ATP6V1F

ATP6V1F
Identifiers
Aliases	ATP6V1F, ATP6S14, VATF, Vma7, ATPase H+ transporting V1 subunit F
External IDs	MGI: 1913394 HomoloGene: 3119 GeneCards: ATP6V1F
Gene ontology Molecular function • ATPase activity, uncoupled • protein binding • proton-transporting ATPase activity, rotational mechanism • hydrogen ion transmembrane transporter activity • ATPase coupled ion transmembrane transporter activity Cellular component • proton-transporting V-type ATPase, V1 domain • cytosol • proton-transporting two-sector ATPase complex • vacuolar proton-transporting V-type ATPase complex • membrane • extracellular exosome Biological process • insulin receptor signaling pathway • ATP hydrolysis coupled proton transport • ion transport • transferrin transport • transport • proton transport • phagosome acidification • ion transmembrane transport Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9296	66144
Ensembl	ENSG00000128524	ENSMUSG00000004285
UniProt	Q16864	Q9D1K2
RefSeq (mRNA)	NM_004231 NM_001198909	NM_025381
RefSeq (protein)	NP_001185838.1 NP_004222.2	NP_079657.1
Location (UCSC)	Chr 7: 128.86 – 128.87 Mb	Chr 6: 29.47 – 29.47 Mb
PubMed search	[1]	[2]
Wikidata

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ATP-synt_F
Identifiers
Symbol	ATP-synt_F
Pfam	PF01990
InterPro	IPR008218
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

V-type proton ATPase subunit F is an enzyme that in humans is encoded by the ATP6V1F gene.^[3][4][5]

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.^[5]

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.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. 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.
5. "Entrez Gene: ATP6V1F ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F".
6. 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

• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 324 (3): 697–712. doi:10.1042/bj3240697. PMC 1218484. PMID 9210392.
• Stevens TH, Forgac M (1998). "Structure, function and regulation of the vacuolar (H+)-ATPase". Annu. Rev. Cell Dev. Biol. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
• Nelson N, Harvey WR (1999). "Vacuolar and plasma membrane proton-adenosinetriphosphatases". Physiol. Rev. 79 (2): 361–85. PMID 10221984.
• Forgac M (1999). "Structure and properties of the vacuolar (H+)-ATPases". J. Biol. Chem. 274 (19): 12951–4. doi:10.1074/jbc.274.19.12951. PMID 10224039.
• Kane PM (1999). "Introduction: V-ATPases 1992-1998". J. Bioenerg. Biomembr. 31 (1): 3–5. doi:10.1023/A:1001884227654. PMID 10340843.
• Wieczorek H, Brown D, Grinstein S, et al. (1999). "Animal plasma membrane energization by proton-motive V-ATPases". BioEssays. 21 (8): 637–48. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860.
• Nishi T, Forgac M (2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511.
• Kawasaki-Nishi S, Nishi T, Forgac M (2003). "Proton translocation driven by ATP hydrolysis in V-ATPases". FEBS Lett. 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
• Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase". Biol. Cell. 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
• Cross SH, Charlton JA, Nan X, Bird AP (1994). "Purification of CpG islands using a methylated DNA binding column". Nat. Genet. 6 (3): 236–44. doi:10.1038/ng0394-236. PMID 8012384.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

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