ADP-ribosylation factor-like protein 3 (Arl3) is a 182-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9WUL7.
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The mean pLDDT of this model is 92.7 (very high 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 | 82% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP) (PubMed:18376416). Required for normal cytokinesis and cilia signaling. Required for targeting proteins to the cilium, including myristoylated NPHP3 and prenylated INPP5E. Targets NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium (By similarity). Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms (PubMed:15979089).…
Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119 (or UNC119B). Interacts with RP2; interaction is direct and stimulated with the activated GTP-bound form of ARL3. Interacts with SYS1. Interacts with ARL2BP; the GTP-bound form interacts with ARL2BP. Microtubule-associated protein. Does not interact with…
Golgi apparatus membrane, Cytoplasm, cytoskeleton, spindle, Nucleus, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, Cell projection, cilium
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1FZQ | X-ray | 1.7 Å | A=2-182 |
| 3BH7 | X-ray | 1.9 Å | A=17-177 |
| 4ZI3 | X-ray | 2.0 Å | A/B=1-182 |
| 4GOJ | X-ray | 2.1 Å | A/B=1-182 |
| 4ZI2 | X-ray | 2.2 Å | A/B=1-182 |
| 3BH6 | X-ray | 2.6 Å | A=17-177 |
| 7OK7 | X-ray | 3.15 Å | A/B/C/D/E/F=3-182 |
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