ATP6V0E1

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; OMA:ATP6V0E1 - orthologs
Gene location (Human)
Chr.	Chromosome 5 (human)
End	173,035,445 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	26,918,621 bp
RNA expression pattern
	Top expressed in
	epithelium of nasopharynx; ; corpus epididymis; ; endothelial cell; ; palpebral conjunctiva; ; gingival epithelium; ; stromal cell of endometrium; ; kidney tubule; ; tail of epididymis; ; periodontal fiber; ; anterior pituitary;
	Top expressed in
	choroid plexus of fourth ventricle; ; medullary collecting duct; ; transitional epithelium of urinary bladder; ; right kidney; ; calvaria; ; Epithelium of choroid plexus; ; renal corpuscle; ; granulocyte; ; vestibular membrane of cochlear duct; ; vestibular sensory epithelium;
	More reference expression data
	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
	8992
	11974
	ENSG00000113732
	ENSMUSG00000015575
	O15342
	Q9CQD8
	NM_003945
	NM_025272
	NP_003936
	NP_079548
	Wikidata
View/Edit Human	View/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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000113732 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000015575 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ludwig J, Kerscher S, Brandt U, Pfeiffer K, Getlawi F, Apps DK, Schagger H (Jun 1998). "Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules". J Biol Chem. 273 (18): 10939–10947. doi:10.1074/jbc.273.18.10939. PMID 9556572.
^ Sambade M, Kane PM (Apr 2004). "The yeast vacuolar [[Proton-translocating atpases|proton-translocating]] ATPase contains a subunit [[homology (biology)|homologous]] to the [[Manduca sexta]] and bovine e subunits that is essential for function". J Biol Chem. 279 (17): 17361–17365. doi:10.1074/jbc.M314104200. PMID 14970230. {{cite journal}}: URL–wikilink conflict (help)
^ ^a ^b "Entrez Gene: ATP6V0E1 ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1".

External links

Human ATP6V0E1 genome location and ATP6V0E1 gene details page in the UCSC Genome Browser.

Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 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". Annu. Rev. Cell Dev. Biol. 13: 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.
Forgac M (1999). "Structure and properties of the vacuolar (H+)-ATPases". J. Biol. Chem. 274 (19): 12951–12954. 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): 637–648. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
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): 453–457. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
Lu M; Vergara S; Zhang L; et al. (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". J. Biol. Chem. 277 (41): 38409–38415. doi:10.1074/jbc.M203521200. PMID 12163484. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Strausberg RL; Feingold EA; Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000113732 – Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[pmid9556572-5] Ludwig J, Kerscher S, Brandt U, Pfeiffer K, Getlawi F, Apps DK, Schagger H (Jun 1998). "Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules". J Biol Chem. 273 (18): 10939–10947. doi:10.1074/jbc.273.18.10939. PMID 9556572.

[pmid14970230-6] Sambade M, Kane PM (Apr 2004). "The yeast vacuolar [[Proton-translocating atpases|proton-translocating]] ATPase contains a subunit [[homology (biology)|homologous]] to the [[Manduca sexta]] and bovine e subunits that is essential for function". J Biol Chem. 279 (17): 17361–17365. doi:10.1074/jbc.M314104200. PMID 14970230. {{cite journal}}: URL–wikilink conflict (help)

[entrez-7] "Entrez Gene: ATP6V0E1 ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1".

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References

External links

Further reading