Premium
Gene structure of calcium‐dependent protease retains the ancestral organization of the calcium‐binding protein gene
Author(s) -
Emori Yasufumi,
Ohno Shigeo,
Tobita Masako,
Suzuki Koichi
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80094-1
Subject(s) - protease , calcium binding protein , exon , calcium , calmodulin , gene , tmprss6 , gene duplication , ef hand , binding domain , biochemistry , chemistry , binding protein , biology , peptide sequence , genetics , binding site , microbiology and biotechnology , enzyme , serine protease , organic chemistry
The gene structure of calcium‐dependent protease (Ca 2+ ‐protease) was determined. It comprises at least 21 exons, and these were assigned to the 4 functional domains of the protease. The protease domain does not show clear correlation between exons and functional units, but the calmodulin‐like calcium‐binding domain shows strong correlation. Each of the 4 consecutive calcium‐binding regions in the C‐terminal part of Ca 2+ ‐protease is encoded by one exon. This gene structure supports the idea that the 4 calcium‐binding regions of calcium‐binding proteins such as calmodulin arose by 2 steps of gene duplication.