Summary: Mon1 contributes to the Rab7 guanine nucleotide exchange factor activity of the Mon1-Ccz1(-Bulli) complex.

Reason: Rab7 GEF activity resides in the Mon1-Ccz1 heterodimer (with Bulli in metazoa); the contributes_to qualifier correctly reflects that the activity belongs to the complex. Conserved from yeast Mon1-Ccz1, so the IBA/ISS rows are sound.

Summary: Mon1 contributes to the Rab7 guanine nucleotide exchange factor activity of the Mon1-Ccz1(-Bulli) complex.

Reason: Rab7 GEF activity resides in the Mon1-Ccz1 heterodimer (with Bulli in metazoa); the contributes_to qualifier correctly reflects that the activity belongs to the complex. Conserved from yeast Mon1-Ccz1, so the IBA/ISS rows are sound.

Summary: Mon1 contributes to the Rab7 guanine nucleotide exchange factor activity of the Mon1-Ccz1(-Bulli) complex.

Reason: Rab7 GEF activity resides in the Mon1-Ccz1 heterodimer (with Bulli in metazoa); the contributes_to qualifier correctly reflects that the activity belongs to the complex. Conserved from yeast Mon1-Ccz1, so the IBA/ISS rows are sound.

Summary: Mon1 binds Rab5.

Reason: The interaction with Rab5 (Q9V3I2) is functionally meaningful: a conserved Rab5-binding site in Mon1 is required for membrane GEF activity and growth in vivo. Generic protein binding should be replaced by small GTPase binding.

Proposed replacements: small GTPase binding

Summary: Mon1 is found in the cytosol.

Reason: The Mon1-Ccz1 complex cycles between the cytosol and Rab5-positive endosomal membranes; correct, though the functional location is the endosome membrane.

Summary: Mon1 is found in the cytosol.

Reason: The Mon1-Ccz1 complex cycles between the cytosol and Rab5-positive endosomal membranes; correct, though the functional location is the endosome membrane.

Summary: Protein targeting to vacuole (InterPro mapping from the Mon1 family).

Reason: Yeast Mon1 is needed for vacuolar protein delivery via Rab7 (Ypt7) activation; the fly equivalent is delivery to lysosomes, which is better captured by the endosome-to-lysosome transport annotations. Retained as non-core.

Summary: General vesicle-mediated transport.

Reason: Correct but general; MODIFY to endosome to lysosome transport via multivesicular body sorting pathway, which Mon1 already carries (IBA, IMP).

Proposed replacements: endosome to lysosome transport via multivesicular body sorting pathway

Summary: Mon1 is required for endosome-to-lysosome transport.

Reason: Dmon1 loss causes enlarged maturing endosomes that fail to recruit Rab7 and accumulate transmembrane cargo; Mon1 directly performs the Rab7 activation step. The IBA reflects the conserved function.

Summary: Mon1 is required for endosome-to-lysosome transport.

Reason: Dmon1 loss causes enlarged maturing endosomes that fail to recruit Rab7 and accumulate transmembrane cargo; Mon1 directly performs the Rab7 activation step. The IBA reflects the conserved function.

Summary: Late endosome to vacuole transport via MVB sorting.

Reason: Consistent with the Rab7 GEF role of the complex.

Summary: Mon1 is a subunit of the Mon1-Ccz1 complex.

Reason: Direct biochemical co-purification and the cryo-EM structure of the Drosophila Mon1-Ccz1-RMC1(Bulli) trimer establish complex membership.

Summary: Mon1 is a subunit of the Mon1-Ccz1 complex.

Reason: Direct biochemical co-purification and the cryo-EM structure of the Drosophila Mon1-Ccz1-RMC1(Bulli) trimer establish complex membership.

Summary: Mon1 is a subunit of the Mon1-Ccz1 complex.

Reason: Direct biochemical co-purification and the cryo-EM structure of the Drosophila Mon1-Ccz1-RMC1(Bulli) trimer establish complex membership.

Summary: Mon1 is a subunit of the Mon1-Ccz1 complex.

Reason: Direct biochemical co-purification and the cryo-EM structure of the Drosophila Mon1-Ccz1-RMC1(Bulli) trimer establish complex membership.

Summary: Mon1 is a subunit of the Mon1-Ccz1 complex.

Reason: Direct biochemical co-purification and the cryo-EM structure of the Drosophila Mon1-Ccz1-RMC1(Bulli) trimer establish complex membership.

Summary: Mon1 reported in the synaptic cleft at the larval NMJ.

Reason: The abstract proposes a presynaptically regulated transsynaptic mechanism but does not describe Mon1 localisation in the cleft; extracellular localisation of a cytosolic GEF subunit is unexpected and the full text is not available to verify the IDA.

Summary: The Mon1 N-terminal domain autoinhibits the GEF activity of Mon1-Ccz1.

Reason: The experiments show intramolecular/intra-complex autoinhibition by the disordered Mon1 N-terminus of the complex Mon1 itself belongs to. This is a regulatory feature of the GEF rather than an activity of Mon1 acting on another GEF, so annotating Mon1 with GEF inhibitor activity overstates it.

Summary: Mon1, with Ccz1, is required to recruit Rab7 to autophagosomes for their fusion with lysosomes.

Reason: In starved larval fat cells, Mon1 mutant cells fail to recruit Rab7 to Atg8a-positive autophagosomes, accumulate autophagosomes and lack autolysosomes (Hegedus et al. 2016). As the Rab7 GEF subunit, Mon1 performs the Rab7 recruitment/activation step on the autophagosome, so it does part of the work of autophagy rather than merely being necessary for it. Comparators agree - its partner Ccz1 already carries autophagy in fly (ISS from yeast Ccz1), and yeast Mon1 (P53129) carries autophagy by IMP - so this fills a gap in the fly Mon1 record rather than departing from a curation convention. Autophagosome maturation (GO:0097352) is not used because it is defined as the PI3P/Atg8 removal step before fusion; the more specific autophagosome-lysosome fusion term is raised as a suggested question instead.