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 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.
Mukai
H
H
Department of Biology, Faculty of Science, Kobe University, Japan.
Mori
K
K
Takanaga
H
H
Kitagawa
M
M
Shibata
H
H
Shimakawa
M
M
Miyahara
M
M
Ono
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017124:Conserved Sequence; D018076:DNA, Complementary / Q000096:biosynthesis / Q000737:chemistry*; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D011493:Protein Kinase C; D017346:Protein Serine-Threonine Kinases; D011505:Protein-Tyrosine Kinases / Q000737:chemistry / Q000235:genetics*; D016415:Sequence Alignment; D014981:Xenopus / Q000235:genetics*
D018076:DNA, Complementary; C061570:protein kinase N; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C