Abstract
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 language | English |
|---|---|
| Pages (from-to) | 1227-1235 |
| Number of pages | 9 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 186 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Aug 14 1992 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Molecular cloning of rabbit CAP-50, a calcyclin associated annexin protein. / Tokumitsu, Hiroshi; Mizutani, Akihiro; Muramatsu, Masa aki; Yokota, Takashi; Arai, Ken ichi; Hidaka, Hiroyoshi.
In: Biochemical and Biophysical Research Communications, Vol. 186, No. 3, 14.08.1992, p. 1227-1235.Research output: Contribution to journal › Article
}
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
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.
UR - http://www.scopus.com/inward/record.url?scp=0026980041&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026980041&partnerID=8YFLogxK
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 -