Structural homology of myosin alkali light chains, troponin C and carp calcium binding protein

Nature ◽  
1974 ◽  
Vol 252 (5485) ◽  
pp. 646-649 ◽  
Author(s):  
A. G. Weeds ◽  
A. D. McLachlan
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Light Chains ◽  
Structural Homology

The amino acid sequence of porcine intestinal calcium-binding protein

1979 ◽  
Vol 57 (6) ◽  
pp. 737-748 ◽  
Author(s):  
Theo Hofmann ◽  
Michiko Kawakami ◽  
Anthony J. W. Hitchman ◽  
Joan E. Harrison ◽  
Keith J. Dorrington
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intestinal Mucosa ◽  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

The complete amino acid sequence of the calcium-binding protein (CaBP) from pig intestinal mucosa has been determined: Ac-Ser-Ala-Gln-Lys-Ser-Pro-Ala-Glu-Leu-Lys-Ser-Ile-Phe-Glu-Lys-Tyr-Ala-Ala-Lys-Glu-Gly-Asp-Pro-Asn-Gln-Leu-Ser-Lys-Glu-Glu-Leu-Lys-Gln-Leu-Ile-Gln-Ala-Glu-Phe-Pro-Ser-Leu-Leu-Lys-Gly-Pro-Arg-Thr-Leu-Asp-Asp-Leu-Phe-Gln-Glu-Leu-Asp-Lys-Asn-Gly-Asn-Gly-Glu-Val-Ser-Phe-Glu-Glu-Phe-Gln-Val-Leu-Val-Lys-Lys-Ile-Ser-Gln-OH. The N-terminal octapeptide sequence was determined by mass spectrometry analysis by Morris and Dell. The first 45 residues of bovine CaBP differ only in six positions from the corresponding sequence of the porcine protein, except that the sequence starts in position two of the porcine sequence. The mammalian intestinal CaBP's belong to the troponin-C superfamily on the basis of an analysis by Barker and Dayhoff.

Analysis of the complete sequence of a muscle calcium-binding protein of Schistosoma mansoni

Parasitology ◽  
1992 ◽  
Vol 105 (3) ◽  
pp. 399-408 ◽  
Author(s):  
T. J. Stewart ◽  
A. L. Smith ◽  
J. C. Havercroft
Keyword(s):  
Schistosoma Mansoni ◽  
Light Chain ◽  
Calcium Binding ◽  
Binding Protein ◽  
Complete Sequence ◽  
Regulatory Light Chain ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Predicted Amino Acid Sequence ◽  
Ef Hand

SUMMARYThe complete sequence of the cDNA encoding a 20 kDa calcium-binding protein of Schistosoma mansoni (Sm20) has been determined. The predicted amino acid sequence contains 4 EF hand domains but examination of the predicted secondary structure of Sm20, together with the specific residues in each calcium-binding domain, suggests that only 1 EF hand (domain IV) is functional. Sm20 is most homologous to calmodulin, troponin C and the regulatory light-chain of myosin, particularly those of invertebrates. However, troponin C and the regulatory light-chain of myosin can be distinguished from Sm20 by size and by their differential levels of expression during the life-cycle. Sm20 also appears to be distinct from calmodulin but may be functionally equivalent to the soluble sarcoplasmic calcium-binding proteins of molluscs and crustacea which may act as a reservoir for calcium in muscle. Sm20 is encoded by a small multi-gene family whose members are clustered within a 15 kb region of the genome. A 20 kDa antigen, cross-reactive with Sm20, is expressed in Schistosoma haematobium, Fasciola hepatica and Paragonomus mexicanus.

Calcium-binding protein 1 of Entamoeba histolytica transiently associates with phagocytic cups in a calcium-independent manner

2008 ◽  
Vol 10 (6) ◽  
pp. 1373-1389 ◽  
Author(s):  
Ruchi Jain ◽  
Julien Santi-Rocca ◽  
Narendra Padhan ◽  
Sudha Bhattacharya ◽  
Nancy Guillen ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Independent Manner ◽  
Phagocytic Cups

scholarly journals Regulation of adenylate cyclase from glial tumor cells by calcium and a calcium-binding protein.

1976 ◽  
Vol 251 (15) ◽  
pp. 4744-4750 ◽  
Author(s):  
M A Brostrom ◽  
C O Brostrom ◽  
B M Breckenridge ◽  
D J Wolff
Keyword(s):  
Adenylate Cyclase ◽  
Tumor Cells ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Glial Tumor
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