ATP6V0D1

ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1
Identifiers
Symbols	ATP6V0D1 ; ATP6D; ATP6DV; P39; VATX; VMA6; VPATPD
External IDs	OMIM: 607028 MGI: 1201778 HomoloGene: 3444 IUPHAR: 829 GeneCards: ATP6V0D1 Gene
EC number	3.6.3.14
Gene ontology Molecular function • protein binding • hydrogen-exporting ATPase activity, phosphorylative mechanism • protein complex binding Cellular component • lysosomal membrane • early endosome • centrosome • synaptic vesicle • endosome membrane • membrane • apical plasma membrane • vacuolar proton-transporting V-type ATPase complex • phagocytic vesicle membrane • proton-transporting V-type ATPase, V0 domain • axon terminus • extracellular exosome Biological process • cellular iron ion homeostasis • brain development • insulin receptor signaling pathway • ATP hydrolysis coupled proton transport • proton transport • endoplasmic reticulum unfolded protein response • transferrin transport • ion transmembrane transport • IRE1-mediated unfolded protein response • cilium assembly • cellular protein metabolic process • interaction with host • transmembrane transport • phagosome maturation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
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: 105.52 – 105.57 Mb
PubMed search

V-type proton ATPase subunit d 1 is an enzyme that in humans is encoded by the ATP6V0D1 gene.^[1][2]

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.^[2]

References

1. 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.
2. "Entrez Gene: ATP6V0D1 ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1".

Further reading

• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324. ( Pt 3): 697–712. 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. PMID 10221984.
• 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.
• 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): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
• 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. 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.