ATP6V0E1

V-type proton ATPase subunit e 1 is an enzyme that in humans is encoded by the ATP6V0E1 gene.

ATP6V0E1
Identifiers
Aliases	ATP6V0E1, ATP6H, ATP6V0E, M9.2, Vma21, Vma21p, ATPase H+ transporting V0 subunit e1
External IDs	OMIM: 603931 MGI: 1328318 HomoloGene: 2931 GeneCards: ATP6V0E1
Gene location (Human) Chr. Chromosome 5 (human) Band 5q35.1 Start 172,983,771 bp End 173,035,445 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 A3.3 Start 26,882,205 bp End 26,918,621 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in corpus epididymis endothelial cell palpebral conjunctiva stromal cell of endometrium kidney tubule periodontal fiber anterior pituitary visceral pleura islet of Langerhans germinal epithelium Top expressed in medullary collecting duct calvaria renal corpuscle blood yolk sac proximal tubule lip pyloric antrum endocardial cushion right lung lobe More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transporter activity ATPase-coupled ion transmembrane transporter activity proton transmembrane transporter activity hydrolase activity proton-transporting ATPase activity, rotational mechanism Cellular component integral component of membrane proton-transporting V-type ATPase, V0 domain phagocytic vesicle membrane membrane endosome membrane Biological process insulin receptor signaling pathway transferrin transport ion transport vacuolar acidification ion transmembrane transport regulation of macroautophagy proton transmembrane transport transmembrane transport phagosome acidification Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8992 11974 Ensembl ENSG00000113732 ENSMUSG00000015575 UniProt O15342 Q9CQD8 RefSeq (mRNA) NM_003945 NM_025272 RefSeq (protein) NP_003936 NP_079548 Location (UCSC) Chr 5: 172.98 – 173.04 Mb Chr 17: 26.88 – 26.92 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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 and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is possibly part of the V0 subunit. Since two nontranscribed pseudogenes have been found in dogs, it is possible that the localization to chromosome 2 for this gene by radiation hybrid mapping is representing a pseudogene. Genomic mapping puts the chromosomal location on 5q35.3.

External links

• Human ATP6V0E1 genome location and ATP6V0E1 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". Biochemical Journal. 324 (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". Annual Review of Cell and Developmental Biology. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
• Nelson N, Harvey WR (1999). "Vacuolar and plasma membrane proton-adenosinetriphosphatases". Physiological Reviews. 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". Journal of Biological Chemistry. 274 (19): 12951–12954. doi:10.1074/jbc.274.19.12951. PMID 10224039.
• Kane PM (1999). "Introduction: V-ATPases 1992-1998". Journal of Bioenergetics and Biomembranes. 31 (1): 3–5. doi:10.1023/A:1001884227654. PMID 10340843.
• Wieczorek H, Brown D, Grinstein S, Ehrenfeld J, Harvey WR (1999). "Animal plasma membrane energization by proton-motive V-ATPases". BioEssays. 21 (8): 637–648. 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". Nature Reviews Molecular Cell Biology. 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 Letters. 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". Biology of the Cell. 95 (7): 453–457. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263. S2CID 17519696.
• Lu M, Vergara S, Zhang L, Holliday LS, Aris J, Gluck SL (2002). "The amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function". Journal of Biological Chemistry. 277 (41): 38409–38415. doi:10.1074/jbc.M203521200. PMID 12163484.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.