Q8WTW4: GATOR1 complex protein NPRL2 (NPRL2)

GATOR1 complex protein NPRL2 (NPRL2) is a 380-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8WTW4.

Gene
NPRL2
Organism
Homo sapiens
Length
380 residues
Mean pLDDT
69.4
Model
AF-Q8WTW4-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.4 (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 right51%
50 to 70Low: treat with caution47%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Catalytic component of the GATOR1 complex, a multiprotein complex that functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:29590090, PubMed:35338845, PubMed:38006878). 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 ubiquitinated and…

Subunit structure

Within the GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5, NPRL2 and NPRL3 (PubMed:19521502, 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, PubMed:29590090). GATOR1 interacts with GPR155/LYCHOS;…

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 ÅA=1-380
8FW5EM3.08 ÅB=1-380
9O5AEM3.2 ÅH=1-380
9O5DEM3.34 ÅD=1-380
7T3BEM3.9 ÅB=1-380
6CESEM4.0 ÅN=1-380
7T3AEM4.0 ÅB=1-380
7T3CEM4.0 ÅB=1-380
6CETEM4.4 ÅN=1-380
9O5EEM5.0 ÅD/G=1-380

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