ATP6V1E1

ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1
Identifiers
Symbols	ATP6V1E1 ; ATP6E; ATP6E2; ATP6V1E; P31; Vma4
External IDs	OMIM: 108746 MGI: 894326 HomoloGene: 1282 GeneCards: ATP6V1E1 Gene
EC number	3.6.3.14
Gene ontology Molecular function • protein binding • hydrogen-exporting ATPase activity, phosphorylative mechanism • proton-transporting ATPase activity, rotational mechanism • ATPase binding Cellular component • mitochondrion • lysosomal membrane • endosome • cytosol • microvillus • apical plasma membrane • proton-transporting two-sector ATPase complex • proton-transporting two-sector ATPase complex, catalytic domain • extracellular exosome Biological process • cellular iron ion homeostasis • metabolic process • insulin receptor signaling pathway • ATP hydrolysis coupled proton transport • proton transport • transferrin transport • ion transmembrane transport • interaction with host • transmembrane transport • phagosome maturation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	529	11973
Ensembl	ENSG00000131100	ENSMUSG00000019210
UniProt	P36543	P50518
RefSeq (mRNA)	NM_001039366	NM_007510
RefSeq (protein)	NP_001034455	NP_031536
Location (UCSC)	Chr 22: 17.59 – 17.63 Mb	Chr 6: 120.8 – 120.82 Mb
PubMed search

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

1. Baud V, Mears AJ, Lamour V, Scamps C, Duncan AM, McDermid HE, Lipinski M (Jul 1994). "The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22". Hum Mol Genet 3 (2): 335–9. doi:10.1093/hmg/3.2.335. PMID 8004105.
2. van Hille B, Vanek M, Richener H, Green JR, Bilbe G (Jan 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. doi:10.1006/bbrc.1993.2434. PMID 8250920.
3. "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. PMC 1218484. PMID 9210392.
• Stevens TH, Forgac M (1998). "Structure, function and regulation of the vacuolar (H+)-ATPase.". Annu. Rev. Cell Dev. Biol. 13 (1): 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. 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.
• 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. 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.
• 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.
• 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. doi:10.1073/pnas.94.26.14608. PMC 25069. 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.