ARFGEF1

ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene is involved in the activation of ARFs by accelerating replacement of bound GDP with GTP. It contains a Sec7 domain, which may be responsible for the guanine-nucleotide exchange activity and also the brefeldin A inhibition. [provided by RefSeq]

ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited)

Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined.

Endomembrane system organization Source: UniProtKB
Exocytosis Source: ProtInc
Golgi organization Source: UniProtKB
Negative regulation of actin filament polymerization Source: UniProtKB
Negative regulation of GTPase activity Source: UniProtKB
Neuron projection development Source: Ensembl
Positive regulation of GTPase activity Source: GOC
Positive regulation of protein glycosylation in Golgi Source: UniProtKB
Positive regulation of protein kinase B signaling Source: Ensembl
Positive regulation of wound healing Source: UniProtKB
Protein transport Source: UniProtKB-KW
Regulation of ARF protein signal transduction Source: InterPro
Regulation of establishment of cell polarity Source: UniProtKB

Cytoplasm; Golgi apparatus; Trans-Golgi network membrane; Nucleus; Nucleolus; Nucleus matrix; Perinuclear region. Translocates from cytoplasm to membranes and nucleus upon cAMP treatment.

Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1.