cDNa for the 16 kDa subunit of vacuolar H+-ATPase was cloned from mouse cerebellum and sequenced. The deduced polypeptide (155 amino acid residues; molecular weight, 15,808) was highly hydrophobic and homologous to the subunits of bovine adrenal medulla, Torpedo marmorata electric lobe, Drosophila and yeast. Glu-139 (supposed to be essential for proton transport) was also conserved as the potential dicyclohexylcarbodiimide binding site. The subunit had four transmembrane segments: Segment II and IV were highly homologous and Glu-139 was located in Segment IV. The roles of the non-conserved regions are discussed.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - May 15 1991|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology