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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''ADP-ribosylation factor 3''' is a [[protein]] that in humans is encoded by the ''ARF3'' [[gene]].<ref name="pmid8661066">{{cite journal | vauthors = Hirai M, Kusuda J, Hashimoto K | title = Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively | journal = Genomics | volume = 34 | issue = 2 | pages = 263–5 | date = June 1996 | pmid = 8661066 | pmc = | doi = 10.1006/geno.1996.0283 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARF3 ADP-ribosylation factor 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=377| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_ARF3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hur.
| PDB = {{PDB2|1hur}}, {{PDB2|1j2j}}, {{PDB2|1o3y}}, {{PDB2|1r8q}}, {{PDB2|1r8s}}, {{PDB2|1re0}}, {{PDB2|1rrf}}, {{PDB2|1rrg}}, {{PDB2|1s9d}}, {{PDB2|1u81}}, {{PDB2|2j59}}
| Name = ADP-ribosylation factor 3
| HGNCid = 654
| Symbol = ARF3
| AltSymbols =;
| OMIM = 103190
| ECnumber = 
| Homologene = 68195
| MGIid = 99432
| GeneAtlas_image1 = PBB_GE_ARF3_200734_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARF3_211622_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ARF3_200011_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006888 |text = ER to Golgi vesicle-mediated transport}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 377
    | Hs_Ensembl = ENSG00000134287
    | Hs_RefseqProtein = NP_001650
    | Hs_RefseqmRNA = NM_001659
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 47616259
    | Hs_GenLoc_end = 47637577
    | Hs_Uniprot = P61204
    | Mm_EntrezGene = 11842
    | Mm_Ensembl = ENSMUSG00000051853
    | Mm_RefseqmRNA = NM_007478
    | Mm_RefseqProtein = NP_031504
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 98565660
    | Mm_GenLoc_end = 98591197
    | Mm_Uniprot = Q3U344
  }}
}}
'''ADP-ribosylation factor 3''', also known as '''ARF3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARF3 ADP-ribosylation factor 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=377| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ARF3 ADP-ribosylation factor 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=377| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ARF3 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[ARFIP1]],<ref name = pmid9038142/><ref name = pmid10413101>{{cite journal | vauthors = Williger BT, Provost JJ, Ho WT, Milstine J, Exton JH | title = Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D | journal = FEBS Lett. | volume = 454 | issue = 1-2 | pages = 85–9  | date = July 1999 | pmid = 10413101 | doi =  10.1016/s0014-5793(99)00771-1}}</ref>
* [[ARFIP2]],<ref name = pmid9038142>{{cite journal | vauthors = Kanoh H, Williger BT, Exton JH | title = Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes | journal = J. Biol. Chem. | volume = 272 | issue = 9 | pages = 5421–9  | date = February 1997 | pmid = 9038142 | doi =  10.1074/jbc.272.9.5421}}</ref>
* [[GGA1]],<ref name = pmid12221117/><ref name = pmid10749927/>
* [[GGA3]],<ref name = pmid12221117>{{cite journal | vauthors = Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O | title = ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization | journal = Mol. Biol. Cell | volume = 13 | issue = 9 | pages = 3078–95  | date = September 2002 | pmid = 12221117 | pmc = 124144 | doi = 10.1091/mbc.E02-02-0078 }}</ref><ref name = pmid10749927>{{cite journal | vauthors = Boman AL, ((Zhang Cj)), Zhu X, Kahn RA | title = A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi | journal = Mol. Biol. Cell | volume = 11 | issue = 4 | pages = 1241–55  | date = April 2000 | pmid = 10749927 | pmc = 14844 | doi =  10.1091/mbc.11.4.1241}}</ref>  and
