Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin potently blocks mammalian N-type calcium channels (Cav2.2/CACNA1B) (IC(50)=330 nM on human channels). It is 9-fold more potent in displacing radiolabeled omega-conotoxin GVIA from fish brain membranes than from human SH-SY5Y cells. Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin potently blocks mammalian N-type calcium channels (Cav2.2/CACNA1B) (IC(50)=600 nM on human channels). It is 60-fold more potent in displacing radiolabeled omega-conotoxin GVIA from fish brain membranes than from human SH-SY5Y cells. In vivo, when tested on rat neuropathic pain model, this toxin shows an analgesic activity (PubMed:30194442). Expressed by the venom duct. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. The cysteine framework is VI/VII (C-C-CC-C-C). C.moncuri is a vermivorous cone snail. Both MoVIA and MoVIB have an Arg-58 (Arg-13 in mature peptides) that replaces the functionnally critical Tyr-13 found in potent Cav2.2/CACNA1B inhibitors from fish-hunting species (such as MVIIA (AC P05484) and GVIA (AC P01522)). Belongs to the conotoxin O1 superfamily.