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92  structures 1457  species 0  interactions 2434  sequences 46  architectures

Family: V-ATPase_G (PF03179)

Summary: Vacuolar (H+)-ATPase G subunit

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V-ATPase Edit Wikipedia article

V-ATPase schematic
OPM superfamily5
OPM protein2bl2
V-ATPase, subunit c (Vo)
Membrane-spanning region of the V-type sodium ATPase from Enterococcus hirae. Calculated hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots
V-ATPase, subunit C (V1)
PDB 1u7l EBI.jpg
crystal structure of subunit C (vma5p) of the yeast v-atpase
V-ATPase, subunit I/a
V-ATPase, subunit E
Pfam clanCL0255
V-ATPase, subunit d/d2
PDB 1r5z EBI.jpg
crystal structure of subunit C (yeast subunit d) of v-atpase
V-ATPase, subunit H, N-terminal
PDB 1ho8 EBI.jpg
crystal structure of the regulatory subunit H of the v-type atpase of saccharomyces cerevisiae
Pfam clanCL0020
V-ATPase, subunit G
Pfam clanCL0255

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms.[1] V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.

The Archaea-type ATPase (A-ATPase) is a related group of ATPases found in Archaea that often work as an ATP synthase. It forms a clade V/A-ATPase with V-ATPase. Most members of either group shuttle protons (H+
), but a few members have evolved to use sodium ions (Na+
) instead.

Roles played by V-ATPases

V-ATPases are found within the membranes of many organelles, such as endosomes, lysosomes, and secretory vesicles, where they play a variety of roles crucial for the function of these organelles. For example, the proton gradient across the yeast vacuolar membrane generated by V-ATPases drives calcium uptake into the vacuole through an H+
antiporter system.[2] In synaptic transmission in neuronal cells, V-ATPase acidifies synaptic vesicles.[3] Norepinephrine enters vesicles by V-ATPase.

V-ATPases are also found in the plasma membranes of a wide variety of cells such as intercalated cells of the kidney, osteoclasts (bone resorbing cells), macrophages, neutrophils, sperm, midgut cells of insects, and certain tumor cells.[4] Plasma membrane V-ATPases are involved in processes such as pH homeostasis, coupled transport, and tumor metastasis. V-ATPases in the acrosomal membrane of sperm acidify the acrosome. This acidification activates proteases required to drill through the plasma membrane of the egg. V-ATPases in the osteoclast plasma membrane pump protons onto the bone surface, which is necessary for bone resorption. In the intercalated cells of the kidney, V-ATPases pump protons into the urine, allowing for bicarbonate reabsorption into the blood. In addition, other variety of biological processes, such as toxin delivery, viral entry, membrane targeting, apoptosis, regulation of cytoplasmic pH, proteolytic process, and acidification of intracellular systems, are important roles of V-ATPases.[5]

V-ATPases also play a significant role in cell morphogenesis development. Disruption of the gene vma-1 gene which encodes for the catalytic subunit (A) of the enzyme severely impairs the rate of growth, differentiation, and the capacity to produce viable spores in fungus Neurospora crassa. [6]


The yeast V-ATPase is the best characterized. There are at least thirteen subunits identified to form a functional V-ATPase complex, which consists of two domains. The subunits belong to either the Vo domain (membrane associated subunits, lowercase letters on the figure) or the V1 domain (peripherally associated subunits, uppercase letters on the figure).

The V1 includes eight subunits, A-H, with three copies of the catalytic A and B subunits, three copies of the stator subunits E and G, and one copy of the regulatory C and H subunits. In addition, the V1 domain also contains the subunits D and F, which form a central rotor axle.[7] The V1 domain contains tissue-specific subunit isoforms including B, C, E, and G. Mutations to the B1 isoform result in the human disease distal renal tubular acidosis and sensorineural deafness.

The Vo domain contains six different subunits, a, d, c, c', c", and e, with the stoichiometry of the c ring still a matter of debate with a decamer being postulated for the tobacco hornworm (Manduca sexta) V-ATPase. The mammalian Vo domain contains tissue-specific isoforms for subunits a and d, while yeast V-ATPase contains two organelle-specific subunit isoforms of a, Vph1p, and Stv1p. Mutations to the a3 isoform result in the human disease infantile malignant osteopetrosis, and mutations to the a4 isoform result in distal renal tubular acidosis, in some cases with sensorineural deafness.

