Extending the C2 domain family: C2s in PKCs delta, epsilon, eta, theta, phospholipases, GAPs, and perforin.
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 poreforming proteins, perforin.
Ponting
C P
CP
University of Oxford, Fibrinolysis Research Unit, United Kingdom. chris@biop.ox.ac.uk
Parker
P J
PJ
D000595:Amino Acid Sequence; D020690:GTPase-Activating Proteins; D007527:Isoenzymes / Q000737:chemistry*; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D054353:Perforin; D010740:Phospholipases / Q000737:chemistry*; D052899:Pore Forming Cytotoxic Proteins; D011493:Protein Kinase C / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment
D020690:GTPase-Activating Proteins; D007527:Isoenzymes; D008562:Membrane Glycoproteins; D052899:Pore Forming Cytotoxic Proteins; D011506:Proteins; D054353:Perforin; D011493:Protein Kinase C; D010740:Phospholipases