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MGP000192

UniProt Annotations

Entry Information
Gene NameADP-ribosylation factor 1
Protein EntryARF1_HUMAN
UniProt IDP84077
SpeciesHuman
Comments
Comment typeDescription
FunctionGTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. 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).
InteractionQ99418:CYTH2; NbExp=4; IntAct=EBI-447171, EBI-448974; O60271:SPAG9; NbExp=3; IntAct=EBI-447171, EBI-1023301;
PtmDemyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3. {ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:23535599}.
SimilarityBelongs to the small GTPase superfamily. Arf family. {ECO:0000305}.
Subcellular LocationGolgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
SubunitInteracts with ARHGAP21, ASAP2, GGA1, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2. Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its function. Interacts with PI4KB in the Golgi complex. Interacts with NCS1/FREQ in the Golgi and at the plasma membrane. Interacts with PLEKHA3. Interacts with PLEKHA8; the interaction, together with phosphatidylinositol 4-phosphate binding, is required for FAPP2- mediated glucosylceramide transfer activity. Interacts (activated) with PICK1 (via PDZ domain); the interaction blocks Arp2/3 complex inhibition. {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10102276, ECO:0000269|PubMed:15107860, ECO:0000269|PubMed:17347647, ECO:0000269|PubMed:17555535, ECO:0000269|PubMed:21454700, ECO:0000269|PubMed:23889934, ECO:0000269|PubMed:8861955}.
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