Alpha-D-conopeptides act as non-competitive inhibitors of nicotinic acetylcholine receptors (nAChR). This toxin has strong inhibitory activity on rat alpha-9-alpha-10 (CHRNA9/CHRNA10) (IC(50)=1.2 nM) and a moderate inhibitory activity on human alpha-7 (CHRNA7) (IC(50)=210 nM), rat alpha-3-beta-2 (CHRNA3/CHRNB2) (IC(50)=498 nM), rat alpha-3-beta-4 (CHRNA3/CHRNB4) (IC(50)=614 nM) and rat alpha-1-beta-1-delta-epsilon (CHRNA1/CHRNB1/CHRNE/CHRND) (IC(50)=743 nM) subtypes. Shows a weaker inhibitory activity on human alpha-9-alpha-10 (IC(50)=28 nM) than on the rat channel. This is explained by a different residue in the probable binding site (His-31 in rat alpha-10 and Leu-31 in human). Expressed by the venom duct. Displays a mini-granulin fold, a structure composed of two short, stacked beta-hairpins connected by two parallel disulfide bonds. This newly described fold is derived from the same cysteine connectivity as knottins (ICK fold). The name 'mini-granulin fold' comes from the structural homology with the N-terminal region of the human granulin. The cysteine framework is XX (C-CC-C-CC-C-C-C-C). Shows a very weak activity on alpha-4-beta-2 and alpha-4-beta-4 nAChR subtypes. The Val-47 is found by direct protein sequencing in the protein described in Xu et al., 2015, and in the translated sequence in Yao et al., 2019. The Ile-47 is only found in the translated sequence described in Xu et al., 2015. Belongs to the conotoxin D superfamily.