Q9EQG6: Kinase D-interacting substrate of 220 kDa (Kidins220)

Kinase D-interacting substrate of 220 kDa (Kidins220) is a 1762-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9EQG6.

Gene
Kidins220
Organism
Rattus norvegicus
Length
1762 residues
Mean pLDDT
61.3
Model
AF-Q9EQG6-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 61.3 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate17%
70 to 90Confident: backbone generally right34%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions40%

What pLDDT means and how to read it

Function

Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal…

Subunit structure

Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a nerve growth factor (NGF)-dependent manner (PubMed:17724123). Interacts with RAPGEF2; the interaction is strengthened after NGF stimulation (PubMed:17724123). Isoform 2 interacts (via C-terminal domain) with MAGI2 isoform 1 (via PDZ domain) (PubMed:17724123).…

Subcellular location

Membrane, Late endosome

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
9L9IX-ray2.0 ÅA=1-130
7D6FX-ray2.7 ÅB=1748-1762

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