Q12980: GATOR1 complex protein NPRL3 (NPRL3)

GATOR1 complex protein NPRL3 (NPRL3) is a 569-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12980.

Gene
NPRL3
Organism
Homo sapiens
Length
569 residues
Mean pLDDT
66.1
Model
AF-Q12980-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 66.1 (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 accurate0%
70 to 90Confident: backbone generally right53%
50 to 70Low: treat with caution26%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:29590090, PubMed:35338845). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (PubMed:23723238, PubMed:29590090, PubMed:35338845). In the presence of abundant amino acids, the GATOR1 complex is negatively regulated by GATOR2, the other GATOR subcomplex, in this amino…

Subunit structure

Within the GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5, NPRL2 and NPRL3 (PubMed:23723238, PubMed:29590090, PubMed:35338845). GATOR1 mediates the strong interaction of the GATOR complex with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) heterodimers (PubMed:23723238). GATOR1 interacts with GPR155/LYCHOS; interaction takes place in presence of…

Subcellular location

Lysosome membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9V0JEM2.97 ÅB=1-569
8FW5EM3.08 ÅC=1-569
9O5AEM3.2 ÅC=1-569
9O5DEM3.34 ÅC=1-569
7T3BEM3.9 ÅC=1-569
6CESEM4.0 ÅM=1-569
7T3AEM4.0 ÅC=1-569
7T3CEM4.0 ÅC=1-569
6CETEM4.4 ÅM=1-569
9O5EEM5.0 ÅC/F=1-569

More AlphaFold highlights

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