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XB-ART-27729
Second Messengers Phosphoproteins 1988 Jan 01;125-6:251-60.
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Molecular cloning and sequence analysis of two distinct types of Xenopus laevis protein kinase C.

Chen KH , Peng ZG , Lavu S , Kung HF .


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Two distinct types of protein kinase C cDNA clones were isolated from a Xenopus laevis oocyte cDNA library, and the complete nucleotide sequences were determined. The sequences encode a single open reading frame with a domain structure that consists of four constant (designated C1-C4) and five variable (designated V1-V5) regions. Comparison of the two sequences shows good homology at the nucleotide and deduced amino acid level. The differences reside primarily in the variable regions. Each clone encodes 671 and 676 amino acids, respectively, having extensive homology with published sequences of human, rat, and bovine protein kinase C. These results provide evidence that these two distinct types of protein kinase C are members of a multigene family in amphibian and mammalian species.

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Species referenced: Xenopus laevis
Genes referenced: prkca prkcb