Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban.
Complementary DNA (cDNA) clones specific for phospholamban of sarcoplasmic reticulum membranes have been isolated from a canine cardiac cDNA library. The amino acid sequence deduced from the cDNA sequence indicates that phospholamban consists of 52 amino acid residues and lacks an amino-terminal signal sequence. The protein has an inferred mol wt 6,080 that is in agreement with its apparent monomeric mol wt 6,000, estimated previously by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Phospholamban contains two distinct domains, a hydrophilic region at the amino terminus (domain I) and a hydrophobic region at the carboxy terminus (domain II). We propose that domain I is localized at the cytoplasmic surface and offers phosphorylatable sites whereas domain II is anchored into the sarcoplasmic reticulum membrane.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002135:Calcium-Binding Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004285:Dogs; D008970:Molecular Weight; D009206:Myocardium / Q000032:analysis; D011487:Protein Conformation; D012995:Solubility; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D004247:DNA; D000099211:Phospholamban