Unconventional myosin-Ic (Myo1c) is a 1063-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9WTI7.
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The mean pLDDT of this model is 84.1 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 33% |
| 70 to 90 | Confident: backbone generally right | 59% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes
Interacts (via its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-dependent (PubMed:17994197). Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and CALM (PubMed:15976448). Interacts with POLR1A (PubMed:16514417). Interacts with POLR2A (PubMed:11030652, PubMed:16960872). Component of the…
Cytoplasm, Nucleus, Cytoplasm, cell cortex, Cell projection, stereocilium membrane, Cytoplasmic vesicle, Cell projection, ruffle membrane, Nucleus, nucleolus, Nucleus, nucleoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9CFV | EM | 2.7 Å | P=36-755 |
| 9CFX | EM | 2.7 Å | P=36-755 |
| 9CFU | EM | 2.8 Å | P=36-755 |
| 9CFW | EM | 3.0 Å | P=36-755 |
| 4R8G | X-ray | 3.5 Å | E=733-1063 |
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