ATP6V1E1

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ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1
Identifiers
Symbols ATP6V1E1 ; ATP6E; ATP6E2; ATP6V1E; P31; Vma4
External IDs Template:OMIM5 Template:MGI HomoloGene1282
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1, also known as ATP6V1E1, 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different V1 domain E subunit isoforms. Pseudogenes for this gene have been found in the genome.[1]

References

  1. 1.0 1.1 "Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1".

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.
  • Hemken P, Guo XL, Wang ZQ; et al. (1992). "Immunologic evidence that vacuolar H+ ATPases with heterogeneous forms of Mr = 31,000 subunit have different membrane distributions in mammalian kidney". J. Biol. Chem. 267 (14): 9948–57. PMID 1533641.
  • Baud V, Mears AJ, Lamour V; et al. (1994). "The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22". Hum. Mol. Genet. 3 (2): 335–9. PMID 8004105.
  • van Hille B, Vanek M, Richener H; et al. (1994). "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase". Biochem. Biophys. Res. Commun. 197 (1): 15–21. PMID 8250920.
  • Puech A, Saint-Jore B, Funke B; et al. (1998). "Comparative mapping of the human 22q11 chromosomal region and the orthologous region in mice reveals complex changes in gene organization". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14608–13. PMID 9405660.
  • Breton S, Wiederhold T, Marshansky V; et al. (2000). "The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated cells". J. Biol. Chem. 275 (24): 18219–24. doi:10.1074/jbc.M909857199. PMID 10748165.

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