O88653: Ragulator complex protein LAMTOR3 (Lamtor3)

Ragulator complex protein LAMTOR3 (Lamtor3) is a 124-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O88653.

Gene
Lamtor3
Organism
Mus musculus
Length
124 residues
Mean pLDDT
95.9
Model
AF-O88653-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 95.9 (very high 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 accurate92%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:15263099). Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane (By similarity). Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in…

Subunit structure

Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and RagD/RRAGD; regulated by amino acid availability.…

Subcellular location

Late endosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1VETX-ray1.9 ÅA=1-124
1VEUX-ray2.15 ÅA=1-124

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