Arf6

Wednesday, 26 March 2025

ADP-ribosylation factor 6

PDB rendering based on 1e0s.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1E0S, 2A5D, 2A5F, 2A5G, 2BAO, 2BAU, 2J5X, 2W83, 3LVQ, 3LVR, 3N5C, 3PCR

Identifiers

Symbols

ARF6; []

External IDs

OMIM: 600464 MGI: 99435 HomoloGene: 1256 ChEMBL: 5987 GeneCards: ARF6 Gene

Gene Ontology
Molecular function	• nucleotide binding • GTPase activity • protein binding • GTP binding • thioesterase binding
Cellular component	• ruffle • intracellular • membrane fraction • cytoplasm • endosome • endosome • early endosome • Golgi apparatus • plasma membrane • cell cortex • endosome membrane • filopodium membrane • recycling endosome
Biological process	• liver development • GTP catabolic process • apoptotic process • cellular component movement • cell adhesion • small GTPase mediated signal transduction • nervous system development • protein transport • vesicle-mediated transport • cell differentiation • positive regulation of actin filament polymerization • cortical actin cytoskeleton organization • ruffle organization • protein localization at cell surface • regulation of Rac protein signal transduction • negative regulation of receptor-mediated endocytosis • regulation of filopodium assembly • regulation of dendritic spine development • positive regulation of establishment of protein localization in plasma membrane
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
50.36 – 50.36 Mb

Chr 12:
70.47 – 70.48 Mb

PubMed search

[1]

[2]

ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety of cellular functions that are frequently involved in trafficking of biological membranes and transmembrane protein cargo. ARF6 has specifically been implicated in endocytosis of plasma membrane proteins and also, to a lesser extent, plasma membrane protein recycling.

This gene encodes a member of the human ARF gene family, which is part of the RAS superfamily. The ARF 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 product of this gene is localized to the plasma membrane, and regulates vesicular trafficking, remodelling of membrane lipids, and signaling pathways that lead to actin remodeling. A pseudogene of this gene is located on chromosome 7.^[1]

ARF6 can interact with βarrestin upon receptor activation.

1 Interactions
2 References
3 Further reading
4 External links

Interactions [link]

Arf6 has been shown to interact with:

Arrestin beta 1,^[2]
ARFIP2,^[3]^[4]
EXOC5,^[5] and
KIAA0090,^[6]
Muscarinic acetylcholine receptor M3.^[7]

References [link]

^ "Entrez Gene: ARF6 ADP-ribosylation factor 6". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=382.
^ Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (November 2001). "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45): 42509–13. DOI:10.1074/jbc.M108399200. PMID 11533043.
^ D'Souza-Schorey C, Boshans RL, McDonough M, Stahl PD, Van Aelst L (September 1997). "A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements". EMBO J. 16 (17): 5445–54. DOI:10.1093/emboj/16.17.5445. PMC 1170175. PMID 9312003. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170175.
^ Shin OH, Exton JH (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. 285 (5): 1267–73. DOI:10.1006/bbrc.2001.5330. PMID 11478794.
^ Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C, Camonis J, Chavrier P (December 2003). "ARF6 controls post-endocytic recycling through its downstream exocyst complex effector". J. Cell Biol. 163 (5): 1111–21. DOI:10.1083/jcb.200305029. PMC 2173613. PMID 14662749. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173613.
^ Prieto C, De Las Rivas J (July 2006). "APID: Agile Protein Interaction DataAnalyzer". Nucleic Acids Res. 34 (Web Server issue): W298–302. DOI:10.1093/nar/gkl128. PMC 1538863. PMID 16845013. https://bioinfow.dep.usal.es/apid/html/home.htm.
^ Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September 2003). "ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor". J. Biol. Chem. 278 (36): 33818–30. DOI:10.1074/jbc.M305825200. PMID 12799371.

