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Gene structure of calcium-dependent protease retains the ancestral organization of the calcium-binding protein gene.
The gene structure of calcium-dependent protease (Ca2+-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 Ca2+-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.
PMID: 3000828 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Isolation and characterization of the human diacylglycerol kinase gene.
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[Biochem J. 1993]
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CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells.
Theopold U, Pintér M, Daffre S, Tryselius Y, Friedrich P, Nässel DR, Hultmark D.
Mol Cell Biol. 1995 Feb; 15(2):824-34.
[Mol Cell Biol. 1995]
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Structure and nucleotide sequence of the rat intestinal vitamin D-dependent calcium binding protein gene.
Krisinger J, Darwish H, Maeda N, DeLuca HF.
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[Proc Natl Acad Sci U S A. 1988]
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