Q8IUC6: TIR domain-containing adapter molecule 1 (TICAM1)

TIR domain-containing adapter molecule 1 (TICAM1) is a 712-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8IUC6.

Gene
TICAM1
Organism
Homo sapiens
Length
712 residues
Mean pLDDT
62.8
Model
AF-Q8IUC6-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.8 (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 accurate23%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions47%

What pLDDT means and how to read it

Function

Involved in innate immunity against invading pathogens. Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis (PubMed:12471095, PubMed:12539043, PubMed:14739303, PubMed:28747347, PubMed:35215908, PubMed:31511519). Ligand binding to these receptors results in TRIF recruitment through its TIR domain (PubMed:12471095, PubMed:12539043, PubMed:14739303). Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively (PubMed:12471095, PubMed:12539043,…

Subunit structure

Homodimer (PubMed:12539043). Found in a multi-helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells with or without poly(I:C) RNA ligand stimulation. Interacts (via TIR domain) with DDX21 (via C-terminus). Interacts (via TIR domain) with DHX36 (via C-terminus) (By similarity). Interacts with AZI2 and IRF7 (PubMed:12471095,…

Subcellular location

Cytoplasmic vesicle, autophagosome, Cytoplasm, cytosol, Mitochondrion

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3RC4X-ray1.5 ÅB=360-372
5JELX-ray1.6 ÅB=199-219
4BSXX-ray2.23 ÅA/B/C/D=1-153
4C0MX-ray2.8 ÅA/B/C/D=1-153
9DK8EM3.3 ÅA/B/C/D/E/F=1-545
8RLMEM3.5 ÅA/B/C/D/E/F=1-712
2M1XNMRA=387-545
2M63NMRA=1-156

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