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