Document Detail


Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning.
MedLine Citation:
PMID:  3379055     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
cDNA cloning was used to deduce the complete amino acid sequence of canine cardiac calsequestrin, the principal Ca2+-binding protein of cardiac junctional sarcoplasmic reticulum. Cardiac calsequestrin contains 391 amino acid residues plus a 19-residue amino-terminal signal sequence. The molecular weight of the mature protein, excluding carbohydrate, is 45,269. Cardiac calsequestrin is highly acidic, and a striking feature is the enrichment of acidic residues (60%) within the 63 carboxyl-terminal residues. No part of the sequence contains EF hand Ca2+-binding structures. The photo-affinity probe 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine was used to localize the Ca2+-regulated hydrophobic site to amino acid residues 192-223. The cardiac and skeletal muscle isoforms of calsequestrin (Fliegel, L., Ohnishi, M., Carpenter, M. R., Khanna, V. K., Reithmeier, R. A. F., and MacLennan, D. H. (1987) Proc. Natl. Acad. Sci. U. S. A. 84, 1167-1171), although the products of different genes, are 65% identical, are acidic, and share one glycosylation site. However, cardiac calsequestrin has several unique features. First, it has a 31-amino acid extension at its carboxyl terminus (residues 361-391), which contains 71% acidic residues and a second glycosylation site. Second, its mRNA contains a second open reading frame with the capacity to code for a 111-amino acid protein. Third, contrary to the restricted expression of the fast skeletal isoform, cardiac calsequestrin mRNA is present in both cardiac and slow skeletal muscle, but not in fast skeletal muscle. We conclude that the deduced amino acid sequence of cardiac calsequestrin is consistent with its ability to bind large amounts of Ca2+ (40 mol of Ca2+/mol of calsequestrin). The protein probably binds Ca2+ by acting as a charged surface rather than by presenting multiple discrete Ca2+-binding sites.
Authors:
B T Scott; H K Simmerman; J H Collins; B Nadal-Ginard; L R Jones
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  263     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1988 Jun 
Date Detail:
Created Date:  1988-07-27     Completed Date:  1988-07-27     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8958-64     Citation Subset:  IM    
Affiliation:
Krannert Institute of Cardiology, Indiana University School of Medicine, Indianapolis 46202.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/J03766
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Calsequestrin / genetics*
Cloning, Molecular*
DNA / genetics*
Dogs
Genes*
Molecular Sequence Data
Muscle Proteins / genetics*
Muscles / metabolism
Myocardium / metabolism*
Peptide Fragments / analysis
Protein Conformation
Rabbits
Sequence Homology, Nucleic Acid
Trypsin
Chemical
Reg. No./Substance:
0/Calsequestrin; 0/Muscle Proteins; 0/Peptide Fragments; 9007-49-2/DNA; EC 3.4.21.4/Trypsin

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