Mammalian tropoelastin: multiple domains of the protein define an evolutionarily divergent amino acid sequence.

We have recently derived the complete amino acid sequence of rat tropoelastin from a series of overlapping cDNA clones. Comparison of this protein sequence to bovine and human tropoelastin has revealed significant differences in the rates of evolutionary divergence of the various domains of tropoelastin. The overall rate of divergence of the hydrophobic domains of tropoelastin was twice as fast as the cross-link domains of the protein. Certain hydrophobic domains, however, are as conserved as cross-link regions, particularly the hydrophobic sequence coded for by exon 33, the only exon subject to alternate usage in all three mammalian species and the most conserved domain in rat, bovine and human tropoelastin. This conservation of sequence strongly suggests a more complex function of the hydrophobic region encoded by exon 33, beyond the elastic recoil characteristic of all hydrophobic domains of tropoelastin. A comparison of average rates of divergence of hydrophobic and cross-link domains of tropoelastin to functionally-defined domains of other structural proteins, such as collagen, has also revealed that overall, tropoelastin is a highly divergent amino acid sequence, comparable to proteins such as globin and the fibrino-peptides.