Fig. 2: Characterised protein domains and functions in full-length KIF1A.
From: KIF1A-associated neurological disorders: therapeutic opportunities and challenges
a Schematic representation of the domain structure of full-length KIF1A with residue numbers based on the primary assembly isoform (NP_001230937.1, 1791 amino acids (aa)). Domains include MD motor domain (4-361 aa), NC neck coil (366-383 aa), CC1 coiled-coil 1 (438-471 aa), FHA forkhead associated domain (501-614 aa), CC2 coiled-coil 2 (631-690 aa), CC3 coiled-coil 3 (810-831 aa), PH pleckstrin homology domain (1673-1770 aa). According to Stucchi et al., residues 680-1113 form the binding region for liprin-alpha, TANC2 and calmodulin (CaM)-binding regions (LBD) [23]. The figure was generated using Illustrator of Biological Sequences (IBS) [64]. b Schematic of the KIF1A protein showing the transition from an inactive monomeric state to an active dimeric state upon binding with cargo, illustrating the process of autoinhibition release. The figure was not drawn to scale and was created in BioRender. Christodoulou (2025) https://BioRender.com/y61l493.
