1. Xenopus PKN: cloning and sequencing of the cDNA and identification of conserved domains
- Author
-
Kazuya Mori, Hideki Shibata, Masako Miyahara, Yoshitaka Ono, Hideyuki Mukai, Masaki Shimakawa, Hiromi Takanaga, and Michinori Kitagawa
- Subjects
DNA, Complementary ,Xenopus ,Molecular Sequence Data ,Biophysics ,Sequence alignment ,Protein Serine-Threonine Kinases ,Biochemistry ,Conserved sequence ,Open Reading Frames ,Structural Biology ,Complementary DNA ,Genetics ,Animals ,Amino Acid Sequence ,Cloning, Molecular ,Peptide sequence ,Conserved Sequence ,Protein Kinase C ,Cloning ,biology ,Base Sequence ,urogenital system ,Protein-Tyrosine Kinases ,biology.organism_classification ,Molecular biology ,Open reading frame ,Regulatory sequence ,Sequence Alignment - Abstract
cDNA clone encoding Xenopus laevis PKN has been isolated from Xenopus kidney library. Sequencing of this clone has revealed a single open reading frame encoding a protein of 901 amino acids. Immunoprecipitate from cytoplasmic fraction of COS7 cells transfected with this cDNA construct using antiserum against bacterially expressed Xenopus PKN revealed arachidonic acid-dependent autophosphorylation activity. Comparison of the closely related sequences of human and rat PKN with a protein from evolutionarily distant Xenopus, revealed several highly invariant domains in the NH2-terminal regulatory regions, suggesting that they participate in binding interaction with arachidonic acid.
- Published
- 1995