Advertisement
Research Article Free access | 10.1172/JCI112799
Find articles by Fujii, J. in: JCI | PubMed | Google Scholar
Find articles by Ueno, A. in: JCI | PubMed | Google Scholar
Find articles by Kitano, K. in: JCI | PubMed | Google Scholar
Find articles by Tanaka, S. in: JCI | PubMed | Google Scholar
Find articles by Kadoma, M. in: JCI | PubMed | Google Scholar
Find articles by Tada, M. in: JCI | PubMed | Google Scholar
Published January 1, 1987 - More info
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.
Click on an image below to see the page. View PDF of the complete article