ATP6V0E1
Identifiers
AliasesATP6V0E1, ATP6H, ATP6V0E, M9.2, Vma21, Vma21p, ATPase H+ transporting V0 subunit e1
External IDsOMIM: 603931 MGI: 1328318 HomoloGene: 2931 GeneCards: ATP6V0E1
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. 1 2 3 GRCh38: Ensembl release 89: ENSG00000113732 - Ensembl, May 2017
  2. 1 2 3 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, Schagger H (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. 1 2 "Entrez Gene: ATP6V0E1 ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1".

Further reading


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