ift-74 (A0A2C9C2L6, IFT74 ortholog) notes

Accession

UniProt has two unreviewed ift-74 entries, A0A2C9C2L6 (C18H9.8a, CE52310, 624 aa) and A0A2C9C2S9 (C18H9.8b, 579 aa). This review uses A0A2C9C2L6. It is the longer isoform a, it carries all the experimental GOA rows (19 rows, against 5 IEA rows on the b entry), and it is the sequence used by PMID:35969738 PMID:35969738.

Deep research status

Falcon timed out and the perplexity fallback was unavailable, so there is no deep-research file. The review was made by hand from the cached publications.

Summary with provenance

• IFT-74 interacts with IFT-81, and the two mutants have the same phenotypes [PMID:17535250 "We also demonstrated that IFT-81 interacts and co-localizes with IFT-74"; "ift-81 and ift-74 mutants similarly exhibited weak anomalies in cilia formation and obvious disruptions of transport in mature cilia"].
• IFT-74/81 is the tubulin-binding module. DYF-5 phosphorylates the IFT-74 N-terminus and lowers its affinity for tubulin PMID:35969738.
• Microtubule binding was measured with purified IFT-74/81/IFTA-2 in TIRF decoration assays PMID:35969738.
• In the orthologs, IFT74N binds the beta-tubulin tail PMID:23990561.

Curation decisions

• 19 GOA rows: 15 ACCEPT, 2 KEEP_AS_NON_CORE (chemotaxis, detection of stimulus), 1 MARK_AS_OVER_ANNOTATED (multicellular organism growth), and 1 REMOVE (protein binding IPI; the interaction is captured by the IFT-B part_of rows).
• The microtubule binding IDA was accepted because the paper contains an MT decoration assay. The core MF is beta-tubulin binding.