Cloning and Expression Patterns of two Members of A Novel Protein‐kinase‐C‐related Kinase Family

• Published in: European journal of biochemistry Vol. 227; no. 1‐2; pp. 344 - 351
• Main Authors: Palmer, Ruth H., Ridden, John, Parker, Peter J.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.01.1995
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Cell Line; Cloning, Molecular; DNA, Complementary; Humans; Molecular Sequence Data; Phosphorylation; Protein kinase; protein kinase C; Protein Kinase C - genetics; protein‐kinase‐C‐related kinase; RNA, Messenger - genetics; RNA, Messenger - metabolism; Sequence Homology, Amino Acid
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1995.tb20395.x

The cDNA clones for two members of a novel protein kinase family were isolated and sequenced. These protein‐kinase‐C‐related kinases, PRK1 and PRK2, display extensive identity to each other, revealing non‐kinase domain similar regions, HR1 and HR2. HR1 contains a motif repeated three times (HR1a–c), while HR2 shows similarity to the amino‐terminal sequence of protein‐kinase‐C ɛ and η isotypes. Both PRK1 and PRK2, expressed in COS 1 cells, are autophosphorylated in immunoprecipitates, indicating intrinsic kinase activity. PRK1 and PRK2, as well as a third member of this family, PRK3, show distinct patterns of expression in adult tissues.