Centipedes are one of the oldest venomous animals and use their venoms as weapons to attack prey orprotect themselves. Their venoms contain various components with different biomedical andpharmacological properties. However, little attention has been paid to the profiles and diversity of theirtoxin-like proteins/peptides. In this study, we used a proteotranscriptomic approach to uncover thediversity of centipede toxin-like proteins in Scolopendra subspinipes mutilans. Nine hundred twenty-three and 6,736 peptides, which were separately isolated from venom and torso tissues, respectively, wereidentified by ESI-MS/MS and deduced from their transcriptomes. Finally, 1,369 unique proteins wereidentified in the proteome, including 100 proteins that exhibited overlapping expression in venom andtorso tissues. Of these proteins, at least 40 proteins were identified as venom toxin-like proteins.Meanwhile, transcriptome mining identified approximately 10-fold more toxin-like proteins and enabledthe characterization of the precursor architecture of mature toxin-like peptides. Importantly, combinedwith proteomic and transcriptomic analyses, 25 toxin-like proteins/peptides (neurotoxins accounted for50%) were expressed outside the venom gland and involved in gene recruitment processes. Thesefindings highlight the extensive diversity of centipede toxin-like proteins and provide a new foundationfor the medical-pharmaceutical use of centipede toxin-like proteins. Moreover, we are the first group toreport the gene recruitment activity of venom toxin-like proteins in centipede, similar to snakes.