| Domain/Region | Amino Acid Range (approximate) | Function | Evidence |
|---|---|---|---|
| N-terminal domain | aa 1-147 (*Chlamydomonas* IFT46) | Predicted intrinsically disordered region that binds the cargo adapter ODA16 and is required for efficient outer dynein arm (ODA) transport; this N-terminal ODA16-binding function is conserved mainly in organisms with motile cilia | Reviews and primary studies describe direct ODA16 interaction with the IFT46 N-terminus, and truncation causes strong ODA loss from flagella (pqac-00000002, pqac-00000003, pqac-00000027, pqac-00000028) |
| Assembly-critical internal segment | aa 26-50 | Required for functional rescue of flagellar assembly in *Chlamydomonas* ift46 mutants; indicates this short N-proximal segment contributes to core ciliogenic activity beyond the extreme N-terminus | Recombinant rescue experiments showed aa 26-50 are necessary for flagellar assembly rescue, whereas the first 25 aa are dispensable (pqac-00000024, pqac-00000029) |
| C-terminal domain / BBTS3 | aa 246-321 | Basal body targeting sequence (BBTS3); mediates recruitment to basal bodies/ciliary base, supports interaction with IFT52, and corresponds to the conserved IFT46_B_C region important for IFT-B incorporation and trafficking | Localization and mutational studies mapped the basal body targeting sequence to the C-terminus and showed direct functional coupling to IFT52 (pqac-00000012, pqac-00000013, pqac-00000014, pqac-00000017) |
| IFT52-binding interface residues | L285/L286 | Critical residues within the C-terminal region for IFT52 binding; disruption impairs IFT46 recruitment/localization and the IFT52-IFT46 interaction | Point-mutation analysis identified L285/L286 as essential for the IFT52 interaction interface (pqac-00000011, pqac-00000012, pqac-00000013, pqac-00000017) |
| Full C-terminus | Broadly the C-terminal half, including the terminal interaction surface | Required for IFT-B complex stability and assembly through hydrophobic interactions with IFT52; supports formation of the IFT46-IFT52-IFT88 core module and incorporation into the IFT-B1 complex | Structural/biochemical studies show the C-terminus stabilizes IFT-B core assembly via IFT52 interaction and contributes to ternary complex formation with IFT88 (pqac-00000001, pqac-00000015, pqac-00000023, pqac-00000024) |


*Table: This table summarizes the main functional regions of IFT46/DYF-6, linking specific sequence segments to basal body targeting, IFT-B complex assembly, and cargo-adapter interactions. It is useful for distinguishing the conserved ciliogenic core functions of the protein from the motile-cilia-specific ODA transport role of its N-terminus.*