Q9NXC5: GATOR2 complex protein MIOS (MIOS)

GATOR2 complex protein MIOS (MIOS) is a 875-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NXC5.

Gene
MIOS
Organism
Homo sapiens
Length
875 residues
Mean pLDDT
82.8
Model
AF-Q9NXC5-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.8 (confident 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 accurate53%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

As a component of the GATOR2 complex, functions as an activator of the amino acid-sensing branch of the mTORC1 signaling pathway (PubMed:23723238, PubMed:26586190, PubMed:27487210, PubMed:35831510, PubMed:36528027). The GATOR2 complex indirectly activates mTORC1 through the inhibition of the GATOR1 subcomplex (PubMed:23723238, PubMed:26586190, PubMed:27487210, PubMed:35831510, PubMed:36528027). GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1 (PubMed:36528027). In the presence of abundant amino acids, the GATOR2 complex mediates ubiquitination of the NPRL2 core component of the GATOR1 complex, leading to GATOR1 inactivation (PubMed:36528027). In the absence of amino…

Subunit structure

Component of the GATOR2 subcomplex, composed of MIOS, SEC13, SEH1L, WDR24 and WDR59 (PubMed:23723238, PubMed:35831510, PubMed:36528027). The GATOR2 complex interacts with CASTOR1 and CASTOR2; the interaction is negatively regulated by arginine (PubMed:26972053). CASTOR1 and CASTOR2 convey leucine availability via direct interaction with MIOS (PubMed:35831510). The GATOR2 complex interacts with…

Subcellular location

Lysosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9LWFEM3.41 ÅA/B/K/L=1-875
9OTIEM3.5 ÅA/B/L/T=1-875
9LVKEM3.59 ÅA/B/K/L=1-875
7UHYEM3.66 ÅA/B=1-875
9LVJEM3.82 ÅA/B/K/L=1-875

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