The V1 domain is responsible for ATP hydrolysis, whereas the Vo domain is responsible for proton translocation. ATP hydrolysis at the catalytic nucleotide binding sites on subunit A drives rotation of a central stalk composed of subunits D and F, which in turn drives rotation of a barrel of c subunits relative to the a subunit. The complex structure of the V-ATPase has been revealed through the structure of the M. Sexta and Yeast complexes that were solved by single-particle cryo-EM and negative staining, respectively.[8][9][10] These structures have revealed that the V-ATPase has a 3-stator network, linked by a collar of density formed by the C, H, and a subunits, which, while dividing the V1 and Vo domains, make no interactions with the central rotor axle formed by the F, D, and d subunits. Rotation of this central rotor axle caused by the hydrolysis of ATP within the catalytic AB domains results in the movement of the barrel of c subunits past the a subunit, which drives proton transport across the membrane. A stoichiometry of two protons translocated for each ATP hydrolyzed has been proposed by Johnson.[11]

In addition to the structural subunits of yeast V-ATPase, associated proteins that are necessary for assembly have been identified. These associated proteins are essential for Vo domain assembly and are termed Vma12p, Vma21p, and Vma22p.[12][13][14][15] Two of the three proteins, Vma12p and Vma22p, form a complex that binds transiently to Vph1p (subunit a) to aid its assembly and maturation.[14][16][17][18] Vma21p coordinates assembly of the Vo subunits as well as escorting the Vo domain into vesicles for transport to the Golgi.[19]


The V1 domain of the V-ATPase is the site of ATP hydrolysis. Unlike Vo, the V1 domain is hydrophilic.[5] This soluble domain consists of a hexamer of alternating A and B subunits, a central rotor D, peripheral stators G and E, and regulatory subunits C and H. Hydrolysis of ATP drives a conformational change in the six A|B interfaces and with it rotation of the central rotor D. Unlike with the ATP synthase, the V1 domain is not an active ATPase when dissociated.

V1 Subunits[20]
Subunit Human Gene Note
A, B ATP6V1A, ATP6V1B1, ATP6V1B2 Catalytic hexamer.
D ATP6V1D Central rotor stalk, responsible for ion specificity.

Subunit C

V-ATPase (Vacuolar-ATPase) C represents the C terminal subunit that is part of the V1 complex, and is localised to the interface between the V1 and Vo complexes.[21]

Subunit C function

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 (VO) sectors of the enzyme .[22] The release of subunit C from the ATPase complex results in the dissociation of the V1 and Vo subcomplexes, which is an important mechanism in controlling V-ATPase activity in cells. Essentially, by creating a high electrochemical gradient and low pH, this powers the enzyme to create more ATP.

Subunits E, G

These related subunits make up the stalk(s) of A/V-ATPase. They are important in assembly, and may function as pushrods in activity. E has a cap to connect to A/B, while G does not.[20] They likely evolved from a single protein by gene duplication.[23]

Subunit H

This subunit is only involved in activity and not in assembly. This subunit also acts as an inhibitor of free V1 subunits; it stops ATP hydrolysis when V1 and Vo are dissociated.[24]


The Vo domain is responsible for proton translocation. Unlike the F-type ATP synthase, the Vo domain generally transports protons against their own concentration gradient. Rotation of the Vo domain transports the protons in movement coordinated with the V1 domain, which is responsible for ATP hydrolysis. The Vo domain is hydrophobic and composed of several dissociable subunits.[5] These subunits are present in the Vo domain to make this a functional proton translocase; they are described below.

Vo Subunits[20]
Subunit Human Gene Note
a/I ATP6V0A1, ATP6V0A2, ATP6V0A4
c ATP6V0B, ATP6V0C Ring of varied size.
d/C ATP6V0D1, ATP6V0D2
e ATP6V0E1, ATP6V0E2 9 kDa hydrophobic assembly protein.
AC45/S1 ATP6AP1 Accessory subunit
S2 ATP6AP2 Accessory subunit

Subunit a/I

The 116kDa subunit (or subunit a) and subunit I are found in the Vo or Ao complex of V- or A-ATPases, respectively. The 116kDa subunit is a transmembrane glycoprotein required for the assembly and proton transport activity of the ATPase complex. Several isoforms of the 116kDa subunit exist, providing a potential role in the differential targeting and regulation of the V-ATPase for specific organelles.

The function of the 116-kDa subunit is not defined, but its predicted structure consists of 6–8 transmembranous sectors, suggesting that it may function similar to subunit a of FO.

