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J. Biol. Chem., Vol. 263, Issue 18, 8958-8964, 06, 1988
BT Scott, HK Simmerman, JH Collins, B Nadal-Ginard and LR Jones
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.
Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning
Krannert Institute of Cardiology, Indiana University School of Medicine, Indianapolis 46202.
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