* [[KIF23]].<ref name = pmid10506747>{{cite journal | vauthors = Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA | title = Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion | journal = Cell Motil. Cytoskeleton | volume = 44 | issue = 2 | pages = 119–32  | date = October 1999 | pmid = 10506747 | doi = 10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C }}</ref>
{{Div col end}}
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|ARF3}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lee FJ, Moss J, Vaughan M | title = Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae | journal = J. Biol. Chem. | volume = 267 | issue = 34 | pages = 24441–5 | year = 1992 | pmid = 1447192 | doi =  }}
| citations =
* {{cite journal | vauthors = Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M | title = Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin | journal = J. Biol. Chem. | volume = 267 | issue = 13 | pages = 9028–34 | year = 1992 | pmid = 1577740 | doi =  }}
*{{cite journal | author=Lee FJ, Moss J, Vaughan M |title=Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24441-5 |year= 1992 |pmid= 1447192 |doi=  }}
* {{cite journal | vauthors = Tsai SC, Haun RS, Tsuchiya M, Moss J, Vaughan M | title = Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin | journal = J. Biol. Chem. | volume = 266 | issue = 34 | pages = 23053–9 | year = 1991 | pmid = 1744102 | doi =  }}
*{{cite journal | author=Lee CM, Haun RS, Tsai SC, ''et al.'' |title=Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin. |journal=J. Biol. Chem. |volume=267 |issue= 13 |pages= 9028-34 |year= 1992 |pmid= 1577740 |doi=  }}
* {{cite journal | vauthors = Stearns T, Willingham MC, Botstein D, Kahn RA | title = ADP-ribosylation factor is functionally and physically associated with the Golgi complex | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 3 | pages = 1238–42 | year = 1990 | pmid = 2105501 | pmc = 53446 | doi = 10.1073/pnas.87.3.1238 }}
*{{cite journal | author=Tsai SC, Haun RS, Tsuchiya M, ''et al.'' |title=Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin. |journal=J. Biol. Chem. |volume=266 |issue= 34 |pages= 23053-9 |year= 1992 |pmid= 1744102 |doi=  }}
* {{cite journal | vauthors = Bobak DA, Nightingale MS, Murtagh JJ, Price SR, Moss J, Vaughan M | title = Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 86 | issue = 16 | pages = 6101–5 | year = 1989 | pmid = 2474826 | pmc = 297783 | doi = 10.1073/pnas.86.16.6101 }}
*{{cite journal | author=Stearns T, Willingham MC, Botstein D, Kahn RA |title=ADP-ribosylation factor is functionally and physically associated with the Golgi complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 1238-42 |year= 1990 |pmid= 2105501 |doi= }}
* {{cite journal | vauthors = Orcl L, Palmer DJ, Amherdt M, Rothman JE | title = Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol | journal = Nature | volume = 364 | issue = 6439 | pages = 732–4 | year = 1993 | pmid = 8355790 | doi = 10.1038/364732a0 }}
*{{cite journal | author=Bobak DA, Nightingale MS, Murtagh JJ, ''et al.'' |title=Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 16 |pages= 6101-5 |year= 1989 |pmid= 2474826 |doi= }}
* {{cite journal | vauthors = Haun RS, Moss J, Vaughan M | title = Characterization of the human ADP-ribosylation factor 3 promoter. Transcriptional regulation of a TATA-less promoter | journal = J. Biol. Chem. | volume = 268 | issue = 12 | pages = 8793–800 | year = 1993 | pmid = 8473323 | doi =  }}
*{{cite journal | author=Orcl L, Palmer DJ, Amherdt M, Rothman JE |title=Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. |journal=Nature |volume=364 |issue= 6439 |pages= 732-4 |year= 1993 |pmid= 8355790 |doi= 10.1038/364732a0 }}
* {{cite journal | vauthors = Helms JB, Palmer DJ, Rothman JE | title = Two distinct populations of ARF bound to Golgi membranes | journal = J. Cell Biol. | volume = 121 | issue = 4 | pages = 751–60 | year = 1993 | pmid = 8491770 | pmc = 2119793 | doi = 10.1083/jcb.121.4.751 }}