Subunit d/C

Subunit d in V-ATPases, called subunit C in A-ATpases, is a part of the Vo complex. They fit onto the middle of the c ring, so are thought to function as a rotor. There are two versions of this subunit in eukaryotes, d/d1 and d2.[25]

In mammals, d1 (ATP6V0D1) is the ubiquitously expressed version and d2 (ATP6V0D2) is expressed in specific cell types only.[25]

Subunit c

Similar to the F-type ATP synthase, the transmembrane region of the V-ATPase includes a ring of membrane-spanning subunits that are primarily responsible for proton translocation. Dissimilar from the F-type ATP synthase, however, the V-ATPase has multiple related subunits in the c-ring; in fungi such as yeast there are three related subunits (of varied stoichiometry) and in most other eukaryotes there are two.

V-ATPase assembly

Yeast V-ATPases fail to assemble when any of the genes that encode subunits are deleted except for subunits H and c".[26][27][28] Without subunit H, the assembled V-ATPase is not active,[13][29] and the loss of the c" subunit results in uncoupling of enzymatic activity.[27]

The precise mechanisms by which V-ATPases assembly are still controversial, with evidence suggesting two different possibilities. Mutational analysis and in vitro assays have shown that preassembled Vo and V1 domains can combine to form one complex in a process called independent assembly. Support for independent assembly includes the findings that the assembled Vo domain can be found at the vacuole in the absence of the V1 domain, whereas free V1 domains can be found in the cytoplasm and not at the vacuole.[30][31] In contrast, in vivo pulse-chase experiments have revealed early interactions between Vo and V1 subunits, to be specific, the a and B subunits, suggesting that subunits are added in a step-wise fashion to form a single complex in a concerted assembly process.[32]

V-ATPase evolution

A relatively new technique called ancestral gene resurrection has shed new light on the evolutionary history of the V-ATPase. It has been shown how the V-ATPase structure of the ancestral form consisting of two different proteins evolves into the fungi version with three different proteins.[33][34][35] The V-Type ATPase is similar to the archaeal (so called) A-Type ATP synthase, a fact that supports an archaeal origin of eukaryotes (like Eocyte Hypothesis, see also Lokiarchaeota). The exceptional occurrence of some lineages of archaea with F-type and of some lineages of bacteria with A-type ATPase respectively is regarded as a result of horizontal gene transfer.[36]

Regulation of V-ATPase activity

V-ATPases are known to be specifically inhibited by macrolide antibiotics, such as concanamycin (CCA) and balifomycin A1.[37] In vivo regulation of V-ATPase activity is accomplished by reversible dissociation of the V1 domain from the Vo domain. After initial assembly, both the insect Manduca sexta and yeast V-ATPases can reversibly disassemble into free Vo and V1 domains after a 2- to 5-minute deprivation of glucose.[30] Reversible disassembly may be a general mechanism of regulating V-ATPase activity, since it exists in yeast and insects. Reassembly is proposed to be aided by a complex termed RAVE (regulator of H+
-ATPase of vacuolar and endosomal membranes).[38] Disassembly and reassembly of V-ATPases does not require new protein synthesis but does need an intact microtubular network.[39]

Human diseases


Osteopetrosis is generic name that represents a group of heritable conditions in which there is a defect in osteoclastic bone resorption. Both dominant and recessive osteopetrosis occur in humans.[40][41] Autosomal dominant osteopetrosis shows mild symptoms in adults experiencing frequent bone fractures due to brittle bones.[40] A more severe form of osteopetrosis is termed autosomal recessive infantile malignant osteopetrosis.[41][42][43] Three genes that are responsible for recessive osteopetrosis in humans have been identified. They are all directly involved in the proton generation and secretion pathways that are essential for bone resorption. One gene is carbonic anhydrase II (CAII), which, when mutated, causes osteopetrosis with renal tubular acidosis(type 3).[44] Mutations to the chloride channel ClC7 gene also lead to both dominant and recessive osteopetrosis.[40] Approximately 50% of patients with recessive infantile malignant osteopetrosis have mutations to the a3 subunit isoform of V-ATPase.[42] [45][46] In humans, 26 mutations have been identified in V-ATPase subunit isoform a3, found in osteoclasts, that result in the bone disease autosomal recessive osteopetrosis.[42][41][45][47]

Distal renal tubular acidosis (dRTA)

