Fig. 3

Comparison of the predicted amino acid sequences of GRs from different species. The amino acid sequence of the dog GR was aligned with that of human, mouse, and guinea pig GRs using Clustal W software. The “*” below columns in the amino acid sequences indicate that the residues in that column are identical in all sequences in the alignment. The “:” and “.” symbols indicate that semiconserved substitutions were observed. Numbers to the right refer to amino acid positions. GR amino acid sequences were obtained from the NCBI database (NP_000167.1 for human, P06537.1 for mouse, and NP_01166458.1 for guinea pig). The GR is composed of four domains, which are shown in shaded boxes: N-terminal regulatory domain, DNA-binding domain, hinge region, and ligand-binding domain. Each domain was defined according to the domain composition of the human GR. Closed circles, closed boxes, open box, and closed triangles indicate phosphorylation sites, SUMOylation sites, ubiquitination site, and acetylation sites, respectively, which were identified in the human GR. Stars indicate known mutation sites in the human GR associated with natural resistance