The relative positioning of these residues on the modeled tertiary structure of novel CEA protein domains revealed that they are, also, spatially conserved. A series of evolutionarily conserved amino acid residues, functionally important, were identified. The domain organization of the retrieved protein sequences was analyzed, and, subsequently, comprehensive phylogenetic analyses of the entire length CEA homologous proteins were performed. Toward this end, the publicly available genomes were searched extensively for CEA homologs. Taking into account this characteristic, we made an effort to reconstruct the evolutionary history of the CEA gene family. Of particular interest, the well-studied human and mouse CEA genes are arranged in clusters in a single chromosome. In general, the CEA-encoded proteins are composed of an extracellular region with Ig variable and constant-like domains and a cytoplasmic region containing signaling motifs. The CEA family members are implicated in pleiotropic (patho)physiological functions including cell–cell adhesion, pregnancy, immunity, neovascularization, regulation of insulin homeostasis, and carcinogenesis.
The CEA family is divided into two groups, the carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) and the pregnancy-specific glycoproteins. The carcinoembryonic antigen ( CEA) gene family belongs to the immunoglobulin (Ig) superfamily and codes for a vast number of glycoproteins that differ greatly both in amino acid composition and function.
0 kommentar(er)
