ARF3

ARF3

Identifiers

ARF3, ADP ribosylation factor 3

External IDs

OMIM: 103190; MGI: 99432; GeneCards: ARF3

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q13.12	Start	48,935,723 bp^[1]
Band	12q13.12	End	48,957,487 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15\|15 F1	Start	98,634,515 bp^[2]
Band	15\|15 F1	End	98,661,095 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

prefrontal cortex

entorhinal cortex

postcentral gyrus

Brodmann area 10

superior frontal gyrus

Brodmann area 46

Region I of hippocampus proper

frontal pole

nucleus accumbens

dorsolateral prefrontal cortex

Top expressed in

nucleus accumbens

dorsal striatum

dentate gyrus of hippocampal formation granule cell

olfactory tubercle

prefrontal cortex

superior frontal gyrus

lateral septal nucleus

anterior amygdaloid area

piriform cortex

Region I of hippocampus proper

More reference expression data


More reference expression data

Gene ontology
Molecular function	nucleotide binding GTP binding GTPase activity
Cellular component	cytoplasm perinuclear region of cytoplasm Golgi membrane Golgi apparatus extracellular exosome intracellular anatomical structure plasma membrane
Biological process	protein transport phosphatidylinositol biosynthetic process small GTPase mediated signal transduction vesicle-mediated transport retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum transport intracellular protein transport Golgi to plasma membrane transport
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


377


11842


ENSG00000134287


ENSMUSG00000051853


P61204


P61205

RefSeq (mRNA)


NM_001659


NM_007478 NM_001355510

RefSeq (protein)


NP_001650


NP_031504 NP_001342439

Location (UCSC)

Chr 12: 48.94 – 48.96 Mb

Chr 15: 98.63 – 98.66 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.^[5]^[6]

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.^[6]

Interactions

ARF3 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000134287 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000051853 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "Entrez Gene: ARF3 ADP-ribosylation factor 3".
^ ^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.
^ 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. S2CID 40655171.
^ ^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 124144. PMID 12221117.
^ ^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 14844. PMID 10749927.
^ 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

Human ARF3 genome location and ARF3 gene details page in the UCSC Genome Browser.

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. doi:10.1016/S0021-9258(18)35786-7. 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. doi:10.1016/S0021-9258(19)50383-0. 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. doi:10.1016/S0021-9258(18)54462-8. 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. Bibcode:1990PNAS...87.1238S. 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. Bibcode:1989PNAS...86.6101B. 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. Bibcode:1993Natur.364..732O. doi:10.1038/364732a0. PMID 8355790. S2CID 4348442.
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. doi:10.1016/S0021-9258(18)52944-6. 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. S2CID 40655171.
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 Cj, 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, Hruby DE, Dawson MI, Leid M (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. S2CID 10348751.
Irobi J, Nelis E, Verhoeven K, De Vriendt E, Dierick I, De Jonghe P, Van Broeckhoven C, Timmerman V (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. S2CID 8453412.
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. S2CID 36764648.
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

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