ATP6V1E1

From Wikipedia, the free encyclopedia

ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1

Identifiers

ATP6V1E1; ATP6E; ATP6E2; ATP6V1E; P31; Vma4

External IDs

OMIM: 108746 MGI: 894326 HomoloGene: 1282

Gene ontology
Molecular Function:	• protein binding • hydrogen-exporting ATPase activity, phosphorylative mechanism • hydrolase activity • metal ion binding • hydrogen ion transporting ATP synthase activity, rotational mechanism • hydrogen ion transporting ATPase activity, rotational mechanism
Cellular Component:	• cytoplasm • mitochondrion • plasma membrane • proton-transporting two-sector ATPase complex
Biological Process:	• ion transport • ATP synthesis coupled proton transport • ATP hydrolysis coupled proton transport • proton transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001039366 (mRNA)
NP_001034455 (protein)

NM_007510 (mRNA)
NP_031536 (protein)

Location

Chr 22: 16.45 - 16.49 Mb

Chr 6: 120.76 - 120.79 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1.

[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.
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.