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Transporter Information:
Name: ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c
Symbol: ATP6V0C
TC: 3.A.2.2.3
Locations: 16p13.3
Aliases: VATL, Vma3
GenBank: M62762
Swiss-Prot: P27449
Accession Number: NM_001694
Old Name: ATPase, H+ transporting, lysosomal (vacuolar proton pump) 16kD
PubMed (1709739): Gillespie GA, Somlo S, Germino GG, Weinstat-Saslow D, Reeders ST. CpG island in the region of an autosomal dominant polycystic kidney diseaselocus defines the 5' end of a gene encoding a putative proton channel.Proc Natl Acad Sci U S A. 1991 May 15;88(10):4289-93. PMID: 1709739 [PubMed - indexed for MEDLINE]

In an attempt to isolate candidate genes for autosomal dominant polycystic kidney disease, a number of CpG-rich islands have been identified from a region defined genetically as the site of disease mutations. Genomic fragments adjacent to one of these islands were used to isolate cDNAs from both HeLa cells and cultured cystic epithelium that encode a 155-amino acid peptide having four putative transmembrane domains. The corresponding transcript was found in all tissues tested but was most abundant in brain and kidney. Potential control response elements were identified in the genomic region 5' to the initiation codon. The deduced amino acid sequence has 93% similarity to the 16-kDa proteolipid component that is believed to be part of the proton channel of the vacuolar H(+)-ATPase. Possible roles for a mutated proton channel in the pathogenesis of cystic disease were considered. However, sequencing of cDNAs corresponding to both alleles of an affected individual revealed no differences in the deduced amino acid sequence. Moreover, transcript size and abundance were not altered in cystic kidney.

PubMed (8250920): van Hille B, Vanek M, Richener H, Green JR, Bilbe G. Cloning and tissue distribution of subunits C, D, and E of the human vacuolarH(+)-ATPase.Biochem Biophys Res Commun. 1993 Nov 30;197(1):15-21. PMID: 8250920 [PubMed - indexed for MEDLINE]

The vacuolar proton ATPase (V-ATPase) translocates protons into intracellular organelles or across the plasma membrane of specialised cells such as osteoclast and renal intercalated cells. The catalytic site of the V-ATPase consists of a hexamer of three A subunits and three B subunits which bind and hydrolyse ATP and are regulated by accessory subunits C, D and E. cDNAs encoding subunits C, D, and E were cloned from human osteoclastoma, a tissue highly enriched in osteoclasts, as a first step in the characterisation of the V-ATPase used by the osteoclast. By Northern blot analysis only one mRNA species were detected for each of these subunits, which is consistent the constant transcription level in all tissues irrespective of the presence of specialised cells highly enriched in V-ATPases.