ARF1

ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2 and ARF3), class II (ARF4 and ARF5) and class III (ARF6), and members of each class share a common gene organization. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

Full Name

ADP Ribosylation Factor 1

Function

GTP-binding protein involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. 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 plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).
(Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.

Biological Process

Actin filament organization Source: Ensembl
Antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
Ccellular copper ion homeostasis Source: UniProtKB
Cellular response to virus Source: UniProtKB
Dendritic spine organization Source: UniProtKB
Golgi to transport vesicle transport Source: Ensembl
Interleukin-12-mediated signaling pathway Source: Reactome
Intracellular protein transport Source: GO_Central
Long-term synaptic depression Source: UniProtKB
Lysosomal membrane organization Source: Ensembl
Mitotic cleavage furrow ingression Source: Ensembl
Phosphatidylinositol biosynthetic process Source: Reactome
Positive regulation of calcium ion-dependent exocytosis Source: Ensembl
Positive regulation of dendritic spine development Source: Ensembl
Positive regulation of endocytosis Source: Ensembl
Positive regulation of ER to Golgi vesicle-mediated transport Source: Ensembl
Positive regulation of late endosome to lysosome transport Source: Ensembl
Positive regulation of protein secretion Source: Ensembl
Positive regulation of sodium ion transmembrane transport Source: Ensembl
Post-Golgi vesicle-mediated transport Source: Reactome
Postsynaptic actin cytoskeleton organization Source: Ensembl
Regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKB
Regulation of defense response to virus by virus Source: Reactome
Regulation of phospholipid metabolic process Source: Ensembl
Regulation of receptor internalization Source: UniProtKB
Synaptic vesicle budding Source: Ensembl
Very-low-density lipoprotein particle assembly Source: Ensembl
Vesicle-mediated transport Source: GO_Central

Cellular Location

Golgi apparatus; Trans-Golgi network membrane; Perinuclear region; Synaptosome; Postsynaptic density; Membrane

Involvement in disease

Periventricular nodular heterotopia 8 (PVNH8): A form of periventricular nodular heterotopia, a disorder resulting from a defect in the pattern of neuronal migration in which ectopic collections of neurons lie along the lateral ventricles of the brain or just beneath, contiguously or in isolated patches. PVNH8 is an autosomal dominant disease characterized by developmental disabilities, speech delay, seizures and attention deficit hyperactivity disorder.

PTM

Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3.