Molecular cloning and sequencing of the cDNA coding for a calcium‐binding protein regucalcin from rat liver

FEBS Letters

Shimokawa, Noriaki¹  Yamaguchi, Masayoshi¹ 

[1] Laboratory of Metabolism and Endocrinology, Graduate School of Nutritional Sciences, University of Shizuoka, 52-1 Yada, Shizuoka City 422, Japan

关键词: Regucalcin;    cDNA cloning;    Primary structure;    Rat liver;   

DOI  :  10.1016/0014-5793(93)80998-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cDNA of a Ca²⁺-binding protein regucalcin was cloned from a rat liver cDNA library which was constructed in λZAPII by immunoscreening. Positive clones were obtained from which spanned the region of interest, and they gave a sequence of 1.7 kb by sequencing with the dideoxynucleotide method. Analysis of the sequence of the cloned cDNA showed that the cDNA encoded the complete amino acid sequence of the regucalcin molecule. Regucalcin was composed of 299 amino acid residues and its molecular weight was estimated to be 33,388 Da. The hydropathy profile of regucalcin showed a highly hydrophilic character. The nucleotide and amino acid sequences of regucalcin did not have statistically significant homology, as compared with the registered sequences which are found in the EMBL and GenBank databases containing several other Ca²⁺-binding proteins (calmodulin, calbindin-D28k and S-100β). The regucalcin molecule did not contain the EF-hand motif as a Ca²⁺-binding domain. The present study demonstrates that regucalcin is a unique Ca²⁺-binding protein in the liver of rats.

【 授权许可】

Unknown