Amino-acid sequence of the beta-subunit of the (Na+ + K+)ATPase deduced from a cDNA.
The sodium/potassium-dependent ATPase [(Na+ + K+)ATPase], which establishes and maintains the Na+ and K+ gradients across the plasma membrane of animal cells, consists of two subunits, alpha and beta. Complementary DNA clones encoding the catalytic (alpha) subunit of sheep kidney and Torpedo californica electroplax enzymes have previously been isolated and characterized. However, there is little information concerning the primary structure of the beta-subunit, a glycoprotein of unknown function and relative molecular mass (Mr) approximately 55,000 (ref. 3). Here we describe the isolation and characterization of a cDNA clone containing the entire coding region of the beta-subunit of the sheep kidney (Na+ + K+)ATPase. We also discuss structural aspects of the protein and present evidence for a possible evolutionary relationship with the KdpC subunit of the Escherichia coli K+-ATPase.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D007668:Kidney / Q000201:enzymology; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D012756:Sheep; D000254:Sodium-Potassium-Exchanging ATPase / Q000235:genetics*
D046911:Macromolecular Substances; D010446:Peptide Fragments; D004247:DNA; D000254:Sodium-Potassium-Exchanging ATPase