Rearuh

ARF1
Available structures
PDB	Ortholog search: PDBe RCSB ;
List of PDB id codes
	1HUR, 1RE0, 1U81, 3O47, 4HMY, 1R8Q, 1RRG, 1RRF
Identifiers
Aliases	; ARF1, ADP ribosylation factor 1
External IDs	MGI: 99431 HomoloGene: 133930 GeneCards: ARF1
Gene location (Human)
Chr.	Chromosome 1 (human)
	; ; ;
End	228,099,212 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
	; ; ;
End	59,228,270 bp
; RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• phospholipase D activator activity; • nucleotide binding; • GTP binding; • magnesium ion binding; • signal transducer activity, downstream of receptor; • GTPase activity; • GDP binding; • protein binding; • RNA binding; • protein domain specific binding; • protein heterodimerization activity;
Cellular component	• extracellular exosome; • late endosome; • cytoplasm; • synapse; • trans-Golgi network; • Golgi apparatus; • cell junction; • endomembrane system; • peroxisomal membrane; • cell leading edge; • neuron projection; • postsynaptic density; • postsynaptic membrane; • membrane; • focal adhesion; • intracellular; • perinuclear region of cytoplasm; • sarcomere; • COPI-coated vesicle; • cytosol; • Golgi membrane; • plasma membrane; • protein complex;
Biological process	• positive regulation of endocytosis; • positive regulation of protein secretion; • very-low-density lipoprotein particle assembly; • regulation of defense response to virus by virus; • positive regulation of calcium ion-dependent exocytosis; • regulation of receptor internalization; • synaptic vesicle budding; • small GTPase mediated signal transduction; • cellular copper ion homeostasis; • long term synaptic depression; • antigen processing and presentation of exogenous peptide antigen via MHC class II; • Golgi to transport vesicle transport; • post-Golgi vesicle-mediated transport; • actin filament organization; • lysosomal membrane organization; • positive regulation of ER to Golgi vesicle-mediated transport; • dendritic spine organization; • regulation of phospholipid metabolic process; • regulation of Arp2/3 complex-mediated actin nucleation; • positive regulation of late endosome to lysosome transport; • protein transport; • phosphatidylinositol biosynthetic process; • positive regulation of sodium ion transmembrane transport; • vesicle-mediated transport; • positive regulation of catalytic activity; • positive regulation of dendritic spine development; • mitotic cleavage furrow ingression; • interleukin-12-mediated signaling pathway; • transport;
	Sources:Amigo / QuickGO;
Orthologs
	375
	11840
	ENSG00000143761
	ENSMUSG00000048076
	P84077
	P84078
	NM_001658; NM_001024226; NM_001024227; NM_001024228
	NM_001130408; NM_007476
	NP_001019397; NP_001019398; NP_001019399; NP_001649
	NP_001123880; NP_031502
	Wikidata
View/Edit Human	View/Edit Mouse

ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene.^[5]

Function

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.^[6]

The major mechanism of action of Brefeldin A is through inhibition of ARF1.

Interactions

ARF1 has been shown to interact with:

CHRM3,^[7]

COPB1,^[8]^[9]

GGA3,^[10]^[11] and

PLD2.^[12]^[13]

References

^ ^a^b^c GRCh38: Ensembl release 89: ENSG00000143761 - Ensembl, May 2017

^ ^a^b^c GRCm38: Ensembl release 89: ENSMUSG00000048076 - Ensembl, May 2017

^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}

^ "Mouse PubMed Reference:".

^ Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M (June 1992). "Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin". J Biol Chem. 267 (13): 9028–34. PMID 1577740.

^ "Entrez Gene: ARF1 ADP-ribosylation factor 1".

^ Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September 2003). "ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor". J. Biol. Chem. 278 (36): 33818–30. doi:10.1074/jbc.M305825200. PMID 12799371.

^ Fischer KD, Helms JB, Zhao L, Wieland FT (April 2000). "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods. 20 (4): 455–64. doi:10.1006/meth.2000.0958. PMID 10720466.

^ Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP". EMBO J. 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. PMC 306616. PMID 10921873.

^ Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (April 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". J. Cell Biol. 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.

^ Puertollano R, Randazzo PA, Presley JF, Hartnell LM, Bonifacino JS (April 2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell. 105 (1): 93–102. doi:10.1016/s0092-8674(01)00299-9. PMID 11301005.

^ Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH (July 2001). "Actin directly interacts with phospholipase D, inhibiting its activity". J. Biol. Chem. 276 (30): 28252–60. doi:10.1074/jbc.M008521200. PMID 11373276.

^ Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH (July 2000). "Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner". J. Biol. Chem. 275 (28): 21295–301. doi:10.1074/jbc.M002463200. PMID 10801846.