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

Biochim Biophys Acta. 1995 Apr 4;1261(2):296-300. doi: 10.1016/0167-4781(95)00030-k.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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*

Substances

  • DNA, Complementary
  • protein kinase N
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Protein Kinase C

Associated data

  • GENBANK/D43890