Protein-coding gene in the species Homo sapiens
ATP6V1F |
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Identifiers |
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Aliases | ATP6V1F, ATP6S14, VATF, Vma7, ATPase H+ transporting V1 subunit F |
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External IDs | OMIM: 607160; MGI: 1913394; HomoloGene: 3119; GeneCards: ATP6V1F; OMA:ATP6V1F - orthologs |
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Gene location (Human) |
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![Chromosome 7 (human)](//upload.wikimedia.org/wikipedia/commons/thumb/9/99/Ideogram_human_chromosome_7.svg/300px-Ideogram_human_chromosome_7.svg.png) | Chr. | Chromosome 7 (human)[1] |
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| Band | 7q32.1 | Start | 128,862,856 bp[1] |
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End | 128,865,847 bp[1] |
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Gene location (Mouse) |
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![Chromosome 6 (mouse)](//upload.wikimedia.org/wikipedia/commons/thumb/c/c0/Ideogram_house_mouse_chromosome_6.svg/260px-Ideogram_house_mouse_chromosome_6.svg.png) | Chr. | Chromosome 6 (mouse)[2] |
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| Band | 6|6 A3.3 | Start | 29,467,717 bp[2] |
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End | 29,470,511 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - prefrontal cortex
- left testis
- right testis
- right frontal lobe
- cingulate gyrus
- anterior cingulate cortex
- monocyte
- nucleus accumbens
- amygdala
- right hemisphere of cerebellum
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| Top expressed in | - right kidney
- yolk sac
- human kidney
- proximal tubule
- olfactory bulb
- cerebellum
- lens
- urinary bladder
- dentate gyrus of hippocampal formation granule cell
- hippocampus proper
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| More reference expression data |
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BioGPS | ![](//upload.wikimedia.org/wikipedia/commons/thumb/b/be/PBB_GE_ATP6V1F_201527_at_fs.png/250px-PBB_GE_ATP6V1F_201527_at_fs.png) | More reference expression data |
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Gene ontology |
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Molecular function | - protein binding
- proton-transporting ATPase activity, rotational mechanism
- proton transmembrane transporter activity
- ATPase-coupled ion transmembrane transporter activity
- ATPase 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
- ion transport
- transferrin transport
- phagosome acidification
- ion transmembrane transport
- transport
- proton transmembrane transport
| Sources:Amigo / QuickGO |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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RefSeq (protein) | | |
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Location (UCSC) | Chr 7: 128.86 – 128.87 Mb | Chr 6: 29.47 – 29.47 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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ATP-synt_F |
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Identifiers |
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Symbol | ATP-synt_F |
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Pfam | PF01990 |
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InterPro | IPR008218 |
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Available protein structures: |
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Pfam | structures / ECOD |
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PDB | RCSB PDB; PDBe; PDBj |
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PDBsum | structure summary |
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V-type proton ATPase subunit F is an enzyme that in humans is encoded by the ATP6V1F gene.[5][6][7]
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.[7]
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.[8]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000128524 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004285 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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.
- ^ 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.
- ^ a b "Entrez Gene: ATP6V1F ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F".
- ^ 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.
External links
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. doi:10.1152/physrev.1999.79.2.361. PMID 10221984. S2CID 1477911.
- 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. S2CID 23505139.
- 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. S2CID 21122465.
- 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. S2CID 10507213.
- 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. S2CID 17519696.
- 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. S2CID 12847618.
- 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
This article incorporates text from the public domain
Pfam and
InterPro: IPR008218