Molecular cloning of rabbit CAP-50, a calcyclin associated annexin protein

Hiroshi Tokumitsu, Akihiro Mizutani, Masa aki Muramatsu, Takashi Yokota, Ken ichi Arai, Hiroyoshi Hidaka

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6 Citations (Scopus)


CAP-50 is a member of annexin family proteins which binds specifically to calcyclin in a Ca2+ dependent manner (Tokumitsu. H., Mizutani. A., Minami. H., Kobayashi. R., and Hidaka. H. (1992) J. Biol. Chem. 267,8919-8924). The cDNA representing the rabbit form of this protein has been cloned from rabbit lung cDNA library. Sequence analysis of two overlapping clones revealed a 81-nucleotides 5′-nontranslated region, 1512-nucleotides of open reading frame, a 672-nucleotides 3′-nontranslated region, and a poly(A) tail. Authenticity of the clones was confirmed by comparison of portions of the deduced amino acid sequence with eight sequences of proteolytic peptides obtained from rabbit lung protein. CAP-50 cDNA encodes a 503 residue protein with a calculatedMr of 54,043 and shows that the protein is composed of four imperfect repeats and hydrophobic N-terminal region. C-terminal region including four imperfect repeats shows 58.1% identity with human synexin (annexin VII), 48.0% identity with annexin I, 47.4% identity with annexin II, 60.1% identity with annexin IV, 54.5% identity with annexin V. Hydrophobic N-terminal region composed of 202 amino acid residues is not homologous with other annexin proteins suggesting that CAP-50 is a novel member of annexin family proteins.

Original languageEnglish
Pages (from-to)1227-1235
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - Aug 14 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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