The cDNA sequence for the protein-tyrosine kinase substrate p36 (calpactin I heavy chain) reveals a multidomain protein with internal repeats

• Published in: Cell Vol. 46; no. 2; pp. 201 - 212
• Main Authors: Saris, Chris J.M., Tack, Brian F., Kristensen, Torsten, Glenney, John R., Hunter, Tony
• Format: Journal Article
• Language: English
• Published: Cambridge, MA Elsevier Inc 18.07.1986; Cell Press
• Subjects: Amino Acid Sequence; Animals; Annexins; Base Sequence; Biological and medical sciences; Calcium-Binding Proteins - genetics; calpactin I; cDNA; Cell structures and functions; Cloning, Molecular; Cytoskeleton, cytoplasm. Intracellular movements; DNA - genetics; DNA Restriction Enzymes; Fundamental and applied biological sciences. Psychology; genes; lipocortin I; Mice; Molecular and cellular biology; Molecular Weight; nucleotide sequence; Protein-Tyrosine Kinases - genetics; Repetitive Sequences, Nucleic Acid; RNA, Messenger - genetics; C terminal»-Sequence; Repeated sequence; heavy-Peptide chain; Rabbit; Primary structure; Lagomorpha; Substrate; Vertebrata; Brush border; Mammalia; Complementary DNA; Protein kinase; Cytoskeleton; Isolation; Comparative study
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/0092-8674(86)90737-3

We have isolated and sequenced a full-length cDNA clone for the protein-tyrosine kinase substrate p36 (calpactin I heavy chain). This sequence predicts a 339 amino acid (M r 38,493) protein containing an N-terminal region of 20 amino acids, known to interact with a 10 kd protein (light chain), and a C-terminal region, found to contain two Ca 2+ phospholipid - binding sites, that can be aligned as four 70 amino acid repeats. A single p36 gene was detected in the mouse genome, and a major p36 mRNA of 1.6 kb was found to be expressed in different mouse tissues. Unexpectedly, p36 and the phospholipase A 2 inhibitor lipocortin I were found to be 50% identical in sequence over the C-terminal 300 residues. The function of p36 and its relation to other proteins are discussed.