Protein kinase C is a family of protein kinases that transfers phosphate from ATP to selected serine residues or threonine residues in target proteins. Conventional members integrate calcium ion and diacylglycerol signals with membrane association, while other family members have different activation requirements. A statement about one isoform should not be assumed to describe every member. [ref]
NCBI Gene by the National Library of Medicine. Human PRKCA, Gene ID 5578, Summary and Gene Ontology: calcium/diacylglycerol-dependent serine/threonine kinase activity
A useful pathway example begins with activation of phospholipase C, which produces diacylglycerol and an inositol-phosphate signal that releases stored calcium ions. These signals can cooperate to recruit and activate a conventional protein kinase C. The downstream phosphorylation then changes target behaviour; a rise in calcium is not itself the phosphorylation reaction. [ref]
Molecular Biology of the Cell, 4th edition by Bruce Alberts and others. Chapter 15, Signaling through G-Protein-Linked Cell-Surface Receptors: protein kinase C
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