A glycine and proline-rich antibacterial protein was cloned from larvae of a beetle, Protaetia brevitarsis. The DNAs encoded a deduced propeptide of 127 amino acid residues with predicted molecular weight of 14.0 kDa and PI of 7.89. Structural analysis of this protein indicated the presence of a recognition sequence for the cleavage site within the constitutive secretory pathway(Arg-Xaa-Lys/Arg-Arg), suggesting that mature portion(72 amino acid residues) is produced by cleavage of signal peptide and propeptide from 127 amino-acid-long precursor protein. Mature portion sequence of this protein showed 72% similarity to that of Oryctes rhinoceros Rhinocerosin and 91% to that of Holotrichia diomphalia holotricin 2. The mRNA expression was reached the highest level at 4 hrs after E. coli injection and then declined gradually.