Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (PubMed:14630920). Probably, required for the degradation of the old cuticle (PubMed:14630920). Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity. The disulfide bridge formed between Cys-38 in the propeptide and the active site residue Cys-95 may prevent activation of the zymogen through formation of a reversible covalent bond with the active site residue. In molting larvae, localizes in both the new and old cuticles, specifically at the interface where the old cuticle is being degraded before ecdysis (PubMed:14630920). Localizes to yolk granules in the developing oocyte (PubMed:16857685). Expressed in hypodermis, cuticle and pharynx (at protein level) (PubMed:14630920, PubMed:16857685). Expressed in germ cells, developing oocytes, sheath cells surrounding germ cells and oocytes, and in the eggshell (at protein level) (PubMed:16857685). Not expressed in sperm (PubMed:16857685). Expressed in embryos, larvae and adults (at protein level) (PubMed:14630920, PubMed:16857685). In larvae, only expressed in hypodermis and cuticle (at protein level) (PubMed:14630920, PubMed:16857685). Expressed in the ecdysed cuticle during molting (at protein level) (PubMed:16857685). Expression transiently increases during early embryonic stages and prior to the larval L2/L3, L3/L4 and L4/adult molts (PubMed:14630920, PubMed:16857685). RNAi-mediated knockdown causes an arrest at the 50-cell embryonic stage. The few surviving animals are arrested at the larval L2 to L3 molt with their cuticle remaining attached to the mid-portion of the body. RNAi-mediated knockdown at various larval stages causes severe defects in molting. Belongs to the peptidase C1 family.