GenBank-Updates@genbank.bio.net (03/27/91)
LOCUS SYNCAM 450 bp ds-DNA SYN 27-MAR-1991
DEFINITION Synthetic VU-1 calmodulin gene, complete cds.
ACCESSION M11334 M19293 M19294
KEYWORDS calcium-binding protein; calmodulin.
SOURCE Sixty-one chemically synthesized DNA fragments, clone pVUC-1.
ORGANISM Artificial gene
Artificial sequences; Genes.
REFERENCE 1 (bases 1 to 450)
AUTHORS Roberts,D.M., Crea,R., Malecha,M., Alvarado-Urbina,G.,
Chiarello,R.H. and Watterson,D.M.
TITLE Chemical synthesis and expression of a calmodulin gene designed for
site-specific mutagenesis
JOURNAL Biochemistry 24, 5090-5098 (1985)
STANDARD simple staff_review
REFERENCE 2 (bases 306 to 450)
AUTHORS Roberts,D.M., Rowe,P.M., Siegel,F.L., Lukas,T.J. and Watterson,D.M.
TITLE Trimethyllysine and protein function: Effect of methylation and
mutagenesis of lysine 115 of calmodulin on NAD kinase activation
JOURNAL J. Biol. Chem. 261, 1491-1494 (1986)
STANDARD simple staff_review
REFERENCE 3 (bases 1 to 450)
AUTHORS Craig,T.A., Watterson,D.M., Prendergast,F.G., Haiech,J. and
Roberts,D.M.
TITLE Site-specific mutagenesis of the alpha-helices of calmodulin:
Effects of altering a charge cluster in the helix that links the
two halves of calmodulin
JOURNAL J. Biol. Chem. 262, 3278-3284 (1987)
STANDARD full staff_entry
REFERENCE 4 (bases 1 to 450)
AUTHORS Kilhoffer,M.-C., Roberts,D.M., Adibi,A.O., Watterson,D.M. and
Haiech,J.
TITLE Investigation of the mechanism of calcium binding to calmodulin:
Use of an isofunctional mutant with a tryptophan introduced
JOURNAL J. Biol. Chem. 263, 17023-17029 (1988)
STANDARD full staff_entry
REFERENCE 5 (sites)
AUTHORS Weber,P.C., Lukas,T.J., Craig,T.A., Wilson,E., King,M.M. and
Kwiatkowski,A.P.
TITLE Computational and site-specific mutagenesis analyses of the
asymmetric charge distribution on calmodulin
JOURNAL Proteins 6, 70-75 (1989)
STANDARD full staff_review
REFERENCE 6 (sites)
AUTHORS Shoemaker,M.O., Lau,W., Shattuck,R.L., Kwiatkowski,A.P.,
Matrisian,P.E., Guerra-Santos,L., Wilson,E., Lukas,T.J., Van
Eldik,L.J. and Watterson,D.M.
TITLE Use of DNA Sequence and Mutant Analyses and Antisense
Oligodeoxynucleotides to Examine the Molecular Basis of Nonmuscle
Myosin Light Chain Kinase Autoinhibition, Calmodulin Recognition,
and Activity
JOURNAL J. Cell Biol. 111, 1107-1125 (1990)
STANDARD full staff_review
REFERENCE 7 (sites)
AUTHORS Massom,L.R., Lukas,T.J., Persechini,A., Kretsinger,R.H.,
Watterson,D.M. and Jarrett,H.W.
TITLE Trifluoperazine Binding to Mutant Calmodulins
JOURNAL Biochemistry 30, 663-667 (1991)
STANDARD full staff_review
REFERENCE 8 (sites)
AUTHORS Haiech,J., Kilhoffer,M.-C., Lukas,T.J., Craig,T.A., Roberts,D.M.
and Watterson,D.M.
TITLE Restoration of the Calcium Binding Activity of Mutant Calmodulins
Towards Normal by the Presence of a Calmodulin Binding Structure
JOURNAL J. Biol. Chem. (1991) In press
STANDARD full staff_review
COMMENT Draft entry and computer-readable sequence for [Biochemistry 24,
5090-5098 (1985)],[J. Biol. Chem. 261, 1491-1494 (1986)] kindly
provided by T.Craig, 04-JAN-1988.
The synthetic calmodulin gene presented here is a hybrid of higher
plant and vertebrate calmodulins that are indistinguishable in
terms of phosphodiesterase and myosin light chain kinase activator
activities but have readily distinguishable NAD kinase activator
properties.
FEATURES Location/Qualifiers
CDS 1..450
/note="synthetic calmodulin"
/codon_start=1
mutation 247..247
/note="g in [Biochemistry 24, 5090-5098 (1985)]; a in [J.
Biol. Chem. 262, 3278-3284 (1987)] (Glu->Lys)"
mutation 249..249
/note="a in [Biochemistry 24, 5090-5098 (1985)]; g in [J.
Biol. Chem. 262, 3278-3284 (1987)] (Glu->Lys)"
mutation 250..250
/note="g in [Biochemistry 24, 5090-5098 (1985)]; a in [J.
Biol. Chem. 262, 3278-3284 (1987)] (Glu->Lys)"
mutation 253..253
/note="g in [Biochemistry 24, 5090-5098 (1985)]; a in [J.
Biol. Chem. 262, 3278-3284 (1987)] (Glu->Lys)"
mutation 299..299
/note="t in [Biochemistry 24, 5090-5098 (1985)]; g in [J.
Biol. Chem. 263, 17023-17029 (1988)] (Phe->Trp)"
mutation 300..300
/note="c in [Biochemistry 24, 5090-5098 (1985)]; g in [J.
Biol. Chem. 263, 17023-17029 (1988)] (Phe->Trp)"
mutation 346..346
/note="a in [Biochemistry 24, 5090-5098 (1985)]; c in [J.
Biol. Chem. 261, 1491-1494 (1986)] (Lys->Arg)"
mutation 347..347
/note="a in [Biochemistry 24, 5090-5098 (1985)]; g in [J.
Biol. Chem. 261, 1491-1494 (1986)] (Lys->Arg)"
mutation 348..348
/note="g in [Biochemistry 24, 5090-5098 (1985)]; t in [J.
Biol. Chem. 261, 1491-1494 (1986)] (Lys->Arg)"
BASE COUNT 125 a 101 c 123 g 101 t
ORIGIN
1 atggctgatc agctgactga cgagcagatc gctgaattta aagaggcttt ctctctgttt
61 gacaaagacg gtgacggtac catcactacc aaagagctcg gcaccgttat gcgcagcctt
121 ggccagaacc cgactgaagc tgaactgcag gacatgatta acgaagtcga cgctgacggt
181 aacggcacca tcgattttcc ggaatttctg aacctgatgg cgcgcaagat gaaagacact
241 gactctgaag aggaactgaa agaggccttc cgtgttttcg acaaagacgg taacggtttc
301 atctcggccg ctgaactgcg tcacgttatg actaacctgg gtgaaaagct tactgacgaa
361 gaagttgacg aaatgattcg cgaagctgac gtcgatggtg acggccaggt taactacgaa
421 gagttcgttc aggttatgat ggctaagtag
//