Abstract
A complementary DNA encoding an ATP-regulated potassium channel has been isolated by expression cloning from rat kidney. The predicted 45K protein, which features two potential membrane-spanning helices and a proposed ATP-binding domain, represents a major departure from the basic structural design characteristic of voltage-gated and second messenger-gated ion channels. But the presence of an H5 region, which is likely to form the ion conduction pathway, indicates that the protein may share a common origin with voltage-gated potassium channel proteins.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / pharmacology*
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Amino Acid Sequence
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Animals
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Barium / pharmacology
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Barium Compounds*
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Base Sequence
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Cell Membrane / physiology
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Cell Membrane / ultrastructure
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Chlorides*
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Cloning, Molecular
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Female
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Ion Channel Gating
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Kidney Medulla / physiology*
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Membrane Potentials / drug effects
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Models, Structural
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Molecular Sequence Data
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Oocytes / drug effects
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Oocytes / physiology
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Open Reading Frames
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Poly A / genetics
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Potassium Channels / drug effects
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Potassium Channels / genetics*
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Potassium Channels / physiology
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Protein Conformation
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Protein Structure, Secondary
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RNA / genetics
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Rats
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Second Messenger Systems
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Sequence Homology, Amino Acid
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Xenopus laevis
Substances
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Barium Compounds
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Chlorides
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Potassium Channels
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RNA, Messenger
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barium chloride
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Poly A
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Barium
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RNA
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Adenosine Triphosphate