ARF3

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ADP-ribosylation factor 3
PDB rendering based on 1hur.
Available structures: 1hur, 1j2j, 1o3y, 1r8q, 1r8s, 1re0, 1rrf, 1rrg, 1s9d, 1u81, 2j59
Identifiers
Symbol(s) ARF3;
External IDs OMIM: 103190 MGI: 99432 HomoloGene: 68195
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 377 11842
Ensembl ENSG00000134287 ENSMUSG00000051853
Uniprot P61204 Q3U344
Refseq NM_001659 (mRNA)
NP_001650 (protein)		 NM_007478 (mRNA)
NP_031504 (protein)
Location Chr 12: 47.62 - 47.64 Mb Chr 15: 98.57 - 98.59 Mb
Pubmed search [1] [2]

ADP-ribosylation factor 3, also known as ARF3, is a human gene.[1]

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.[1]

[edit] References

  1. ^ a b Entrez Gene: ARF3 ADP-ribosylation factor 3.

[edit] Further reading

  • Lee FJ, Moss J, Vaughan M (1992). "Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae.". J. Biol. Chem. 267 (34): 24441-5. PMID 1447192. 
  • Lee CM, Haun RS, Tsai SC, et al. (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. 
  • Tsai SC, Haun RS, Tsuchiya M, et al. (1992). "Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin.". J. Biol. Chem. 266 (34): 23053-9. PMID 1744102. 
  • Stearns T, Willingham MC, Botstein D, Kahn RA (1990). "ADP-ribosylation factor is functionally and physically associated with the Golgi complex.". Proc. Natl. Acad. Sci. U.S.A. 87 (3): 1238-42. PMID 2105501. 
  • Bobak DA, Nightingale MS, Murtagh JJ, et al. (1989). "Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin.". Proc. Natl. Acad. Sci. U.S.A. 86 (16): 6101-5. PMID 2474826. 
  • Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol.". Nature 364 (6439): 732-4. doi:10.1038/364732a0. PMID 8355790. 
  • Haun RS, Moss J, Vaughan M (1993). "Characterization of the human ADP-ribosylation factor 3 promoter. Transcriptional regulation of a TATA-less promoter.". J. Biol. Chem. 268 (12): 8793-800. PMID 8473323. 
  • Helms JB, Palmer DJ, Rothman JE (1993). "Two distinct populations of ARF bound to Golgi membranes.". J. Cell Biol. 121 (4): 751-60. PMID 8491770. 
  • Hirai M, Kusuda J, Hashimoto K (1997). "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. 
  • Hosaka M, Toda K, Takatsu H, et al. (1997). "Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6).". J. Biochem. 120 (4): 813-9. PMID 8947846. 
  • Kanoh H, Williger BT, Exton JH (1997). "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes.". J. Biol. Chem. 272 (9): 5421-9. PMID 9038142. 
  • Williger BT, Provost JJ, Ho WT, et al. (1999). "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D.". FEBS Lett. 454 (1-2): 85-9. PMID 10413101. 
  • Boman AL, Kuai J, Zhu X, et al. (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. 
  • Takeya R, Takeshige K, Sumimoto H (2000). "Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors.". Biochem. Biophys. Res. Commun. 267 (1): 149-55. doi:10.1006/bbrc.1999.1932. PMID 10623590. 
  • Boman AL, Zhang C, Zhu X, Kahn RA (2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi.". Mol. Biol. Cell 11 (4): 1241-55. PMID 10749927. 
  • Nevrivy DJ, Peterson VJ, Avram D, et al. (2000). "Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors.". J. Biol. Chem. 275 (22): 16827-36. PMID 10828067. 
  • Zhdankina O, Strand NL, Redmond JM, Boman AL (2001). "Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi.". Yeast 18 (1): 1-18. doi:10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5. PMID 11124697. 
  • Irobi J, Nelis E, Verhoeven K, et al. (2002). "Mutation analysis of 12 candidate genes for distal hereditary motor neuropathy type II (distal HMN II) linked to 12q24.3.". J. Peripher. Nerv. Syst. 7 (2): 87-95. PMID 12090300. 
  • Li F, Mandal M, Mishra SK, et al. (2002). "Heregulin promotes expression and subcellular redistribution of ADP-ribosylation factor 3.". FEBS Lett. 524 (1-3): 49-53. PMID 12135740. 
  • Boman AL, Salo PD, Hauglund MJ, et al. (2003). "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. PMID 12221117. 
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