Background: Microneme protein 3 (MIC3) is a key adhesion molecule in Methods: A comprehensive set of bioinformatics tools and web servers was employed to predict the physicochemical properties, allergenicity, antigenicity, solubility, post-translational modification sites, subcellular localization, transmembrane domains, signal peptides, secondary and tertiary structures, potential B- and T-lymphocyte epitopes, and simulated immune responses of the TgMIC3 protein. Results: A total of 75 post-translational modification sites were predicted in TgMIC3. Furthermore, secondary structure analysis using GOR IV, SOPMA, and NetSurfP-3.0 indicated that random coils and extended strands were the predominant structural elements. In addition, several high-affinity B- and T-cell epitopes were identified across the protein sequence. Subsequent structural validation revealed that 82.91% and 98.60% of residues were located in favored regions in the initial and refined 3D models, respectively. The findings of the allergenicity and antigenicity assessments indicated that the MIC3 antigen seemed to be a non-allergen with an immunogenic nature. Moreover, immune simulation using the C-ImmSim server demonstrated that TgMIC3 could induce robust humoral and cell-mediated immune responses following three simulated antigen administrations.