F-actin-uncapping protein LRRC16A (Carmil1) is a 1374-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6EDY6.
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The mean pLDDT of this model is 66.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 33% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 38% |
What pLDDT means and how to read it
Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028)
Homodimer (By similarity). Interacts (via C-terminus) with heterodimeric capping protein (CP); this interaction uncaps barbed ends capped by CP, enhances barbed-end actin polymerization and promotes lamellipodial formation and cell migration (PubMed:16054028). Interacts with MYO1E (By similarity). Interacts with TRIO (By similarity)
Cytoplasm, Cytoplasm, cytoskeleton, Cell membrane, Cell projection, lamellipodium
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3AA0 | X-ray | 1.7 Å | C=985-1005 |
| 4K17 | X-ray | 2.9 Å | A/B/C/D=1-668 |
| 3AAE | X-ray | 3.3 Å | V/W/X/Y/Z=971-1002 |
| 2KZ7 | NMR | C=965-1039 |
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