ARF3

ADP-ribosylation factor 3

PDB rendering based on 1hur.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1hur, 1j2j, 1o3y, 1r8q, 1r8s, 1re0, 1rrf, 1rrg, 1s9d, 1u81, 2j59

Identifiers

Symbol

ARF3

External IDs

OMIM: 103190 MGI: 99432 HomoloGene: 68195 GeneCards: ARF3 Gene

Gene ontology
Molecular function	• GTPase activity • GTP binding
Cellular component	• Golgi membrane • perinuclear region of cytoplasm • extracellular vesicular exosome
Biological process	• GTP catabolic process • phospholipid metabolic process • phosphatidylinositol biosynthetic process • small GTPase mediated signal transduction • protein transport • vesicle-mediated transport • small molecule metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
49.33 – 49.35 Mb

Chr 15:
98.74 – 98.76 Mb

PubMed search

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.^[1]^[2]

Function

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.^[2]

Interactions

ARF3 has been shown to interact with:

References

↑ Hirai M, Kusuda J, Hashimoto K (February 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. Check date values in: |year= / |date= mismatch (help)
↑ 2.0 2.1 "Entrez Gene: ARF3 ADP-ribosylation factor 3".
↑ 3.0 3.1 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. CS1 maint: Date and year (link)
↑ 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. CS1 maint: Date and year (link)
↑ 5.0 5.1 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 124144. PMID 12221117. CS1 maint: Date and year (link)
↑ 6.0 6.1 Boman AL, Zhang C, 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 14844. PMID 10749927. CS1 maint: Date and year (link)
↑ 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. CS1 maint: Date and year (link)

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, Moss J, Vaughan M (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, Moss J, Vaughan M (1991). "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. doi:10.1073/pnas.87.3.1238. PMC 53446. PMID 2105501.
Bobak DA, Nightingale MS, Murtagh JJ, Price SR, Moss J, Vaughan M (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. doi:10.1073/pnas.86.16.6101. PMC 297783. 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. doi:10.1083/jcb.121.4.751. PMC 2119793. PMID 8491770.
Hosaka M, Toda K, Takatsu H, Torii S, Murakami K, Nakayama K (1996). "Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6)". J. Biochem. 120 (4): 813–9. doi:10.1093/oxfordjournals.jbchem.a021484. 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. doi:10.1074/jbc.272.9.5421. PMID 9038142.
Williger BT, Provost JJ, Ho WT, Milstine J, Exton JH (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.
Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (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. doi:10.1091/mbc.11.4.1241. PMC 14844. PMID 10749927.
Nevrivy DJ, Peterson VJ, Avram D, Ishmael JE, Hansen SG, Dowell P 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. doi:10.1074/jbc.275.22.16827. 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, De Vriendt E, Dierick I, De Jonghe P 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. doi:10.1046/j.1529-8027.2002.02014.x. PMID 12090300.
Li F, Mandal M, Mishra SK, Barnes CJ, Kumar R (2002). "Heregulin promotes expression and subcellular redistribution of ADP-ribosylation factor 3". FEBS Lett. 524 (1-3): 49–53. doi:10.1016/S0014-5793(02)02994-0. PMID 12135740.
Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O (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 124144. PMID 12221117.

PDB gallery

1hur: HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED

1j2j: Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form

1o3y: Crystal structure of mouse ARF1 (delta17-Q71L), GTP form

1r8q: FULL-LENGTH ARF1-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN

1r8s: ARF1[DELTA1-17]-GDP IN COMPLEX WITH A SEC7 DOMAIN CARRYING THE MUTATION OF THE CATALYTIC GLUTAMATE TO LYSINE

1re0: Structure of ARF1-GDP bound to Sec7 domain complexed with Brefeldin A

1rrf: NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM

1rrg: NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM

1s9d: ARF1[DELTA 1-17]-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN

1u81: Delta-17 Human ADP Ribosylation Factor 1 Complexed with GDP

2j59: CRYSTAL STRUCTURE OF THE ARF1:ARHGAP21-ARFBD COMPLEX

ARF3

Function

Interactions

References

Further reading