*{{cite journal | author=Haun RS, Moss J, Vaughan M |title=Characterization of the human ADP-ribosylation factor 3 promoter. Transcriptional regulation of a TATA-less promoter. |journal=J. Biol. Chem. |volume=268 |issue= 12 |pages= 8793-800 |year= 1993 |pmid= 8473323 |doi=  }}
* {{cite journal | vauthors = Hosaka M, Toda K, Takatsu H, Torii S, Murakami K, Nakayama K | title = Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6) | journal = J. Biochem. | volume = 120 | issue = 4 | pages = 813–9 | year = 1996 | pmid = 8947846 | doi = 10.1093/oxfordjournals.jbchem.a021484 }}
*{{cite journal | author=Helms JB, Palmer DJ, Rothman JE |title=Two distinct populations of ARF bound to Golgi membranes. |journal=J. Cell Biol. |volume=121 |issue= 4 |pages= 751-60 |year= 1993 |pmid= 8491770 |doi= }}
* {{cite journal | vauthors = Kanoh H, Williger BT, Exton JH | title = Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes | journal = J. Biol. Chem. | volume = 272 | issue = 9 | pages = 5421–9 | year = 1997 | pmid = 9038142 | doi = 10.1074/jbc.272.9.5421 }}
*{{cite journal | author=Hirai M, Kusuda J, Hashimoto K |title=Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively. |journal=Genomics |volume=34 |issue= 2 |pages= 263-5 |year= 1997 |pmid= 8661066 |doi= 10.1006/geno.1996.0283 }}
* {{cite journal | vauthors = Williger BT, Provost JJ, Ho WT, Milstine J, Exton JH | title = Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D | journal = FEBS Lett. | volume = 454 | issue = 1-2 | pages = 85–9 | year = 1999 | pmid = 10413101 | doi = 10.1016/S0014-5793(99)00771-1 }}
*{{cite journal | author=Hosaka M, Toda K, Takatsu H, ''et al.'' |title=Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6). |journal=J. Biochem. |volume=120 |issue= 4 |pages= 813-9 |year= 1997 |pmid= 8947846 |doi= }}
* {{cite journal | vauthors = Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA | title = Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion | journal = Cell Motil. Cytoskeleton | volume = 44 | issue = 2 | pages = 119–32 | year = 1999 | pmid = 10506747 | doi = 10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C }}
*{{cite journal | author=Kanoh H, Williger BT, Exton JH |title=Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. |journal=J. Biol. Chem. |volume=272 |issue= 9 |pages= 5421-9 |year= 1997 |pmid= 9038142 |doi= }}
* {{cite journal | vauthors = Takeya R, Takeshige K, Sumimoto H | title = Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors | journal = Biochem. Biophys. Res. Commun. | volume = 267 | issue = 1 | pages = 149–55 | year = 2000 | pmid = 10623590 | doi = 10.1006/bbrc.1999.1932 }}
*{{cite journal | author=Williger BT, Provost JJ, Ho WT, ''et al.'' |title=Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D. |journal=FEBS Lett. |volume=454 |issue= 1-2 |pages= 85-9 |year= 1999 |pmid= 10413101 |doi= }}
* {{cite journal | vauthors = Boman AL, ((Zhang Cj)), Zhu X, Kahn RA | title = A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi | journal = Mol. Biol. Cell | volume = 11 | issue = 4 | pages = 1241–55 | year = 2000 | pmid = 10749927 | pmc = 14844 | doi = 10.1091/mbc.11.4.1241 }}
*{{cite journal  | author=Boman AL, Kuai J, Zhu X, ''et al.'' |title=Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion. |journal=Cell Motil. Cytoskeleton |volume=44 |issue= 2 |pages= 119-32 |year= 1999 |pmid= 10506747 |doi= 10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C }}
* {{cite journal | vauthors = Nevrivy DJ, Peterson VJ, Avram D, Ishmael JE, Hansen SG, Dowell P, Hruby DE, Dawson MI, Leid M | title = Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors | journal = J. Biol. Chem. | volume = 275 | issue = 22 | pages = 16827–36 | year = 2000 | pmid = 10828067 | doi = 10.1074/jbc.275.22.16827 }}