The importance of V-ATPase activity in renal proton secretion is highlighted by the inherited disease distal renal tubular acidosis. In all cases, renal tubular acidosis results from a failure of the normal renal mechanisms that regulate systemic pH. There are four types of renal tubular acidosis. Type 1 is distal renal tubular acidosis and results from a failure of the cortical collecting duct to acidify the urine below pH 5.[48] Some patients with autosomal recessive dRTA also have sensorineural hearing loss.[49] Inheritance of this type of RTA results from either mutations to V-ATPase subunit isoform B1 or isoform a4 or mutations of band 3 (also called AE1), a Cl-/HCO3- exchanger.[49][50][51] Twelve different mutations to V-ATPase isoform B1[52] and twenty-four different mutations in a4 lead to dRTA.[52][49] Reverse transcription polymerase chain reaction studies have shown expression of the a4 subunit in the intercalated cell of the kidney and in the cochlea.[52] dRTA caused by mutations in the a4 subunit gene in some cases can be associated with deafness due to a failure to normally acidify the endolymph of the inner ear.[51]

X-linked myopathy with excessive autophagy (XMEA)

X-linked myopathy with excessive autophagy is a rare genetic disease resulting from mutations in the VMA21 gene.[53] The disease has a childhood onset and results in a slowly progressive muscle weakness, typically beginning in the legs, and some patients can eventually require wheelchair assistance with advanced age. The Vma21 protein assists in assembly of the V-ATPase, and XMEA associated mutations result in decreased activity of the V-ATPase and increased lysosomal pH.[53]


The term Vo has a lowercase letter "o" (not the number "zero") in subscript. The "o" stands for oligomycin, which binds to the homologous region in F-ATPase. It is worth noting that the human gene notations at NCBI designate it as "zero" rather than the letter "o". For example, the gene for the human c subunit of Vo is listed in NCBI gene database as "ATP6V0C" (with a zero), rather than "ATP6VOC" (with an "o"). Many pieces of literature make this mistake as well.

See also


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  6. ^ Bowman, E. J., & Bowman, B. J. (2000). Cellular role of the V-ATPase in Neurospora crassa: analysis of mutants resistant to concanamycin or lacking the catalytic subunit A. The Journal of experimental biology, 203(Pt 1), 97–106.
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  44. ^ Sly WS, Hewett-Emmett D, Whyte MP, Yu YS, Tashian RE (May 1983). "Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification". Proceedings of the National Academy of Sciences of the United States of America. 80 (9): 2752–6. Bibcode:1983PNAS...80.2752S. doi:10.1073/pnas.80.9.2752. PMC 393906. PMID 6405388.
  45. ^ a b Kornak U, Schulz A, Friedrich W, Uhlhaas S, Kremens B, Voit T, Hasan C, Bode U, Jentsch TJ, Kubisch C (August 2000). "Mutations in the a3 subunit of the vacuolar H(+)-ATPase cause infantile malignant osteopetrosis". Human Molecular Genetics. 9 (13): 2059–63. doi:10.1093/hmg/9.13.2059. PMID 10942435.
  46. ^ Frattini A, Pangrazio A, Susani L, Sobacchi C, Mirolo M, Abinun M, Andolina M, Flanagan A, Horwitz EM, Mihci E, Notarangelo LD, Ramenghi U, Teti A, Van Hove J, Vujic D, Young T, Albertini A, Orchard PJ, Vezzoni P, Villa A (October 2003). "Chloride channel ClCN7 mutations are responsible for severe recessive, dominant, and intermediate osteopetrosis". Journal of Bone and Mineral Research. 18 (10): 1740–7. doi:10.1359/jbmr.2003.18.10.1740. PMID 14584882. S2CID 20966489.
  47. ^ Susani L, Pangrazio A, Sobacchi C, Taranta A, Mortier G, Savarirayan R, Villa A, Orchard P, Vezzoni P, Albertini A, Frattini A, Pagani F (September 2004). "TCIRG1-dependent recessive osteopetrosis: mutation analysis, functional identification of the splicing defects, and in vitro rescue by U1 snRNA". Human Mutation. 24 (3): 225–35. doi:10.1002/humu.20076. PMID 15300850. S2CID 31788054.
  48. ^ Alper SL (2002). "Genetic diseases of acid-base transporters". Annual Review of Physiology. 64: 899–923. doi:10.1146/annurev.physiol.64.092801.141759. PMID 11826292.
  49. ^ a b c Karet FE, Finberg KE, Nelson RD, Nayir A, Mocan H, Sanjad SA, et al. (January 1999). "Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness". Nature Genetics. 21 (1): 84–90. doi:10.1038/5022. PMID 9916796. S2CID 34262548.
  50. ^ Karet FE, Gainza FJ, Györy AZ, Unwin RJ, Wrong O, Tanner MJ, et al. (May 1998). "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis". Proceedings of the National Academy of Sciences of the United States of America. 95 (11): 6337–42. Bibcode:1998PNAS...95.6337K. doi:10.1073/pnas.95.11.6337. PMC 27686. PMID 9600966.
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External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Vacuolar (H+)-ATPase G subunit Provide feedback

