ATP6V0D1

ATP6V0D1
Identifiers
Aliases	ATP6V0D1, ATP6D, ATP6DV, P39, VATX, VMA6, VPATPD, ATPase H+ transporting V0 subunit d1
External IDs	OMIM: 607028 MGI: 1201778 HomoloGene: 3444 GeneCards: ATP6V0D1
Gene location (Human) Chr. Chromosome 16 (human) Band 16q22.1 Start 67,438,014 bp End 67,481,181 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 D3 Start 106,251,097 bp End 106,292,679 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte prefrontal cortex lower lobe of lung anterior pituitary Brodmann area 46 blood pons left adrenal gland hypothalamus Brodmann area 9 Top expressed in facial motor nucleus anterior horn of spinal cord hippocampus proper superior frontal gyrus subiculum temporal lobe primary motor cortex prefrontal cortex pontine nuclei piriform cortex More reference expression data BioGPS More reference expression data
Gene ontology 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
Orthologs Species Human Mouse Entrez 9114 11972 Ensembl ENSG00000159720 ENSMUSG00000013160 UniProt P61421 P51863 RefSeq (mRNA) NM_004691 NM_013477 RefSeq (protein) NP_004682 NP_038505 Location (UCSC) Chr 16: 67.44 – 67.48 Mb Chr 8: 106.25 – 106.29 Mb PubMed search
Wikidata
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V-type proton ATPase subunit d 1 is an enzyme that in humans is encoded by the ATP6V0D1 gene.

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.

External links

• Human ATP6V0D1 genome location and ATP6V0D1 gene details page in the UCSC Genome Browser.

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.