Other goals are to determine the diversity in the evolution of this protein in different taxa, the possible horizontal gene transfers, and the correlation of molecular features in the sequences within primates and arthropod groups. But it is important to stress that the protein activity seems be intact or just slightly reduced, once its activity is essential to keep the health in animals. Tollip participates in several immune pathways, mediated or not by Myd88, modulating the responses and the loss or reduction of its affinity to molecular complexes made between it and several other compounds, like IRAK-1, could trigger an exaggerated response of the immune system, leading to death in some cases. Though, there are studies, like Didierlaurent’s, which affirm that mice lacking Tollip become healthy and fertile. Despite all identified polymorphisms and mutations of Tollip, we could not make any inferences about its role in the TLRtriggering activation of dendritic cells, without more in vitro and in vivo tests. Although, some studies have revealed that Tollip does not have a fundamental function in the TLRtriggering activation pathway of dendritic cells. Mutant mice lacking the tollip gene, when compared with wild-type mice, have been shown to not have significant differences. Therefore, mutations in key-residues for Tollip activity does not imply differences at the activation level of dendritic cells. Tollip presents diverse evolutionary tendencies and several of them are indicating successive modifications in the protein structure, in order to stabilize the tertiary structure accumulating aliphatic residues. Primates generally have more unstable proteins, while arthropods have more stability at ININ, AI and GRAVY level. Size was not correlated with any groups and seems to be highly variable in all groups. In/del trends were saw as very frequent. The three dimensional structure analysis revealed the modular characteristic of this protein and the necessity of Ca2+ to keep the correct pocket of C2 domain. Ligand association studies revealed that 768 ligand probably could inhibit the Tollip activity. Positively selected residues were found in almost all domains, but a considerable part of them are relatively conserved, indicating a conservation of active pockets, which is consistent with maintaining protein right activity. The tested animal groups were differentially grouped, when studied with parsimonious and nonparsimonious residues, and revealed through molecular clock analysis that they present different selection and evolving speeds. The recombination supports diverse incongruences observed in the phylogenetic trees obtained with complete and cured Tollip data sets. There are no evidences that support a homogeneity in this immunologic pathway, once Tollip presented evolving trends that are not constant for all groups. Summarizing, some groups are highly evolutionary closed, as arthropods and primates.