ATP6V1D

ATP6V1D
Identifiers
Aliases	ATP6V1D, ATP6M, VATD, VMA8, ATPase H+ transporting V1 subunit D
External IDs	MGI: 1921084 HomoloGene: 5783 GeneCards: ATP6V1D
Gene ontology Molecular function • ATPase activity, coupled to transmembrane movement of substances • protein binding Cellular component • cytosol • centrosome • membrane • cilium • lysosomal membrane • proton-transporting V-type ATPase complex • extracellular exosome Biological process • insulin receptor signaling pathway • transferrin transport • ion transport • proton transport • ion transmembrane transport • cell projection organization • protein localization to cilium • transport • cilium assembly • regulation of macroautophagy • phagosome acidification • transmembrane transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51382	73834
Ensembl	ENSG00000100554	ENSMUSG00000021114
UniProt	Q9Y5K8	P57746
RefSeq (mRNA)	NM_015994	NM_023721
RefSeq (protein)	NP_057078.1 NP_057078.1	NP_076210.1
Location (UCSC)	Chr 14: 67.29 – 67.36 Mb	Chr 12: 78.84 – 78.86 Mb
PubMed search	[1]	[2]
Wikidata

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V-type proton ATPase subunit D is an enzyme that in humans is encoded by the ATP6V1D gene.^[3][4]

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 gene encodes the V1 domain D subunit protein.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Stevens TH, Forgac M (Feb 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.
4. "Entrez Gene: ATP6V1D ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D".

Further reading

• 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.
• 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.
• Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
• Kennell JA, Richards NW, Schaner PE, Gumucio DL (2001). "cDNA cloning, chromosomal localization and evolutionary analysis of mouse vacuolar ATPase subunit D, Atp6m". Cytogenet. Cell Genet. 92 (3–4): 337–41. doi:10.1159/000056924. PMID 11435709.
• Yang CS, Weiner H (2002). "Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol". Arch. Biochem. Biophys. 400 (1): 105–10. doi:10.1006/abbi.2002.2778. PMID 11913976.
• 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): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.