Biology:ATP6V1E1
 Generic protein structure example |
V-type proton ATPase subunit E 1 is an enzyme that in humans is encoded by the ATP6V1E1 gene.[1][2][3]
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.[3]
References
- ↑ "The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22". Hum Mol Genet 3 (2): 335–9. Jul 1994. doi:10.1093/hmg/3.2.335. PMID 8004105.
- ↑ "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase". Biochem Biophys Res Commun 197 (1): 15–21. Jan 1994. doi:10.1006/bbrc.1993.2434. PMID 8250920.
- ↑ 3.0 3.1 "Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=529.
External links
- Human ATP6V1E1 genome location and ATP6V1E1 gene details page in the UCSC Genome Browser.
Further reading
- "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J.. 324 ( Pt 3) (3): 697–712. 1997. doi:10.1042/bj3240697. PMID 9210392.
- "Structure, function and regulation of the vacuolar (H+)-ATPase.". Annu. Rev. Cell Dev. Biol. 13 (1): 779–808. 1998. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
- "Vacuolar and plasma membrane proton-adenosinetriphosphatases.". Physiol. Rev. 79 (2): 361–85. 1999. doi:10.1152/physrev.1999.79.2.361. 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.
- "Animal plasma membrane energization by proton-motive V-ATPases.". BioEssays 21 (8): 637–48. 1999. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860.
- "The vacuolar (H+)-ATPases--nature's most versatile proton pumps.". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. 2002. doi:10.1038/nrm729. PMID 11836511.
- "Proton translocation driven by ATP hydrolysis in V-ATPases.". FEBS Lett. 545 (1): 76–85. 2003. 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.
- "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. 1992. doi:10.1016/S0021-9258(19)50184-3. PMID 1533641.
- "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. 1998. doi:10.1073/pnas.94.26.14608. PMID 9405660.
- "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. 2000. doi:10.1074/jbc.M909857199. PMID 10748165.
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