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Transporter Information:
Name: ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E isoform 1
Symbol: ATP6V1E1
TC: 3.A.2.2.3
Locations: 22pter-q11.2
Aliases: P31, Vma4, ATP6E2
GenBank: X76228
Swiss-Prot: P36543
Accession Number: NM_001696
Old Name: ATPase, H+ transporting, lysosomal (vacuolar proton pump) 31kD
PubMed (8004105): Baud V, Mears AJ, Lamour V, Scamps C, Duncan AM, McDermid HE, Lipinski M. The E subunit of vacuolar H(+)-ATPase localizes close to the centromere onhuman chromosome 22.Hum Mol Genet. 1994 Feb;3(2):335-9. PMID: 8004105 [PubMed - indexed for MEDLINE]

As part of a general effort to identify new genes mapping to disease-associated regions of human chromosome 22, we have isolated heterogeneous nuclear RNA from somatic cell hybrids selected for their chromosome 22 content. Inter-Alu PCR amplification yielded a series of human DNA fragments which all detected evolutionarily-conserved sequences. The centromere-most gene fragment candidate, XEN61, was shown to lie centromeric to the chromosome 22 breakpoint in the X/22-33-11TG somatic cell hybrid. This region, which is still devoid of characterized genes, overlaps with the critical region for the cat eye syndrome (CES), a developmental disorder associated with chromosomal duplication within 22pter-q11.2. Gene dosage analysis performed on DNA from six CES patients consistently revealed the presence of four copies of XEN61. A fetal brain cDNA clone, 61EW, was identified with XEN61 and entirely sequenced. The deduced protein is the E subunit of vacuolar H(+)-ATPase. This 31 KDa component of a proton pump is essential in eukaryotic cells as it both controls acidification of the vacuolar system and provides it with its main protonmotive force. RT-PCR experiments using oligonucleotides designed from the 61EW cDNA sequence indicated that the corresponding messenger is widely transcribed.

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.

>P36543|VATE1_HUMAN Vacuolar ATP synthase subunit E 1 - Homo sapiens (Human).