*{{cite journal | author=Takeya R, Takeshige K, Sumimoto H |title=Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors. |journal=Biochem. Biophys. Res. Commun. |volume=267 |issue= 1 |pages= 149-55 |year= 2000 |pmid= 10623590 |doi= 10.1006/bbrc.1999.1932 }}
* {{cite journal | vauthors = Zhdankina O, Strand NL, Redmond JM, Boman AL | title = Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi | journal = Yeast | volume = 18 | issue = 1 | pages = 1–18 | year = 2001 | pmid = 11124697 | doi = 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5 }}
*{{cite journal | author=Boman AL, Zhang C, Zhu X, Kahn RA |title=A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. |journal=Mol. Biol. Cell |volume=11 |issue= 4 |pages= 1241-55 |year= 2000 |pmid= 10749927 |doi= }}
* {{cite journal | vauthors = Irobi J, Nelis E, Verhoeven K, De Vriendt E, Dierick I, De Jonghe P, Van Broeckhoven C, Timmerman V | title = Mutation analysis of 12 candidate genes for distal hereditary motor neuropathy type II (distal HMN II) linked to 12q24.3 | journal = J. Peripher. Nerv. Syst. | volume = 7 | issue = 2 | pages = 87–95 | year = 2002 | pmid = 12090300 | doi = 10.1046/j.1529-8027.2002.02014.x }}
*{{cite journal | author=Nevrivy DJ, Peterson VJ, Avram D, ''et al.'' |title=Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16827-36 |year= 2000 |pmid= 10828067 |doi= }}
* {{cite journal | vauthors = Li F, Mandal M, Mishra SK, Barnes CJ, Kumar R | title = Heregulin promotes expression and subcellular redistribution of ADP-ribosylation factor 3 | journal = FEBS Lett. | volume = 524 | issue = 1-3 | pages = 49–53 | year = 2002 | pmid = 12135740 | doi = 10.1016/S0014-5793(02)02994-0 }}
*{{cite journal  | author=Zhdankina O, Strand NL, Redmond JM, Boman AL |title=Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi. |journal=Yeast |volume=18 |issue= 1 |pages= 1-18 |year= 2001 |pmid= 11124697 |doi= 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5 }}
* {{cite journal | vauthors = Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O | title = ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization | journal = Mol. Biol. Cell | volume = 13 | issue = 9 | pages = 3078–95 | year = 2002 | pmid = 12221117 | pmc = 124144 | doi = 10.1091/mbc.E02-02-0078 }}
*{{cite journal | author=Irobi J, Nelis E, Verhoeven K, ''et al.'' |title=Mutation analysis of 12 candidate genes for distal hereditary motor neuropathy type II (distal HMN II) linked to 12q24.3. |journal=J. Peripher. Nerv. Syst. |volume=7 |issue= 2 |pages= 87-95 |year= 2002 |pmid= 12090300 |doi= }}
*{{cite journal | author=Li F, Mandal M, Mishra SK, ''et al.'' |title=Heregulin promotes expression and subcellular redistribution of ADP-ribosylation factor 3. |journal=FEBS Lett. |volume=524 |issue= 1-3 |pages= 49-53 |year= 2002 |pmid= 12135740 |doi=  }}
*{{cite journal  | author=Boman AL, Salo PD, Hauglund MJ, ''et al.'' |title=ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization. |journal=Mol. Biol. Cell |volume=13 |issue= 9 |pages= 3078-95 |year= 2003 |pmid= 12221117 |doi= 10.1091/mbc.E02-02-0078 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=377}}
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{{gene-12-stub}}

Latest revision as of 18:11, 29 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

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n/a

UniProt

n/a

n/a

RefSeq (mRNA)

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n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: ARF3 ADP-ribosylation factor 3".
  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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 6.0 6.1 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 14844. PMID 10749927.
  7. ↑ 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.

External links

Further reading


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