Table 3.

The table contains data extracted from the publication (23) used for characterizing the ATI2 protein’s disordered state

Data to be annotated for the structural state	Description
Scientific publication	‘The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties’ (23)
Organism	A. thaliana
Protein	ATG8-interacting protein 2 (ATI2)
UniProt ACC	Q8VY98
Region boundaries	1–193
Experimental methods for the IDR assessment	SDS-PAGE (Sodium Dodecyl-Sulfate Polyacrylamide Gel Electrophoresis), size-exclusion chromatography, far-UV CD, NMR spectroscopy and temperature-induced protein unfolding
Aspect of the annotation and term	Disorder
Publication statement	‘We noticed that the migration rates of ATI1-N and ATI2-N in SDS-PAGE were slower than expected by their molecular weights (MwATI1-N = 20.46 kDa; MwATI2-N = 21.02 kDa) (Figure 3A). This simple observation represents a first indication that ATI1-N and ATI2-N may be intrinsically disordered, because IDRs are typically depleted in hydrophobic residues, and, consequently, tend to bind less SDS, explaining their abnormally slow mobility in SDS-PAGE (21)’. (SDS-PAGE)

The region flexibility (1–193) was verified by five different techniques, all of which has been included in DisProt as five separate pieces of evidence, associated with each experimental method and supported by a corresponding statement from the publication. One statement as an example was reported in this table.