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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban. Fujii, J., Ueno, A., Kitano, K., Tanaka, S., Kadoma, M., Tada, M. J. Clin. Invest. (1987) [Pubmed]
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