ATP6V0E1

Protein-coding gene in the species Homo sapiens
ATP6V0E1
Identifiers
AliasesATP6V0E1, ATP6H, ATP6V0E, M9.2, Vma21, Vma21p, ATPase H+ transporting V0 subunit e1
External IDsOMIM: 603931 MGI: 1328318 HomoloGene: 2931 GeneCards: ATP6V0E1
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for ATP6V0E1
Genomic location for ATP6V0E1
Band5q35.1Start172,983,771 bp[1]
End173,035,445 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for ATP6V0E1
Genomic location for ATP6V0E1
Band17|17 A3.3Start26,882,205 bp[2]
End26,918,621 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 17: 26.88 – 26.92 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

V-type proton ATPase subunit e 1 is an enzyme that in humans is encoded by the ATP6V0E1 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 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.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000113732 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000015575 – 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. ^ Ludwig J, Kerscher S, Brandt U, Pfeiffer K, Getlawi F, Apps DK, et al. (June 1998). "Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules". Journal of Biological Chemistry. 273 (18): 10939–10947. doi:10.1074/jbc.273.18.10939. PMID 9556572.
  6. ^ Sambade M, Kane PM (April 2004). "The yeast vacuolar proton-translocating ATPase contains a subunit homologous to the Manduca sexta and bovine e subunits that is essential for function". Journal of Biological Chemistry. 279 (17): 17361–17365. doi:10.1074/jbc.M314104200. PMID 14970230.
  7. ^ a b "Entrez Gene: ATP6V0E1 ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1".

External links

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.


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