data for evolutive analysis of insulin related peptides in bilaterian species

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].

在两侧对称生物中，除参与二硫键形成的半胱氨酸残基外，胰岛素相关肽的氨基酸序列保守性相对较低。在A链中，保守的半胱氨酸残基被纳入一个特征性基序之中。探究该基序的变异情况，将有助于揭示该家族的进化历史。本文中呈现的表格包含了大量双侧对称生物进化群体（如原口动物、节肢动物、棘层动物）中的胰岛素相关肽。通过NCBI数据库的虚拟广泛筛查与文献研究相结合，为识别和分类这些胰岛素相关肽的结构特征提供了一个框架。数据集包括每个序列的NCBI ID，并提供至FASTA格式的超链接。此外，对于每个序列，还指定了结构类型（α、β或γ）、A链基序、总半胱氨酸数、C肽切割方式以及潜在的额外结构域（D或E）。数据与研究论文《软体动物胰岛素相关肽的分子进化和功能特性：Crassostrea gigas基因组及转录组广泛筛查的贡献》[1]相关联。