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]
End	67,360,265 bp[1]
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)[2]
End	78,861,638 bp[2]
Gene ontology
Molecular function	• ATPase activity, coupled to transmembrane movement of substances; • GO:0001948 protein binding; • proton-transporting ATPase activity, rotational mechanism;
Cellular component	• cytosol; • centrosome; • membrane; • cilium; • lysosomal membrane; • proton-transporting V-type ATPase complex; • extracellular exosome; • cell 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 morphogenesis; • transport; • hydrogen ion transmembrane transport; • transmembrane transport;
	Sources:Amigo / QuickGO
Orthologs
	51382
	73834
	ENSG00000100554
	ENSMUSG00000021114
	Q9Y5K8
	P57746
	NM_015994
	NM_023721
	NP_057078; NP_057078.1
	NP_076210
	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

GRCh38: Ensembl release 89: ENSG00000100554 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000021114 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
"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.

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.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100554 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid9442887-5] 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.

[entrez-6] "Entrez Gene: ATP6V1D ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D".

ATP6V1D

References

External links

Further reading