Data for evolutive analysis of insulin related peptides in bilaterian species

• Published in: Data in Brief
• Main Authors: Maëva Cherif--Feildel, Clothilde Heude Berthelin, Guillaume Rivière, Pascal Favrel, Kristell Kellner
• Format: Article in Journal/Newspaper
• Language: English
• Published: Elsevier 2019
• Subjects: Computer applications to medicine. Medical informatics; R858-859.7; Science (General); Q1-390; Crassostrea gigas
• Online Access: https://doi.org/10.1016/j.dib.2018.12.050; https://doaj.org/article/12426666d4874724976cf8558d6170c0

In bilaterian species, the amino acid sequence conservation between Insulin related peptides is relatively low except for the cysteine residues involved in the disulphide bonds. In the A chain, the conserved cystein residues are included in a signature motif. Investigating the variations in this motif would give insight into the phylogenetic history of the family. The table presented in this paper contains a large set of insulin-related peptides in bilateral phylogenetic groups (deuterostomian, ecdysozoan, lophotrochozoan). NCBI databases in silico wide screening combined with bibliographic researches provided a framework for identifying and categorising the structural characteristics of these insulin related peptides. The dataset includes NCBI IDs of each sequence with hyperlinks to FASTA format. Moreover, the structural type (α, β or γ), the A chain motif, the total number of cysteins, the C peptide cleavage mode and the potential additional domains (D or E) are specified for each sequence. The data are associated with the research article “Molecular evolution and functional characterisation of insulin-related peptides in molluscs: contributions of Crassostrea gigas genomic and transcriptomic-wide screening” [1]. The table presented here can be found at http://dx.doi.org/10.17632/w4gr8zcpk5.4#file-21c0f6a5-a3e3-4a15-86e0-e5a696458866.