Protein Domain : IPR005725

Type:  Family Name:  ATPase, V1 complex, subunit A
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 [].This entry represents subunit A from the V1 complex of V-ATPases. There are three copies each of subunits A and B (), both of which participate in nucleotide binding. However, only subunit A is catalytic, functioning in ATP hydrolysis to drive the rotation of the D and F subunits of V1, as well as the V0 complex c-ring rotor subunit for proton translocation [, ]. Short Name:  ATPase_V1-cplx_asu
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0 Child Features

4 Contains

DB identifier Type Name
IPR000194 Domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
IPR000793 Domain ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
IPR004100 Domain ATPase, F1 complex alpha/beta subunit, N-terminal domain
IPR020003 Active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site

1 Cross References

Identifier
TIGR01042

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0046961 IPR005725
GO:0015991 IPR005725
GO:0033180 IPR005725

3 Ontology Annotations

GO Term Gene Name
GO:0046961 IPR005725
GO:0015991 IPR005725
GO:0033180 IPR005725

1 Parent Features

DB identifier Type Name
IPR022878 Family V-type ATP synthase catalytic alpha chain

610 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
167777 D8R3X7 PAC:15421544 Selaginella moellendorffii 591  
evm.model.supercontig_155.13 PAC:16409732 Carica papaya 623  
30169.m006261 B9RHV0 PAC:16821064 Ricinus communis 573  
Cucsa.359540.2 PAC:16980587 Cucumis sativus 547  
Cucsa.359540.1 A0A0A0K6R4 PAC:16980586 Cucumis sativus 623  
orange1.1g011655m A0A067DYZ6 PAC:18135579 Citrus sinensis 480  
orange1.1g010179m A0A067DVI5 PAC:18135578 Citrus sinensis 516  
AT1G78900.1 O23654 PAC:19655769 Arabidopsis thaliana 623  
AT1G78900.2 O23654 PAC:19655770 Arabidopsis thaliana 623  
Thhalv10018289m V4M7X4 PAC:20191118 Eutrema salsugineum 622  
Thhalv10018288m V4M7X4 PAC:20191117 Eutrema salsugineum 622  
Ciclev10030969m V4TDB5 PAC:20802476 Citrus clementina 623  
Lus10037321 PAC:23152489 Linum usitatissimum 623  
Lus10035737 PAC:23147584 Linum usitatissimum 623  
Lus10033382 PAC:23172081 Linum usitatissimum 639  
Lus10034836 PAC:23142249 Linum usitatissimum 623  
Potri.008G005000.3 A0A2K1Z9H7 PAC:27037484 Populus trichocarpa 587  
Potri.008G005000.1 B9HK35 PAC:27037483 Populus trichocarpa 623  
Potri.008G005000.2 PAC:27037485 Populus trichocarpa 547  
Potri.010G253500.1 B9HV14 PAC:26980284 Populus trichocarpa 623  
Potri.010G253500.2 A0A2K1Z063 PAC:26980285 Populus trichocarpa 582  
Gorai.009G119300.2 A0A0D2QE69 PAC:26771014 Gossypium raimondii 530  
Gorai.009G119300.1 A0A0D2UKJ6 PAC:26771013 Gossypium raimondii 623  
Gorai.011G002600.1 A0A0D2VGB5 PAC:26810655 Gossypium raimondii 623  
Gorai.011G002600.3 A0A0D2UM26 PAC:26810657 Gossypium raimondii 547  
Gorai.011G002600.4 A0A0D2T020 PAC:26810658 Gossypium raimondii 530  
Gorai.011G002600.2 A0A0D2UK48 PAC:26810656 Gossypium raimondii 590  
25960 I0YKZ3 PAC:27392891 Coccomyxa subellipsoidea C-169 618  
43849 C1MIH4 PAC:27344961 Micromonas pusilla CCMP1545 638  
59806 C1E9Q8 PAC:27404321 Micromonas sp RCC299 619  

9 Publications

First Author Title Year Journal Volume Pages PubMed ID
            15473999
            15078220
            9741106
            20450191
            18937357
            1385979
            15629643
            15907459
            11836511