Internal amino acid sequence analysis of the 80 kDa protein kinase C substrate from rat brain: Relationship to the 87 kDa substrate from bovine brain

Jorge D. Erusalimsky, Clive Morris, Kate Perks, Ron Brown, Susan Brooks, Enrique Rozengurt*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

We have obtained sequence data from five proteolytic peptides totalling 102 amino acid residues of the 80 kDa protein kinase C substrate purified from rat brain. The amino acid sequences of these five peptides were compared with that deduced from a cDNA encoding the 87 kDa protein kinase C substrate from bovine brain. The overall amino acid sequence identity within the regions covered by our peptides is 54%. Two peptides aligned at the C- and N-termini of the bovine protein kinase C substrate with a very high degree of homology (more than 80% identity). Two other peptides exhibited 62% and 46% identity with two regions located in the C-terminal half of the bovine protein. The fifth peptide which contains the sequence PEQPEQPEQ did not reveal any similarity with the bovine protein. Based on the homologies of our experimentally determined sequences, which represent about 30% of the deduced sequence of the bovine protein, we suggest that although these protein kinase C substrates are not identical, they may belong to a family of related proteins.

Original languageEnglish
Pages (from-to)149-153
Number of pages5
JournalFEBS Letters
Volume255
Issue number1
DOIs
Publication statusPublished - 11 Sept 1989
Externally publishedYes

Keywords

  • Amino acid sequence
  • Cellular signalling
  • Protein kinase C substrate

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