ARF1

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ADP-ribosylation factor 1
Protein ARF1 PDB 1hur.png
PDB rendering based on 1hur.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbol ARF1
External IDs OMIM103180 MGI99431 HomoloGene56086 ChEMBL: 5985 GeneCards: ARF1 Gene
RNA expression pattern
PBB GE ARF1 208750 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 375 11841
Ensembl ENSG00000143761 ENSMUSG00000062421
UniProt P84077 Q8BSL7
RefSeq (mRNA) NM_001024226 NM_007477
RefSeq (protein) NP_001019397 NP_031503
Location (UCSC) Chr 1:
228.27 – 228.29 Mb
Chr 11:
103.97 – 103.99 Mb
PubMed search [1] [2]

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

Function[edit]

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.[2]

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

Interactions[edit]

ARF1 has been shown to interact with:

References[edit]

  1. ^ 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. 
  2. ^ "Entrez Gene: ARF1 ADP-ribosylation factor 1". 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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. 


Further reading[edit]