[Comparative characteristics of the structure and function for syndecan-1 from animal organisms]

Syndecan-1 is a general representative of transmembrane proteoglycans known for their ability to perform diverse functions in multicellular organisms: to influence on cell interactions, to be act as a co-receptor and bind with to a large number ofligands and integrate them on the receptors, to fulfill the protective function, and to affect on wound repair and oncogenesis. Moreover, syndecan-1 as similar to the extracellular matrix plays an essential role in the development of organisms. Such a diversity of functions is associated with its structure. In this work we demonstrate that intracellular and intercellular domains of syndecan-1 are intrinsically disordered regions. Such structural feature allows them to bind with adapter proteins in the cytoplasm and be extended with glycosaminoglicans in the extracellular matrix, and to take part in the diverse and important cellular processes. The comparison of the occurrence of 20 amino acids for syndecan-1 from 32 animal organisms and 17 animal proteomes demonstrated that for the first such amino acids as glycine, treonine, glutamine, glutamic acid, and proline predominate on amount in the content of the former that results to the appearance of disordered regions in the proteins.