Identification and characterization of the gene encoding a second proteolipid subunit of human vacuolar H(+)-ATPase (ATP6F)

Genomics
H NishigoriJ Takeda

Abstract

The proteolipid domain of vacuolar H(+)-ATPase (V-ATPase) plays a major role in H+ transport in microvesicles and other acidic organelles. We have cloned the second human proteolipid of the V-ATPase (designated hATP6F), a homologue of the Saccharomyces cerevisiae proteolipid VMA16, which is an essential subunit of yeast V-ATPase. hATP6F is a hydrophobic protein with five putative transmembrane segments, having 61% amino acid identity and 83% similarity to the yeast protein, except in the N-terminus, and contains a conserved glutamic acid residue (Glu98) that is essential for H(+)-transporting activity. The gene for hATP6F (gene symbol, ATP6F), which consists of eight exons and spans approximately 3.5 kb, was isolated and mapped to human chromosome band 1p32.3 and the region 10.81 cR centromeric of the STS marker SHGC36789 (LOD = 6.75) by fluorescence in situ hybridization and radiation hybrid mapping, respectively. This is the first evidence in human of the existence of a second gene encoding a distinct V-ATPase proteolipid.

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Citations

Dec 8, 2009·Molecular Endocrinology·William A AlaynickAndrew N Billin
Jan 5, 2000·Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research·B S LeeS L Gluck
Jan 28, 2009·Biochimica Et Biophysica Acta·Mailys GuillardRon A Wevers
Sep 24, 2004·Physiological Reviews·Carsten A WagnerJohn P Geibel
May 29, 2000·The Journal of Biological Chemistry·B PowellT H Stevens
Jun 6, 2003·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Hong ZhanShoji Ohkuma

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