TitleCharacterization of a novel EF-hand homologue, CnidEF, in the sea anemone Anthopleura elegantissima
Publication TypeJournal Article
Year of Publication2007
AuthorsHauck, LL, Phillips, WS, Weis, VM
JournalComparative Biochemistry and Physiology B-Biochemistry & Molecular Biology
Volume146
Pagination551-559
Type of ArticleJournal Article
ISSN1096-4959
Abstract

The superfamily of EF-hand proteins is comprised of a large and diverse group of proteins that contain one or more characteristic EF-hand calcium-binding domains. This study describes and characterizes a novel EF-hand cDNA, CnidEF, from the sea anemone Anthopleura elegantissima (Phylum Cnidaria, Class Anthozoa). CnidEF was found to contain two EF-hand motifs near the C-terminus of the deduced amino acid sequence and two regions near the N-terminus that could represent degenerate EF-hand motifs. CnidEF homologues were also identified from two other sea anemone species. A combination of bioinformatic and molecular phylogenetic analyses was used to compare CnidEF to EF-hand proteins in other organisms. The closest homologues identified from these analyses were a luciferin binding protein (LBP) involved in the bioluminescence of the anthozoan Renilla reniformis, and a sarcoplasmic calcium-binding protein (SARC) involved in fluorescence of the annelid worm Nereis diversicolor. Predicted structure and folding analysis revealed a close association with bioluminescent aequorin (AEQ) proteins from the hydrozoan cnidarian Aequorea aequorea. Neighbor-joining analyses grouped CnidEF within the SARC lineage along with AEQ and other cnidarian bioluminescent proteins rather than in the lineage containing calmodulin (CAM) and troponin-C (TNC). (c) 2007 Elsevier Inc. All rights reserved.

URL<Go to ISI>://WOS:000245330400014
DOI10.1016/j.cbpb.2006.12.004