ATP6V1D

Protein-coding gene in the species Homo sapiens
ATP6V1D
Identifiers
AliasesATP6V1D, ATP6M, VATD, VMA8, ATPase H+ transporting V1 subunit D
External IDsOMIM: 609398; MGI: 1921084; HomoloGene: 5783; GeneCards: ATP6V1D; OMA:ATP6V1D - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for ATP6V1D
Genomic location for ATP6V1D
Band14q23.3Start67,294,371 bp[1]
End67,360,265 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for ATP6V1D
Genomic location for ATP6V1D
Band12 C3|12 35.51 cMStart78,887,499 bp[2]
End78,908,412 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 12: 78.89 – 78.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000100554 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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. 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.


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