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28  structures 2653  species 4  interactions 2961  sequences 6  architectures

Family: ATP-synt_F (PF01990)

Summary: ATP synthase (F/14-kDa) subunit

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This is the Wikipedia entry entitled "ATP6V1F". More...

ATP6V1F Edit Wikipedia article

ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F
Symbols ATP6V1F ; ATP6S14; VATF; Vma7
External IDs OMIM607160 MGI1913394 HomoloGene3119 IUPHAR: 818 GeneCards: ATP6V1F Gene
EC number
RNA expression pattern
PBB GE ATP6V1F 201527 at tn.png
More reference expression data
Species Human Mouse
Entrez 9296 66144
Ensembl ENSG00000128524 ENSMUSG00000004285
UniProt Q16864 Q9D1K2
RefSeq (mRNA) NM_001198909 NM_025381
RefSeq (protein) NP_001185838 NP_079657
Location (UCSC) Chr 7:
128.86 – 128.87 Mb
Chr 6:
29.47 – 29.47 Mb
PubMed search [1] [2]
Symbol ATP-synt_F
Pfam PF01990
InterPro IPR008218

V-type proton ATPase subunit F is an enzyme that in humans is encoded by the ATP6V1F gene.[1][2][3]

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is the V1 domain F subunit protein.[3]

Subunit F is a 16 kDa protein that is required for the assembly and activity of V-ATPase, and has a potential role in the differential targeting and regulation of the enzyme for specific organelles. This subunit is not necessary for the rotation of the ATPase V1 rotor, but it does promote catalysis.[4]


  1. ^ Fujiwara T, Kawai A, Shimizu F, Hirano H, Okuno S, Takeda S, Ozaki K, Shimada Y, Nagata M, Watanabe T; et al. (Mar 1996). "Cloning, sequencing and expression of a novel cDNA encoding human vacuolar ATPase (14-kDa subunit)". DNA Res 2 (3): 107–11. doi:10.1093/dnares/2.3.107. PMID 8581736. 
  2. ^ Peng SB, Crider BP, Tsai SJ, Xie XS, Stone DK (Jun 1996). "Identification of a 14-kDa subunit associated with the catalytic sector of clathrin-coated vesicle H+-ATPase". J Biol Chem 271 (6): 3324–7. doi:10.1074/jbc.271.6.3324. PMID 8621738. 
  3. ^ a b "Entrez Gene: ATP6V1F ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F". 
  4. ^ Imamura H, Ikeda C, Yoshida M, Yokoyama K (April 2004). "The F subunit of Thermus thermophilus V1-ATPase promotes ATPase activity but is not necessary for rotation". J. Biol. Chem. 279 (17): 18085–90. doi:10.1074/jbc.M314204200. PMID 14963028. 

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR008218

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.

ATP synthase (F/14-kDa) subunit Provide feedback

This family includes 14-kDa subunit from vATPases [1] which is in the peripheral catalytic part of the complex [2]. The family also includes archaebacterial ATP synthase subunit F [3].

Literature references

  1. Guo Y, Kaiser K, Wieczorek H, Dow JA; , Gene 1996;172:239-243.: The Drosophila melanogaster gene vha14 encoding a 14-kDa F-subunit of the vacuolar ATPase. PUBMED:8682310 EPMC:8682310

  2. Peng SB, Crider BP, Tsai SJ, Xie XS, Stone DK; , J Biol Chem 1996;271:3324-3327.: Identification of a 14-kDa subunit associated with the catalytic sector of clathrin-coated vesicle H+-ATPase. PUBMED:8621738 EPMC:8621738

  3. Wilms R, Freiberg C, Wegerle E, Meier I, Mayer F, Muller V; , J Biol Chem 1996;271:18843-18852.: Subunit structure and organization of the genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Go1. PUBMED:8702544 EPMC:8702544

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008218

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 [PUBMED:15473999, PUBMED:15078220]. 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 [PUBMED:20450191]. They are also found in bacteria [PUBMED: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 [PUBMED:18937357, PUBMED: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.

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 subunit F in the V1 complex of V-ATPases and Na(+)-translocating ATPase in Enterococcus hirae. Subunit F is a 16 kDa protein that is required for the assembly and activity of V-ATPase, and has a potential role in the differential targeting and regulation of the enzyme for specific organelles. This subunit is not necessary for the rotation of the ATPase V1 rotor, but it does promote catalysis [PUBMED:14963028]. In Enterococcus hirae, Na(+)-translocating ATPase extrudes sodium ions from the cytoplasm and generates the Na+ electrochemical gradient by using the energy of ATP [PUBMED:11248190].

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Seed source: Enright A
Previous IDs: none
Type: Family
Author: Enright A, Ouzounis C, Bateman A
Number in seed: 322
Number in full: 2961
Average length of the domain: 92.30 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 85.16 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 23.5
Trusted cut-off 23.6 23.5
Noise cut-off 23.2 23.4
Model length: 91
Family (HMM) version: 13
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Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
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There are 4 interactions for this family. More...

vATP-synt_AC39 ATP-synt_F ATP-synt_ab_C ATP-synt_D


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 ATP-synt_F domain has been found. There are 28 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 seqence.

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