ATP6V0C

ATP6V0C
Identifiers
Aliases	ATP6V0C, ATP6C, ATP6L, ATPL, VATL, VPPC, Vma3, ATPase H+ transporting V0 subunit c
External IDs	MGI: 88116 HomoloGene: 68199 GeneCards: ATP6V0C
Gene ontology Molecular function • proton-transporting ATP synthase activity, rotational mechanism • proton-transporting ATPase activity, rotational mechanism • protein binding • hydrogen ion transmembrane transporter activity • ubiquitin protein ligase binding Cellular component • integral component of membrane • proton-transporting V-type ATPase, V0 domain • phagocytic vesicle membrane • proton-transporting two-sector ATPase complex, proton-transporting domain • membrane • vacuolar membrane • focal adhesion • vacuolar proton-transporting V-type ATPase, V0 domain • lysosomal membrane • vacuole • endosome membrane • extracellular exosome Biological process • insulin receptor signaling pathway • lysosomal lumen acidification • transferrin transport • ion transport • proton transport • positive regulation of Wnt signaling pathway • ion transmembrane transport • transport • viral process • ATP hydrolysis coupled proton transport • regulation of macroautophagy • phagosome acidification Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	527	11984
Ensembl	ENSG00000185883	ENSMUSG00000024121
UniProt	P27449	P63082
RefSeq (mRNA)	NM_001694 NM_001198569	NM_009729
RefSeq (protein)	NP_001185498.1 NP_001685.1	NP_033859.1
Location (UCSC)	Chr 16: 2.51 – 2.52 Mb	Chr 17: 24.16 – 24.17 Mb
PubMed search	[1]	[2]
Wikidata

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V-type proton ATPase 16 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0C gene.^[3][4][5]

Function

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 encoded protein is part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Gillespie GA, Somlo S, Germino GG, Weinstat-Saslow D, Reeders ST (May 1991). "CpG island in the region of an autosomal dominant polycystic kidney disease locus defines the 5' end of a gene encoding a putative proton channel". Proceedings of the National Academy of Sciences of the United States of America. 88 (10): 4289–93. doi:10.1073/pnas.88.10.4289. PMC 51644. PMID 1709739.
4. van Hille B, Vanek M, Richener H, Green JR, Bilbe G (Nov 1993). "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase". Biochemical and Biophysical Research Communications. 197 (1): 15–21. doi:10.1006/bbrc.1993.2434. PMID 8250920.
5. "Entrez Gene: ATP6V0C ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c".

Further reading

• Finbow ME, Harrison MA (Jun 1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". The Biochemical Journal. 324 (Pt 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". Annual Review of Cell and Developmental Biology. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
• Nelson N, Harvey WR (Apr 1999). "Vacuolar and plasma membrane proton-adenosinetriphosphatases". Physiological Reviews. 79 (2): 361–85. PMID 10221984.
• Forgac M (May 1999). "Structure and properties of the vacuolar (H+)-ATPases". The Journal of Biological Chemistry. 274 (19): 12951–4. doi:10.1074/jbc.274.19.12951. PMID 10224039.
• Kane PM (Feb 1999). "Introduction: V-ATPases 1992-1998". Journal of Bioenergetics and Biomembranes. 31 (1): 3–5. doi:10.1023/A:1001884227654. PMID 10340843.
• Wieczorek H, Brown D, Grinstein S, Ehrenfeld J, Harvey WR (Aug 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 (Feb 2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps". Nature Reviews Molecular Cell Biology. 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511.
• Kawasaki-Nishi S, Nishi T, Forgac M (Jun 2003). "Proton translocation driven by ATP hydrolysis in V-ATPases". FEBS Letters. 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
• Morel N (Oct 2003). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase". Biology of the Cell / Under the Auspices of the European Cell Biology Organization. 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
• Hasebe M, Hanada H, Moriyama Y, Maeda M, Futai M (Mar 1992). "Vacuolar type H(+)-ATPase genes: presence of four genes including pseudogenes for the 16-kDa proteolipid subunit in the human genome". Biochemical and Biophysical Research Communications. 183 (2): 856–63. doi:10.1016/0006-291X(92)90562-Y. PMID 1532310.
• Koralnik IJ, Mulloy JC, Andresson T, Fullen J, Franchini G (Aug 1995). "Mapping of the intermolecular association of human T cell leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16 kDa subunit protein". The Journal of General Virology. 76 (8): 1909–16. doi:10.1099/0022-1317-76-8-1909. PMID 7636472.
• Laitala-Leinonen T, Howell ML, Dean GE, Väänänen HK (Jan 1996). "Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts". Molecular Biology of the Cell. 7 (1): 129–42. doi:10.1091/mbc.7.1.129. PMC 278618. PMID 8741845.