () 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 []. 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 [].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 [, , ]. 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 entry represents subunit d from the V0 complex of V-ATPases, which are involved in the translocation of protons across a membrane. There is more than one type of d subunit in V-ATPases, where the D1 subunit is ubiquitous, while the D2 subunit has limited tissue expressivity, possibly to account for differential functions, targeting or regulation of V-ATPase activity [].
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Id Name Short Name Type
IPR002843 ATPase, V0 complex, c/d subunit ATPase_V0-cplx_csu/dsu Family

11 Publications

First Author Title Year Journal Volume Pages
Yasuda R Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. 2001 Nature 410 898-904
Cross RL The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. 2004 FEBS Lett 576 1-4
Rappas M Mechanisms of ATPases--a multi-disciplinary approach. 2004 Curr Protein Pept Sci 5 89-105
Toei M Regulation and isoform function of the V-ATPases. 2010 Biochemistry 49 4715-23
Grüber G New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). 2008 Bioessays 30 1096-109
Schäfer G F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. 1992 Biochim Biophys Acta 1101 232-5
Radax C F-and V-ATPases in the genus Thermus and related species. 1998 Syst Appl Microbiol 21 12-22
Wilkens S A structural model of the vacuolar ATPase from transmission electron microscopy. 2005 Micron 36 109-26
Bajjalieh S A new view of an old pore. 2005 Cell 121 496-7
Müller V An exceptional variability in the motor of archael A1A0 ATPases: from multimeric to monomeric rotors comprising 6-13 ion binding sites. 2004 J Bioenerg Biomembr 36 115-25
Smith AN Vacuolar H+-ATPase d2 subunit: molecular characterization, developmental regulation, and localization to specialized proton pumps in kidney and bone. 2005 J Am Soc Nephrol 16 1245-56



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)