F-actin-uncapping protein LRRC16A (CARMIL1) is a 1371-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5VZK9.
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The mean pLDDT of this model is 67.4 (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 | 36% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 37% |
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:19846667)
Homodimer (PubMed:19846667). Interacts (via C-terminus) with heterodimer capping protein (CP); this interaction uncaps barbed ends capped by CP, enhances barbed-end actin polymerization and promotes lamellipodial formation and cell migration (By similarity). Interacts with heterodimer capping protein (CP) (PubMed:19846667). Interacts with MYO1E (PubMed:19846667). Interacts with TRIO…
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 |
|---|---|---|---|
| 3LK2 | X-ray | 2.2 Å | T=961-1012 |
| 3LK3 | X-ray | 2.68 Å | T=964-1078 |
| 9EC0 | EM | 3.4 Å | A/B=1-1046 |
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