title: Similarity between phospholipase C and the regulatory domain of protein kinase C.
abstract: We report that a 100 residue segment in the carboxy-terminus half of phosphatidylinositol-specific phospholipase C is similar to a segment in the amino-terminus half of protein kinase C. The computer-based comparison score is 9.5 standard deviations higher than that of 2500 comparisons of randomized sequences of these segments (P = 10(-21), suggesting that the two segments have similar biological properties. Phospholipase C has a segment that is homologous to part of the non-catalytic domain of src kinase and other tyrosine protein kinases. The similarity of phospholipase C with protein kinase C, a serine/threonine kinase suggests that novel exon shuffling occurred among serine/threonine and tyrosine kinases and phospholipase C.
authors.affiliation: Department of Medicine, University of California, San Diego, La Jolla 92093.
authors.forename: M E
authors.initials: ME
authors.lastname: Baker
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D003201:Computers; D005091:Exons; D008969:Molecular Sequence Data; D011493:Protein Kinase C / Q000235:genetics*; D051381:Rats; D012045:Regulatory Sequences, Nucleic Acid; D012689:Sequence Homology, Nucleic Acid; D010738:Type C Phospholipases / Q000235:genetics*
chemical_list: D011493:Protein Kinase C; D010738:Type C Phospholipases