Q9D0J4: ADP-ribosylation factor-like protein 2 (Arl2)

ADP-ribosylation factor-like protein 2 (Arl2) is a 184-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9D0J4.

Gene
Arl2
Organism
Mus musculus
Length
184 residues
Mean pLDDT
94.6
Model
AF-Q9D0J4-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.6 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate88%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

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). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear…

Subunit structure

Found in a complex with ARL2, ARL2BP and SLC25A6. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with ELMOD2. The GTP-bound form interacts with ARL2BP. Interacts with TBCD; the GDP-bound form interacts preferentially with TBCD. Interacts with UNC119 (By similarity). Found in a complex with ARL2, ARL2BP and SLC25A4. The GTP-bound form interacts with…

Subcellular location

Mitochondrion intermembrane space, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Nucleus, Cytoplasm

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
1KSHX-ray1.8 ÅA=1-184
1KSGX-ray2.3 ÅA=1-184
1KSJX-ray2.6 ÅA=1-184
4GOKX-ray2.6 ÅA/B=17-184

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