Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
17  structures 1012  species 1  interaction 1179  sequences 2  architectures

Family: ATP-synt_F (PF01990)

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

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

ATP6V1F Edit Wikipedia article

ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F
Identifiers
Symbols ATP6V1F; ATP6S14; VATF; Vma7
External IDs OMIM607160 MGI1913394 HomoloGene3119 GeneCards: ATP6V1F Gene
EC number 3.6.3.14
RNA expression pattern
PBB GE ATP6V1F 201527 at tn.png
More reference expression data
Orthologs
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:
128.5 – 128.51 Mb
Chr 6:
29.47 – 29.47 Mb
PubMed search [1] [2]
ATP-synt_F
Identifiers
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]

References[edit]

  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[edit]


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 vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
  • 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.

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 [PUBMED:11309608, PUBMED:15629643, PUBMED: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 entry represents subunit F found in the V1 complex of V-ATPases (both eukaryotic and bacterial), as well as in the A1 complex of A-ATPases. 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].

More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].

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...

Loading domain graphics...

Alignments

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

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.

  Seed
(100)
Full
(1179)
Representative proteomes NCBI
(861)
Meta
(109)
RP15
(171)
RP35
(280)
RP55
(387)
RP75
(454)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(100)
Full
(1179)
Representative proteomes NCBI
(861)
Meta
(109)
RP15
(171)
RP35
(280)
RP55
(387)
RP75
(454)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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.

  Seed
(100)
Full
(1179)
Representative proteomes NCBI
(861)
Meta
(109)
RP15
(171)
RP35
(280)
RP55
(387)
RP75
(454)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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...

Trees

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: Enright A
Previous IDs: none
Type: Family
Author: Enright A, Ouzounis C, Bateman A
Number in seed: 100
Number in full: 1179
Average length of the domain: 94.90 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 86.32 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 23.5
Trusted cut-off 23.5 23.5
Noise cut-off 23.4 23.2
Model length: 95
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

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...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Interactions

There is 1 interaction for this family. More...

ATP-synt_F

Structures

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 17 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.

Loading structure mapping...