ATPase, H+ transporting, lysosomal V0 subunit a1

ATP6V0A1
Identifiers
Aliases	ATP6V0A1, Atp6v0a1, AA959968, ATP6a1, Atp6n1, Atp6n1a, Atpv0a1, Vpp-1, Vpp1, Stv1, Vph1, a1, ATPase, H+ transporting, lysosomal V0 subunit a1, ATP6N1, ATP6N1A, VPP1, ATPase H+ transporting V0 subunit a1
External IDs	OMIM: 192130 MGI: 103286 HomoloGene: 3795 GeneCards: ATP6V0A1
Gene location (Human)
Chr.	Chromosome 17 (human)[1]
End	42,522,611 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	101,063,719 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• ATPase binding; • proton-transporting ATPase activity, rotational mechanism; • GO:0001948 protein binding; • hydrogen ion transmembrane transporter activity;
Cellular component	• integral component of membrane; • proton-transporting V-type ATPase, V0 domain; • phagocytic vesicle membrane; • Golgi apparatus; • intracellular membrane-bounded organelle; • membrane; • vacuolar proton-transporting V-type ATPase, V0 domain; • melanosome; • vacuolar proton-transporting V-type ATPase complex; • endosome membrane; • extracellular exosome; • cytoplasmic vesicle membrane; • cytoplasmic vesicle; • cytoplasm; • cytosol; • cell membrane; • nuclear speck; • secretory granule membrane; • ficolin-1-rich granule membrane; • lysosomal membrane; • intracellular organelle; • perinuclear region of cytoplasm;
Biological process	• insulin receptor signaling pathway; • transferrin transport; • vacuolar proton-transporting V-type ATPase complex assembly; • toxin transport; • ion transport; • proton transport; • ion transmembrane transport; • ATP synthesis coupled proton transport; • ATP hydrolysis coupled proton transport; • regulation of macroautophagy; • vacuolar acidification; • phagosome acidification; • neutrophil degranulation; • transport;
	Sources:Amigo / QuickGO
Orthologs
	535
	11975
	ENSG00000033627
	ENSMUSG00000019302
	Q93050
	Q9Z1G4
	NM_001130020; NM_001130021; NM_005177
NM_001243049; NM_001243050; NM_001243051; NM_016920; NM_001362636;
	NM_001362637; NM_001362638; NM_001362639; NM_001362640; NM_001362641
NP_001123492; NP_001123493; NP_005168; NP_001365451; NP_001365452;
	NP_001365459; NP_001365460; NP_001365461; NP_001365462; NP_001365463; NP_001365464; NP_001365465; NP_001365466; NP_001365467; NP_001365468; NP_001365469; NP_001365470; NP_001365471; NP_001365472; NP_001365473; NP_001365474; NP_001365475; NP_001365476; NP_001365477; NP_001365478; NP_001365479; NP_001365480; NP_001365481; NP_001365483; NP_001365485; NP_001365486
NP_001229978; NP_001229979; NP_001229980; NP_058616; NP_001349565;
	NP_001349566; NP_001349567; NP_001349568; NP_001349569; NP_001349570
	Wikidata
View/Edit Human	View/Edit Mouse

V-type proton ATPase 116 kDa subunit a isoform 1 is an enzyme that in humans is encoded by the ATP6V0A1 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 one of three A subunit proteins and the encoded protein is associated with clathrin-coated vesicles. The occurrence of splice variants encoding different protein products has been reported, but the full-length natures of these transcripts have not been determined.[6]

References

GRCh38: Ensembl release 89: ENSG00000033627 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000019302 - 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.
Brody LC, Abel KJ, Castilla LH, Couch FJ, McKinley DR, Yin G, Ho PP, Merajver S, Chandrasekharappa SC, Xu J, et al. (Jul 1995). "Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17" (PDF). Genomics. 25 (1): 238–47. doi:10.1016/0888-7543(95)80131-5. PMID 7774924.
"Entrez Gene: ATP6V0A1 ATPase, H+ transporting, lysosomal V0 subunit a1".

External links

Human ATP6V0A1 genome location and ATP6V0A1 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.
Stevens TH, Forgac M (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.
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.
Perin MS, Fried VA, Stone DK, et al. (1991). "Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump". J. Biol. Chem. 266 (6): 3877–81. PMID 1704894.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000033627 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000019302 - 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.

[pmid7774924-5] Brody LC, Abel KJ, Castilla LH, Couch FJ, McKinley DR, Yin G, Ho PP, Merajver S, Chandrasekharappa SC, Xu J, et al. (Jul 1995). "Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17" (PDF). Genomics. 25 (1): 238–47. doi:10.1016/0888-7543(95)80131-5. PMID 7774924.

[entrez-6] "Entrez Gene: ATP6V0A1 ATPase, H+ transporting, lysosomal V0 subunit a1".

ATPase, H+ transporting, lysosomal V0 subunit a1

References

External links

Further reading