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Protein Science, Vol 5, Issue 1 162-166, Copyright © 1996 by Cold Spring Harbor Laboratory Press


FOR THE RECORD

Extending the C2 domain family: C2s in PKCs {delta}, {epsilon}, {eta}, {theta}, phospholipases, GAPs, and perforin

C. P. PONTING and P. J. PARKER
University of Oxford, Fibrinolysis Research Unit, The Old Observatory, South Parks Road, Oxford, OX1 3RH, United Kingdom

Various membrane lipid metabolites, generated by phospholipases C and D (PLCs, PLDs), are known to regulate the activities of protein kinases C (PKCs) and GTP-ase activating proteins (GAPs) in a range of cellular processes. Conventional Ca(2+)-dependent PKCs ({alpha}, {beta}I, {beta}II, and {gamma}), PLCs, and various GAPs are all known to contain copies of a phospholipid-binding domain, termed C2 or CalB. Here we recognize that C2 domains are also present in ``new'' Ca(2+)-independent PKCs ({delta}, {epsilon}, {eta}, and {theta}), other kinases, a eukaryotic PLD, the breakpoint cluster region (BCR) gene product, and two further GAPS. Twenty-two previously unrecognized C2 domain sequences are presented, which include a single copy in the mammalian pore-forming proteins, perforin.
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