Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Adrenal Medulla / enzymology
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Cattle
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Cerebellum / enzymology*
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Cloning, Molecular
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DNA / genetics*
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Drosophila / enzymology
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Electric Organ / enzymology
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Escherichia coli / genetics
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Gene Library
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Macromolecular Substances
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Mice
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Mice, Inbred ICR
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Molecular Sequence Data
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Molecular Weight
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Oligonucleotide Probes
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Proton-Translocating ATPases / genetics*
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Restriction Mapping
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Saccharomyces cerevisiae / enzymology
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Sequence Homology, Nucleic Acid
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Torpedo
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Vacuoles / enzymology*
Substances
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Macromolecular Substances
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Oligonucleotide Probes
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DNA
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Proton-Translocating ATPases