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Protein ARF3 PDB 1hur.png
Aliases ARF3
External IDs MGI: 99432 HomoloGene: 68195 GeneCards: ARF3
RNA expression pattern
PBB GE ARF3 211622 s at fs.png

PBB GE ARF3 200734 s at fs.png

PBB GE ARF3 200011 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 12: 48.94 – 48.96 Mb Chr 15: 98.74 – 98.76 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.[3][4]


ADP-ribosylation factor 3 (ARF3) is a member of the human ARF gene family. These genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 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 ARF3 gene contains five exons and four introns.[4]


ARF3 has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Hirai M, Kusuda J, Hashimoto K (June 1996). "Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively". Genomics. 34 (2): 263–5. doi:10.1006/geno.1996.0283. PMID 8661066. 
  4. ^ a b "Entrez Gene: ARF3 ADP-ribosylation factor 3". 
  5. ^ a b Kanoh H, Williger BT, Exton JH (February 1997). "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes". J. Biol. Chem. 272 (9): 5421–9. doi:10.1074/jbc.272.9.5421. PMID 9038142. 
  6. ^ Williger BT, Provost JJ, Ho WT, Milstine J, Exton JH (July 1999). "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D". FEBS Lett. 454 (1-2): 85–9. doi:10.1016/s0014-5793(99)00771-1. PMID 10413101. 
  7. ^ a b Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O (September 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144Freely accessible. PMID 12221117. 
  8. ^ a b Boman AL, Zhang Cj, Zhu X, Kahn RA (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol. Biol. Cell. 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. PMC 14844Freely accessible. PMID 10749927. 
  9. ^ Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (October 1999). "Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion". Cell Motil. Cytoskeleton. 44 (2): 119–32. doi:10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C. PMID 10506747. 

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