P46662: Merlin (Nf2)

Merlin (Nf2) is a 596-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P46662.

Gene
Nf2
Organism
Mus musculus
Length
596 residues
Mean pLDDT
87.6
Model
AF-P46662-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.6 (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 accurate66%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex (By similarity). Plays a role in lens development and is required for…

Subunit structure

Interacts with NHERF1, HGS and AGAP2. Interacts with SGSM3. Interacts (via FERM domain) with MPP1 (By similarity). Interacts with LAYN (PubMed:15913605). Interacts with WWC1. Interacts with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1. Interacts (via FERM domain) with NOP53; the interaction is direct…

Subcellular location

Cell membrane, Cell projection, Cytoplasm, cytoskeleton, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3WA0X-ray2.31 ÅA/B/C/D/E/F=19-314
4ZRKX-ray2.32 ÅA/B/C/D=1-320
4P7IX-ray2.6 ÅA/B=1-313
1ISNX-ray2.9 ÅA=18-340

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