P84078: ADP-ribosylation factor 1 (Arf1)

ADP-ribosylation factor 1 (Arf1) is a 181-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P84078.

Gene
Arf1
Organism
Mus musculus
Length
181 residues
Mean pLDDT
85.9
Model
AF-P84078-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.9 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate59%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Small GTPase involved in protein trafficking between different compartments (PubMed:11950392). Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasticity of excitatory synapses and spine shrinkage…

Subunit structure

Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392, PubMed:12679809). Interacts with ARHGAP21, ASAP2, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2 (PubMed:17347647). Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its function. Interacts with PI4KB in the Golgi…

Subcellular location

Golgi apparatus membrane, Synapse, synaptosome, Postsynaptic density

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1O3YX-ray1.5 ÅA/B=18-181
2J59X-ray2.1 ÅA/B/C/D/E/F=18-181

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