ATP6V0E1

From Wikipedia, the free encyclopedia


ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1
Identifiers
Symbol(s) ATP6V0E1; ATP6H; ATP6V0E; M9.2; Vma21; Vma21p
External IDs OMIM: 603931 MGI1328318 HomoloGene2931
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 8992 11974
Ensembl ENSG00000113732 ENSMUSG00000015575
Uniprot O15342 Q9CQD8
Refseq NM_003945 (mRNA)
NP_003936 (protein)
NM_025272 (mRNA)
NP_079548 (protein)
Location Chr 5: 172.34 - 172.39 Mb Chr 17: 26.4 - 26.43 Mb
Pubmed search [1] [2]

ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1, also known as ATP6V0E1, 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 possibly part of the V0 subunit. Since two nontranscribed pseudogenes have been found in dog, it is possible that the localization to chromosome 2 for this gene by radiation hybrid mapping is representing a pseudogene. Genomic mapping puts the chromosomal location on 5q35.3.[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: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. 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: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. PMID 12788495. 
  • Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453-7. PMID 14597263. 
  • Ludwig J, Kerscher S, Brandt U, et al. (1998). "Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules.". J. Biol. Chem. 273 (18): 10939-47. PMID 9556572. 
  • Lu M, Vergara S, Zhang L, et al. (2002). "The amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function.". J. Biol. Chem. 277 (41): 38409-15. doi:10.1074/jbc.M203521200. PMID 12163484. 
  • 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. PMID 12477932.