ATP6V1D

ATP6V1D
Identifiers
Aliases	ATP6V1D , ATP6M, VATD, VMA8, ATPase H+ transporting V1 subunit D
External IDs	OMIM: 609398 MGI: 1921084 HomoloGene: 5783 GeneCards: ATP6V1D
Gene location (Human) Chr. Chromosome 14 (human) [1] Band 14q23.3 Start 67,294,371 bp [1] End 67,360,265 bp [1]
Gene location (Mouse) Chr. Chromosome 12 (mouse) [2] Band 12 C3|12 35.51 cM Start 78,887,499 bp [2] End 78,908,412 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell middle temporal gyrus Brodmann area 23 pons prefrontal cortex Brodmann area 9 kidney tubule superior vestibular nucleus entorhinal cortex parietal lobe Top expressed in motor neuron facial motor nucleus substantia nigra nucleus accumbens temporal lobe amygdala prefrontal cortex retinal pigment epithelium cingulate gyrus Region I of hippocampus proper 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

V-type proton ATPase subunit D is an enzyme that in humans is encoded by the ATP6V1D 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 gene encodes the V1 domain D subunit protein. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000100554 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021114 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: ATP6V1D ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D".

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. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.