Q68FD7: Folliculin-interacting protein 1 (Fnip1)

Folliculin-interacting protein 1 (Fnip1) is a 1165-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q68FD7.

Gene
Fnip1
Organism
Mus musculus
Length
1165 residues
Mean pLDDT
54.8
Model
AF-Q68FD7-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 54.8 (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 accurate14%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions56%

What pLDDT means and how to read it

Function

Binding partner of the GTPase-activating protein FLCN: involved in the cellular response to amino acid availability by regulating the non-canonical mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3 (PubMed:23582324). Required to promote FLCN recruitment to lysosomes and interaction with Rag GTPases, leading to activation of the non-canonical mTORC1 signaling (By similarity). In low-amino acid conditions, component of the lysosomal folliculin complex (LFC) on the membrane of lysosomes, which inhibits the GTPase-activating activity of FLCN, thereby inactivating mTORC1 and promoting nuclear translocation of TFEB and TFE3 (By similarity). Upon amino acid restimulation,…

Subunit structure

Homodimer and homomultimer (By similarity). Heterodimer and heteromultimer with FNIP2 (By similarity). Interacts with FLCN (via C-terminus) (By similarity). Component of the lysosomal folliculin complex (LFC), composed of FLCN, FNIP1 (or FNIP2), RagA/RRAGA or RagB/RRAGB GDP-bound, RagC/RRAGC or RagD/RRAGD GTP-bound, and Ragulator (By similarity). Interacts (via LIR motif) with GABARAP;…

Subcellular location

Lysosome membrane, Cytoplasm, cytosol

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7ROYX-ray2.9 ÅG/H=590-619
8UY3X-ray3.2 ÅE/F/H/I=590-619

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