Abstract
The mammalian CIP/KIP family proteins are intrinsically disordered proteins (IDPs) that can regulate various cellular processes. However, many reports have shown that IDPs generally evolve more rapidly than ordered proteins. Here, to elucidate the functional adaptability of CIP/KIP proteins in vertebrate, we analysed the rates of evolution in relation to their structural and sequence properties and predicted the post-translational modification based on the sequence data. The results showed that CIP/KIP proteins generally could maintain their function through evolution in the vertebrate. Basically, the disordered region that acts as a flexible linker or spacer has a conserved propensity for structural disorder and a persistent, fast rate of amino acid substitution, which could result in a significantly faster rate of evolution compared to the ordered proteins. Describing the pattern of structural order-disorder evolution, this study may give an insight into the well-known characteristics of IDPs in the evolution of CIP/KIP proteins.
Highlights
The primary sequence of intrinsically disordered proteins (IDPs) is composed of a high proportion of charged and polar amino acids and is deficient of bulky hydrophobic amino acids[21,22]
The CDI/KID domain was encountered through pfam for all CIP/KIP members in all species, and there were two CDI/KID domains found for p21 of amphibian
Consistent with this, the prediction of order-disorder propensity of CIP/KIP proteins in this study showed that these proteins are highly disordered in structure
Summary
The primary sequence of IDPs is composed of a high proportion of charged and polar amino acids and is deficient of bulky hydrophobic amino acids[21,22] These characteristics may result in a flexible conformation of disordered regions, which are unable to fold spontaneously into three-dimensional structures and tend to adopt specific tertiary conformations, at least locally, only after binding to their partners[21,22,23]. Disordered regions can retain their structure without ever becoming structured or showing the so-called “fuzziness” phenomenon and may function as flexible linkers or spacers[23,26,27] These characteristics have consequences for IDP ability to exhibit functional promiscuity under different conditions[23]. We predicted and examined the phosphorylation and the conserved phosphorylation sites, respectively
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