Transient receptor potential cation channel subfamily V member 3 (TRPV3) is a 790-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NET8.
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The mean pLDDT of this model is 76.5 (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 | 38% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 18% |
What pLDDT means and how to read it
Non-selective calcium permeant cation channel (PubMed:12077604, PubMed:12077606, PubMed:26818531, PubMed:37648856, PubMed:38691614). It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius (PubMed:12077604, PubMed:12077606). Activation exhibits an outward rectification (PubMed:12077604). The channel pore can dilate to provide permeability to larger cations (PubMed:37648856). May associate with TRPV1 and may modulate its activity (PubMed:12077606). Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and…
Homotetramer (PubMed:37648856, PubMed:38691614). May convert from a homotetramer to a homopentamer to allow pore dilation (PubMed:37648856). Interacts with TRPV1; may form a heteromeric channel with TRPV1 (PubMed:12077606). Interacts with SNX11; this interaction promotes TRPV3 trafficking from the cell membrane to lysosome for degradation (PubMed:26818531)
Cell membrane, Cytoplasm, Lysosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6H9J | X-ray | 1.83 Å | D=229-250 |
| 6HA6 | X-ray | 1.98 Å | D=220-246 |
| 7QQN | X-ray | 2.45 Å | B/D=781-790 |
| 8V6K | EM | 2.46 Å | A/B/C/D=1-790 |
| 7XJ0 | EM | 2.53 Å | A/B/C/D=1-790 |
| 8GKA | EM | 2.55 Å | A/B/C/D=1-790 |
| 8V6N | EM | 2.59 Å | A/B/C/D=1-790 |
| 8V6O | EM | 2.83 Å | A/B/C/D=1-790 |
| 7XJ1 | EM | 2.93 Å | A/B/C/D=1-790 |
| 6UW4 | EM | 3.1 Å | A/B/C/D=1-790 |
| 9JDM | EM | 3.13 Å | A/B/C/D=1-790 |
| 6MHS | EM | 3.2 Å | A/B/C/D=2-790 |
| 9UED | EM | 3.29 Å | A/B/C/D=1-790 |
| 9BKU | EM | 3.39 Å | A/B/C/D=1-790 |
| 9JEG | EM | 3.39 Å | A/B/C/D=1-790 |
| 6MHO | EM | 3.4 Å | A/B/C/D=2-790 |
| 6MHV | EM | 3.5 Å | A/B/C/D=2-790 |
| 9JEE | EM | 3.51 Å | A/B/C/D=1-790 |
| 9JE5 | EM | 3.53 Å | A/B/C/D=1-790 |
| 7XJ3 | EM | 3.54 Å | A/B/C/D=1-790 |
Showing 20 of 34 experimental structures (best resolution first).
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