JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Collins, J. H.
Right arrow Articles by Theibert, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Collins, J. H.
Right arrow Articles by Theibert, J. L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 263, Issue 30, 15378-15385, Oct, 1988

Amino acid sequence of a sarcoplasmic calcium-binding protein from the sandworm Nereis diversicolor

JH Collins, JA Cox and JL Theibert
Department of Biological Chemistry, School of Medicine, University of Maryland, Baltimore 21201.

Muscles of invertebrate species contain abundant quantities of soluble, sarcoplasmic, high affinity Ca2+-binding proteins (SCBPs). The SCBPs belong to the calmodulin superfamily and contain four homologous domains (I-IV) which arose by reduplication of a gene for a small ancestral protein. We have determined the amino acid sequence of the SCBP from the sandworm Nereis diversicolor. This protein is the only SCBP which has been crystallized in a form suitable for three- dimensional structure determination by high-resolution x-ray analysis (Babu, Y. S., Cox, J. A., and Cook, W. J. (1987) J. Biol. Chem. 262, 11184-11185). N. diversicolor SCBP is a single polypeptide chain of 174 amino acids, including single residues of glutamine and histidine, 2 tyrosines, and 3 tryptophans. It is devoid of cysteine and has an acetylated amino terminus, a calculated Mr of 19,485, and a net charge of -13 at neutral pH. There was no evidence for heterogeneity in the sequence. Probable Ca2+-binding sites were recognized in domains I, III, and IV. Comparison with other available invertebrate SCBP sequences shows an unusually high degree of variability among these proteins, with only 9 residues common to all species.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Physiol. Rev.Home page
S. L. Hooper and J. B. Thuma
Invertebrate Muscles: Muscle Specific Genes and Proteins
Physiol Rev, July 1, 2005; 85(3): 1001 - 1060.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. Sillen, S. Verheyden, L. Delfosse, T. Braem, J. Robben, G. Volckaert, and Y. Engelborghs
Mechanism of Fluorescence and Conformational Changes of the Sarcoplasmic Calcium Binding Protein of the Sand Worm Nereis diversicolor upon Ca2+ or Mg2+ Binding
Biophys. J., September 1, 2003; 85(3): 1882 - 1893.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Fulton, E. Y. Lai, and S. P. Remillard
A Flagellar Calmodulin Gene of Naegleria, Coexpressed during Differentiation with Flagellar Tubulin Genes, Shares DNA, RNA, and Encoded Protein Sequence Elements
J. Biol. Chem., March 17, 1995; 270(11): 5839 - 5848.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1988 by the American Society for Biochemistry and Molecular Biology.