ATP6V1E1

ATP6V1E1
Identifiers
Aliases	ATP6V1E1 , ATP6E, ATP6E2, ATP6V1E, P31, Vma4, ATPase H+ transporting V1 subunit E1, ARCL2C
External IDs	OMIM: 108746 MGI: 894326 HomoloGene: 1282 GeneCards: ATP6V1E1
Gene location (Human) Chr. Chromosome 22 (human) [1] Band 22q11.21 Start 17,592,136 bp [1] End 17,628,749 bp [1]
Gene location (Mouse) Chr. Chromosome 6 (mouse) [2] Band 6 F1|6 57.01 cM Start 120,771,266 bp [2] End 120,799,754 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in middle temporal gyrus prefrontal cortex pons Brodmann area 9 cingulate gyrus Brodmann area 46 nucleus accumbens superior frontal gyrus frontal pole caudate nucleus Top expressed in facial motor nucleus anterior horn of spinal cord superior frontal gyrus barrel cortex pontine nuclei retinal pigment epithelium prefrontal cortex substantia nigra medial dorsal nucleus cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ATPase binding proton-transporting ATPase activity, rotational mechanism P-type proton-exporting transporter activity protein binding hydrolase activity Cellular component cytoplasm cytosol endosome proton-transporting two-sector ATPase complex microvillus lysosomal membrane apical plasma membrane mitochondrion proton-transporting two-sector ATPase complex, catalytic domain extracellular exosome Biological process insulin receptor signaling pathway transferrin transport ion transport ion transmembrane transport regulation of macroautophagy phagosome acidification transport proton transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 529 11973 Ensembl ENSG00000131100 ENSMUSG00000019210 UniProt P36543 Q53Y06 P50518 RefSeq (mRNA) NM_001696 NM_001039366 NM_001039367 NM_007510 RefSeq (protein) NP_001034455 NP_001034456 NP_001687 NP_001687.1 NP_031536 Location (UCSC) Chr 22: 17.59 – 17.63 Mb Chr 6: 120.77 – 120.8 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

V-type proton ATPase subunit E 1 is an enzyme that in humans is encoded by the ATP6V1E1 gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000131100 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000019210 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1".

External links

• Human ATP6V1E1 genome location and ATP6V1E1 gene details page in the UCSC Genome Browser .

Further reading

• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 324. ( Pt 3) (3): 697–712. doi:10.1042/bj3240697. 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. doi:10.1152/physrev.1999.79.2.361. PMID   10221984. S2CID   1477911.
• 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. S2CID   23505139.
• 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. S2CID   21122465.
• 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. S2CID   10507213.
• 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. doi: 10.1016/S0021-9258(19)50184-3 . 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.