TY - JOUR
T1 - Molecular cloning of rabbit CAP-50, a calcyclin associated annexin protein
AU - Tokumitsu, Hiroshi
AU - Mizutani, Akihiro
AU - Muramatsu, Masa aki
AU - Yokota, Takashi
AU - Arai, Ken ichi
AU - Hidaka, Hiroyoshi
N1 - Funding Information:
We would like to thank Dr. Ryoji Kobayashi for helpful discussions. We also thank Naoko Watanabe and Haruko Deguchi for excellent technical assistance. This work was supported in part by a Grant-Aid for Science research from the Ministry of Education, Science and Culture, Japan (to H.H.) and a grant from the Japan Society for the Promotion of Science for Japanese Junior Scientists (to H.T.) References 1. Hirschhorn, R. R., Aller, P., Yuan, Z., Gibson, C. W., and Baserga, R. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 6004-6008 2. Calabretta, B., Battini, R., Kaczmare, K., de Riel, J. K., and Baserga, R. (1986) J. Biol. Chem. 261, 12628-12632 3. Kuzunichi, J. and Filipek, A. (1987) Biochem. J. 247, 663-667 4. Tokumitsu. H., Kobayashi. R., and Hidaka. H. (1991) Arch. Biochem. Biophys. 288, 202-207 5. Tokumitsu. H., Mizutani. A., Minami. H., Kobayashi. R., and Hidaka. H. (1992) J. Biol. Chem. 267,8919-8924 6. Crompton, M. R., Moss, S. E. and Crumpton, M. J. (1988) Cell 55, 1-3 7. Mizutani, A., Usuda, N., Tokumitsu, H., Minami, H., Yasui K.,Kobayashi, R., and Hidaka, H. (1992) J. Biol. Chem. in press 8. Ito, N., Yonehara, S., Schreurs, J., Gorman, D. M., Maruyama, K., Ishii, A., Yahara, I., Arai, K., Miyajima, A. (1990) Science 247, 324-327 9. Lee, C. C., Wu, R. A., Gibbs, R. G., Cook, D. M. Muzny, and Caskey, C. T. (1988) Science 239, 1288-1291 10. Feinberg, A. P.,and Vogelstein, B. (1983) Anal. Biochem.,132,6-13
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1992/8/14
Y1 - 1992/8/14
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(05)81537-2
DO - 10.1016/S0006-291X(05)81537-2
M3 - Article
C2 - 1380798
AN - SCOPUS:0026980041
VL - 186
SP - 1227
EP - 1235
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -