Xenopus PKN: cloning and sequencing of the cDNA and identification of conserved domains

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 antiseru...

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Bibliographic Details
Published in:Biochimica et biophysica acta 1995-04, Vol.1261 (2), p.296-300
Main Authors: Mukai, H, Mori, K, Takanaga, H, Kitagawa, M, Shibata, H, Shimakawa, M, Miyahara, M, Ono, Y
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
Conserved Sequence
DNA, Complementary - biosynthesis
DNA, Complementary - chemistry
Molecular Sequence Data
Open Reading Frames
Protein Kinase C
Protein-Serine-Threonine Kinases
Protein-Tyrosine Kinases - chemistry
Protein-Tyrosine Kinases - genetics
Sequence Alignment
Xenopus - genetics
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Summary: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.
ISSN:0006-3002
0167-4781
DOI:10.1016/0167-4781(95)00030-k