This family represents the eukaryotic vacuolar (H+)-ATPase (V-ATPase) G subunit. V-ATPases generate an acidic environment in several intracellular compartments. Correspondingly, they are found as membrane-attached proteins in several organelles. They are also found in the plasma membranes of some specialised cells. V-ATPases consist of peripheral (V1) and membrane integral (V0) heteromultimeric complexes. The G subunit is part of the V1 subunit, but is also thought to be strongly attached to the V0 complex. It may be involved in the coupling of ATP degradation to H+ translocation.

Literature references

  1. Forgac M; , FEBS Lett 1998;440:258-263.: Structure, function and regulation of the vacuolar (H+)-ATPases. PUBMED:9872382 EPMC:9872382

  2. Ratajczak R; , Biochim Biophys Acta 2000;1465:17-36.: Structure, function and regulation of the plant vacuolar H(+)-translocating ATPase. PUBMED:10748245 EPMC:10748245

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR005124

This family represents the eukaryotic vacuolar (H+)-ATPase (V-ATPase) G subunit. V-ATPases generate an acidic environment in several intracellular compartments. Correspondingly, they are found as membrane-attached proteins in several organelles. They are also found in the plasma membranes of some specialised cells. V-ATPases consist of peripheral (V1) and membrane integral (V0) heteromultimeric complexes. The G subunit is part of the V1 subunit, but is also thought to be strongly attached to the V0 complex. It may be involved in the coupling of ATP degradation to H+ translocation.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan ATP_synthase (CL0255), which has the following description:

This clan contains subunits of the F0 complex of ATP-synthase. The F0 complex is the non-catalytic unit of ATPase and is involved in proton translocation across membranes.

The clan contains the following 13 members:

ATP-synt_8 ATP-synt_B FliH Fun_ATP-synt_8 HrpE Mt_ATP-synt_B OSCP T3SS_SCTL V-ATPase_G V-ATPase_G_2 vATP-synt_E Yae1_N YMF19


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1274 (release 6.5)
Previous IDs: none
Type: Coiled-coil
Sequence Ontology: SO:0001080
Author: Mifsud W
Number in seed: 25
Number in full: 2434
Average length of the domain: 99.80 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 71.65 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 28.6 28.6
Trusted cut-off 28.6 28.6
Noise cut-off 28.4 28.5
Model length: 105
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the V-ATPase_G domain has been found. There are 92 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0G2K9C7 View 3D Structure Click here
A4I074 View 3D Structure Click here
A4QNE9 View 3D Structure Click here
B2GUV5 View 3D Structure Click here
B4FMV3 View 3D Structure Click here
C6SV85 View 3D Structure Click here
C6SWV2 View 3D Structure Click here
C6SZU9 View 3D Structure Click here
D3ZTZ4 View 3D Structure Click here
I1L620 View 3D Structure Click here
I1N484 View 3D Structure Click here
O74174 View 3D Structure Click here
O75348 View 3D Structure Click here
O82628 View 3D Structure Click here
O82629 View 3D Structure Click here
O82702 View 3D Structure Click here
O82703 View 3D Structure Click here
O95670 View 3D Structure Click here
P48836 View 3D Structure Click here
P78713 View 3D Structure Click here
P79251 View 3D Structure Click here
P91303 View 3D Structure Click here
Q1XHY9 View 3D Structure Click here
Q4CNF9 View 3D Structure Click here
Q4DE73 View 3D Structure Click here
Q54Z13 View 3D Structure Click here
Q59U85 View 3D Structure Click here
Q5TM18 View 3D Structure Click here
Q5WR09 View 3D Structure Click here
Q617N0 View 3D Structure Click here
Q6PBR5 View 3D Structure Click here
Q7FAM9 View 3D Structure Click here
Q862Z6 View 3D Structure Click here
Q8BMC1 View 3D Structure Click here
Q8IE84 View 3D Structure Click here
Q8R2H0 View 3D Structure Click here
Q96LB4 View 3D Structure Click here
Q9CR51 View 3D Structure Click here
Q9SZH0 View 3D Structure Click here
Q9TSV6 View 3D Structure Click here