Protein-coding gene in the species Homo sapiens
| ATP6V1E1 |
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| Identifiers |
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| Aliases | ATP6V1E1, ATP6E, ATP6E2, ATP6V1E, P31, Vma4, ATPase H+ transporting V1 subunit E1, ARCL2C |
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| External IDs | OMIM: 108746; MGI: 894326; HomoloGene: 1282; GeneCards: ATP6V1E1; OMA:ATP6V1E1 - orthologs |
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| Gene location (Human) |
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 | | Chr. | Chromosome 22 (human)[1] |
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| | Band | 22q11.21 | Start | 17,592,136 bp[1] |
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| End | 17,628,749 bp[1] |
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| Gene location (Mouse) |
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 | | Chr. | Chromosome 6 (mouse)[2] |
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| | Band | 6 F1|6 57.01 cM | Start | 120,771,266 bp[2] |
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| End | 120,799,754 bp[2] |
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| RNA expression pattern |
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| Bgee | | Human | Mouse (ortholog) |
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| Top expressed in | - middle temporal gyrus
- prefrontal cortex
- pons
- right frontal lobe
- Brodmann area 9
- C1 segment
- cingulate gyrus
- anterior cingulate cortex
- Brodmann area 46
- nucleus accumbens
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| | Top expressed in | - facial motor nucleus
- dentate gyrus of hippocampal formation granule cell
- anterior horn of spinal cord
- superior frontal gyrus
- primary visual cortex
- right kidney
- Epithelium of choroid plexus
- barrel cortex
- pontine nuclei
- retinal pigment epithelium
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| | More reference expression data |
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| BioGPS |  | | More reference expression data |
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| Gene ontology |
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| 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 |
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| Orthologs |
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| Species | Human | Mouse |
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| Entrez | | |
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| Ensembl | | |
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| UniProt | | |
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| RefSeq (mRNA) | |
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NM_001696
NM_001039366
NM_001039367 |
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| RefSeq (protein) | |
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NP_001034455
NP_001034456
NP_001687
NP_001687.1 |
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| Location (UCSC) | Chr 22: 17.59 – 17.63 Mb | Chr 6: 120.77 – 120.8 Mb |
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| PubMed search | [3] | [4] |
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| Wikidata |
| View/Edit Human | View/Edit Mouse |
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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
- ^ a b c GRCh38: Ensembl release 89: ENSG00000131100 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019210 – 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.
- ^ 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.
- ^ 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.
- ^ a b "Entrez Gene: ATP6V1E1 ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1".
External links
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.
