Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequence
- 15 September 1986
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 205 (2), 313-317
- https://doi.org/10.1016/0014-5793(86)80919-x
Abstract
The complete amino acid sequence of the large subunit (catalytic subunit) of human low-Ca2+ requiring-calcium-activated neutral protease (μCANP) was deduced from its cDNA base sequence. It is composed of 714 amino acid residues and its sequence is highly homologous to the chicken CANP sequence determined previously. Human μCANP, like chicken CANP, has a clear 4-domain structure, and their fundamental structures are essentially the same, although their Ca2+sensitivities are significantly different. The role of each domain in the Ca2+sensitivity and protease activity of CANP is discussed on the basis of sequence comparison.Keywords
This publication has 14 references indexed in Scilit:
- Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease.Journal of Biological Chemistry, 1986
- Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?Nature, 1984
- Reconstitution of calpain I and calpain II from their subunits: Interchangeability of the light subunitsArchives of Biochemistry and Biophysics, 1984
- Comparison of Calcium-Activated Neutral Proteases from Skeletal Muscle of Rabbit and ChickenThe Journal of Biochemistry, 1984
- A simple and very efficient method for generating cDNA librariesGene, 1983
- Amino acid sequence around the active site cysteine residue of calcium‐activated neutral protease (CANP)FEBS Letters, 1983
- Calcium-Dependent Neutral Protease: Its Characterization and RegulationPublished by Elsevier BV ,1982
- [57] Sequencing end-labeled DNA with base-specific chemical cleavagesMethods in enzymology, 1980
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979
- Troponin and Parvalbumin Calcium Binding Regions Predicted in Myosin Light Chain and T4 LysozymeScience, 1975