ATP6V1D

V-type proton ATPase subunit D is an enzyme that in humans is encoded by the ATP6V1D gene.

ATP6V1D
Identifiers
Aliases	ATP6V1D, ATP6M, VATD, VMA8, ATPase H+ transporting V1 subunit D
External IDs	OMIM: 609398; MGI: 1921084; HomoloGene: 5783; GeneCards: ATP6V1D; OMA:ATP6V1D - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q23.3 Start 67,294,371 bp End 67,360,265 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12 C3|12 35.51 cM Start 78,887,499 bp End 78,908,412 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell middle temporal gyrus Brodmann area 23 pons lateral nuclear group of thalamus prefrontal cortex Brodmann area 9 pars compacta kidney tubule superior vestibular nucleus Top expressed in motor neuron facial motor nucleus Epithelium of choroid plexus vestibular membrane of cochlear duct substantia nigra nucleus accumbens temporal lobe amygdala prefrontal cortex retinal pigment epithelium More reference expression data BioGPS n/a
Gene ontology Molecular function ATPase-coupled transmembrane transporter activity protein binding proton-transporting ATPase activity, rotational mechanism Cellular component cytosol centrosome membrane cilium lysosomal membrane proton-transporting V-type ATPase complex extracellular exosome plasma membrane specific granule membrane Biological process insulin receptor signaling pathway transferrin transport ion transport ion transmembrane transport cell projection organization protein localization to cilium regulation of macroautophagy phagosome acidification neutrophil degranulation cilium assembly transport proton transmembrane transport 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 NP_057078.1 NP_076210 Location (UCSC) Chr 14: 67.29 – 67.36 Mb Chr 12: 78.89 – 78.91 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

External links

• Human ATP6V1D genome location and ATP6V1D 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 (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. 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.
• 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. Bibcode:2000PNAS...97.9543H. 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. S2CID 10147842.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.