The structure of the B subunit of calcineurin.
The complete primary structure of the B subunit of calcineurin (protein phosphatase 2B) has been determined by automated sequence analysis. The protein consists of a single polypeptide chain of 168 residues, relative molecular mass 19200. The structure shows 35% identity with the sequence of calmodulin and 29% with troponin C. Homology is mainly confined to the regions of the four putative Ca2+-binding loops. The results demonstrate that the B subunit is a new member of this family of Ca2+-binding proteins. The N-terminal glycine residue is blocked with the C14-saturated fatty acid myristic acid and the first four residues are very similar to those of the catalytic subunit of cyclic-AMP-dependent protein kinase which also contains a myristoyl blocking group.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001322:Autoanalysis; D002148:Calmodulin-Binding Proteins; D055598:Chemical Phenomena; D002621:Chemistry; D003488:Cyanogen Bromide; D010446:Peptide Fragments; D010749:Phosphoprotein Phosphatases
D000596:Amino Acids; D002148:Calmodulin-Binding Proteins; D010446:Peptide Fragments; D010749:Phosphoprotein Phosphatases; D003488:Cyanogen Bromide