ATP6V1F
From Wikipedia, the free encyclopedia
ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F
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Identifiers | ||||||||||||||
Symbol(s) | ATP6V1F; ATP6S14; MGC117321; MGC126037; MGC126038; VATF; Vma7 | |||||||||||||
External IDs | OMIM: 607160 MGI: 1913394 HomoloGene: 3119 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 9296 | 66144 | ||||||||||||
Ensembl | ENSG00000128524 | ENSMUSG00000004285 | ||||||||||||
Uniprot | Q16864 | Q9D1K2 | ||||||||||||
Refseq | NM_004231 (mRNA) NP_004222 (protein) |
NM_025381 (mRNA) NP_079657 (protein) |
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Location | Chr 7: 128.29 - 128.29 Mb | Chr 6: 29.42 - 29.42 Mb | ||||||||||||
Pubmed search | [1] | [2] |
ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F, also known as ATP6V1F, is a human gene.[1]
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.[1]
[edit] References
[edit] Further reading
- Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 ( Pt 3): 697–712. 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: . 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. PMID 10224039.
- Kane PM (1999). "Introduction: V-ATPases 1992-1998.". J. Bioenerg. Biomembr. 31 (1): 3–5. 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: . 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: . 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. PMID 12788495.
- Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453–7. 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: . PMID 8012384.
- Fujiwara T, Kawai A, Shimizu F, et al. (1996). "Cloning, sequencing and expression of a novel cDNA encoding human vacuolar ATPase (14-kDa subunit).". DNA Res. 2 (3): 107–11. PMID 8581736.
- Peng SB, Crider BP, Tsai SJ, et al. (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. PMID 8621738.
- 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: . PMID 12477932.