Protein: DP01461 (UniProt Q13188)
Region: residues 365	to 367
Annotation: selective autophagy (Biological process)
Evidence: protein binding evidence used in manual assertion
Supporting statements:
STK3 interacts with LC3C and GABARAP via a CLIR
GST pulldown assays using the various deletion constructs of STK3 identified the interaction to be mediated by the fragment encompassing the C-terminal region from amino acid position 323, and not the N-terminal part (from position 1 to 357) (Fig. 1F).
GABARAP was used as an interaction partner in these LIR-mapping experiments because it bound strongly to STK3.
Figure 1. STK3 interacts with LC3C and GABARAP via a C-type atypical LIR motif. , HEK293 cells were transiently co-transfected with the indicated FLAG-tagged kinases, wildtype (WT), or kinase-dead (KD), and either GFP–LC3B or GFP-GABARAP. Cell lysates were immunoprecipitated (IP) with FLAG antibodies and analyzed by Western blotting. B, Myc-tagged STK3 kinase constructs were translated in vitro in the presence of [35S]methionine and analyzed in GST affinity isolation experiments for binding to the indicated ATG8s fused to GST. Bound proteins were detected by autoradiography and immobilized GST or GST-tagged proteins visualized by Coomassie Brilliant Blue staining. C, quantification of STK3 binding shown in B and based on three independent experiments. Values are mean ± S.E. D, Myc-tagged STK4 kinase construct was translated in vitro in the presence of [35S]methionine and analyzed in GST affinity isolation experiments for binding to the indicated ATG8s fused to GST. E, schematic drawing of the domain organization of STK3 with the kinase domain, the LIR motif, and the SARAH domain indicated. The extent of deletion mutants and the location of the MVI/AAA LIR mutation are shown below the domain cartoon. G, and H, GST pulldown analyses of binding of Myc-tagged STK3 WT and LIR mutant translated in vitro in the presence of [35S]methionine to GST-LC3C (G) or Myc-tagged STK3 WT translated in vitro in the presence of [35S]methionine to GST-LC3C or GST-LC3C F58A (H). The F58A mutant inhibits binding to the LDS of LC3C. I, HEK293 cells were transiently transfected with FLAG-tagged constructs of STK3 WT and LIR mutant (MVI/AAA), and whole-cell lysates were incubated with recombinant GST or GST–ATG8s family proteins. The bound FLAG-tagged STK3 protein was detected by Western blotting using anti-FLAG antibodies and immobilized GST or GST-tagged proteins visualized by Ponceau S staining. AR, autoradiography; CBB, Coomassie Brilliant Blue.
However, because STK3 also bound strongly to LC3C, we searched the C-terminal part of STK3 for CLIR with the consensus ΦΦΦ, where Φ is an aliphatic amino acid. 
A candidate CLIR, “MVI” was located at positions 365–367, reminiscent of the CLIR previously described for the interaction between CALCOCO2/NDP52 and LC3C (36).
Strikingly, mutation of this CLIR motif to AAA abolished binding between STK3 and LC3C (Fig. 1G). 
Consistently, mutation of the LDS in LC3C F58A resulted in a strongly-decreased binding to STK3 (Fig. 1H).
GST-pulldown assays using extracts from HeLa cells expressing the FLAG–STK3 or the FLAG–STK3 MVI/AAA CLIR mutant verified the strong binding of FLAG–STK3 to GABARAP and LC3C, whereas the CLIR mutant FLAG–STK3 MVI/AAA did not show significant binding.
Furthermore, the GABARAP Y49A LDS mutant displayed strongly-reduced binding to FLAG–STK3 (Fig. 1I).
Taken together, the results show that the CLIR motif in STK3 mediated LDS-dependent binding to both LC3C and GABARAP.
The annotation include the non canonical CLIR motif MVI at position 365 – 367.