Protein-coding gene in the species Homo sapiens
| ATP6V0D1 |
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| Identifiers |
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| Aliases | ATP6V0D1, ATP6D, ATP6DV, P39, VATX, VMA6, VPATPD, ATPase H+ transporting V0 subunit d1 |
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| External IDs | OMIM: 607028; MGI: 1201778; HomoloGene: 3444; GeneCards: ATP6V0D1; OMA:ATP6V0D1 - orthologs |
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| Gene location (Human) |
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 | | Chr. | Chromosome 16 (human)[1] |
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| | Band | 16q22.1 | Start | 67,438,014 bp[1] |
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| End | 67,481,181 bp[1] |
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| Gene location (Mouse) |
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 | | Chr. | Chromosome 8 (mouse)[2] |
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| | Band | 8|8 D3 | Start | 106,251,097 bp[2] |
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| End | 106,292,679 bp[2] |
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| RNA expression pattern |
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| Bgee | | Human | Mouse (ortholog) |
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| Top expressed in | - mucosa of transverse colon
- beta cell
- lateral nuclear group of thalamus
- granulocyte
- mononuclear cell
- monocyte
- Pars compacta
- prefrontal cortex
- right frontal lobe
- lower lobe of lung
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| | Top expressed in | - facial motor nucleus
- anterior horn of spinal cord
- stroma of bone marrow
- hippocampus proper
- superior frontal gyrus
- epithelium of lens
- central gray substance of midbrain
- subiculum
- temporal lobe
- primary motor cortex
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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 | - protein-containing complex binding
- protein binding
- proton transmembrane transporter activity
- P-type proton-exporting transporter activity
- proton-transporting ATPase activity, rotational mechanism
| | Cellular component | - axon terminus
- proton-transporting V-type ATPase, V0 domain
- phagocytic vesicle membrane
- centrosome
- membrane
- synaptic vesicle
- lysosomal membrane
- apical plasma membrane
- neuron projection
- vacuolar proton-transporting V-type ATPase complex
- endosome membrane
- extracellular exosome
- early endosome
- protein-containing complex
- plasma membrane proton-transporting V-type ATPase complex
| | Biological process | - insulin receptor signaling pathway
- transferrin transport
- ion transport
- ion transmembrane transport
- IRE1-mediated unfolded protein response
- brain development
- cell projection organization
- regulation of macroautophagy
- phagosome acidification
- cilium assembly
- vacuolar transport
- vacuolar acidification
- cellular iron ion homeostasis
- cellular response to increased oxygen levels
- 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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| RefSeq (protein) | | |
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| Location (UCSC) | Chr 16: 67.44 – 67.48 Mb | Chr 8: 106.25 – 106.29 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 d 1 is an enzyme that in humans is encoded by the ATP6V0D1 gene.[5][6]
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 known as the D subunit and is found ubiquitously.[6]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000159720 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000013160 – 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.
- ^ 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: ATP6V0D1 ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1".
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. S2CID 17519696.
- Wang SY, Moriyama Y, Mandel M, et al. (1988). "Cloning of cDNA encoding a 32-kDa protein. An accessory polypeptide of the H+-ATPase from chromaffin granules". J. Biol. Chem. 263 (33): 17638–42. doi:10.1016/S0021-9258(19)77884-3. PMID 2903164.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Agarwal AK, White PC (2001). "Structure of the VPATPD gene encoding subunit D of the human vacuolar proton ATPase". Biochem. Biophys. Res. Commun. 279 (2): 543–7. doi:10.1006/bbrc.2000.4003. PMID 11118322.
