“…SLiMPrints specifically identifies the relatively overconstrained proximal groupings of residues within IDRs, indicative of putatively functional IDDs. 19 , 58 The enumerated motifs predicted within Ca V 3.2 IDRs suggest many possible functional peptides as hot-spots of functional IDDs, including proteolytic cleavage sites, ligand binding sites, posttranslational modification sites, and subcellular targeting sites. Notably, Ca V 3.2 IDRs contain several linear polybasic peptide (PBP) sequences composed of approximately 20 aa that are enriched with positively charged arginine (R) and lysine (K), other disordered aa, and phosphorylation sites that are clustered in ICL1-3 and C-terminus and can be considered as potential regulatory IDDs.…”