Further reading [link]

Sabe H (2004). "Requirement for Arf6 in cell adhesion, migration, and cancer cell invasion". J. Biochem. 134 (4): 485–9. DOI:10.1093/jb/mvg181. PMID 14607973.
Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. DOI:10.2174/1570162052773013. PMID 15638726.
Tsuchiya M, Price SR, Tsai SC, et al. (1991). "Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells". J. Biol. Chem. 266 (5): 2772–7. PMID 1993656.
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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=53446.
D'Souza-Schorey C, Stahl PD (1995). "Myristoylation is required for the intracellular localization and endocytic function of ARF6". Exp. Cell Res. 221 (1): 153–9. DOI:10.1006/excr.1995.1362. PMID 7589240.
D'Souza-Schorey C, Li G, Colombo MI, Stahl PD (1995). "A regulatory role for ARF6 in receptor-mediated endocytosis". Science 267 (5201): 1175–8. DOI:10.1126/science.7855600. PMID 7855600.
Welsh CF, Moss J, Vaughan M (1995). "ADP-ribosylation factors: a family of approximately 20-kDa guanine nucleotide-binding proteins that activate cholera toxin". Mol. Cell. Biochem. 138 (1-2): 157–66. DOI:10.1007/BF00928458. PMID 7898460.
Amor JC, Harrison DH, Kahn RA, Ringe D (1995). "Structure of the human ADP-ribosylation factor 1 complexed with GDP". Nature 372 (6507): 704–8. DOI:10.1038/372704a0. PMID 7990966.
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.
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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2119793.
Cavenagh MM, Whitney JA, Carroll K, et al. (1996). "Intracellular distribution of Arf proteins in mammalian cells. Arf6 is uniquely localized to the plasma membrane". J. Biol. Chem. 271 (36): 21767–74. DOI:10.1074/jbc.271.36.21767. PMID 8702973.
D'Souza-Schorey C, Boshans RL, McDonough M, et al. (1997). "A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements". EMBO J. 16 (17): 5445–54. DOI:10.1093/emboj/16.17.5445. PMC 1170175. PMID 9312003. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170175.
Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6". J. Biol. Chem. 273 (1): 23–7. DOI:10.1074/jbc.273.1.23. PMID 9417041.
Yang CZ, Heimberg H, D'Souza-Schorey C, et al. (1998). "Subcellular distribution and differential expression of endogenous ADP-ribosylation factor 6 in mammalian cells". J. Biol. Chem. 273 (7): 4006–11. DOI:10.1074/jbc.273.7.4006. PMID 9461590.
Mao M, Fu G, Wu JS, et al. (1998). "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 8175–80. DOI:10.1073/pnas.95.14.8175. PMC 20949. PMID 9653160. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=20949.
Andreev J, Simon JP, Sabatini DD, et al. (1999). "Identification of a new Pyk2 target protein with Arf-GAP activity". Mol. Cell. Biol. 19 (3): 2338–50. PMC 84026. PMID 10022920. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84026.
Radhakrishna H, Al-Awar O, Khachikian Z, Donaldson JG (1999). "ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements". J. Cell. Sci. 112 (6): 855–66. PMID 10036235.
Kim HS (1999). "Assignment of the human ADP-ribosylation factor 6 (ARF6) gene to chromosome 7q22.1 by radiation hybrid mapping". Cytogenet. Cell Genet. 84 (1-2): 94. DOI:10.1159/000015225. PMID 10343114.
Langille SE, Patki V, Klarlund JK, et al. (1999). "ADP-ribosylation factor 6 as a target of guanine nucleotide exchange factor GRP1". J. Biol. Chem. 274 (38): 27099–104. DOI:10.1074/jbc.274.38.27099. PMID 10480924.
Honda A, Nogami M, Yokozeki T, et al. (1999). "Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation". Cell 99 (5): 521–32. DOI:10.1016/S0092-8674(00)81540-8. PMID 10589680.

PDB gallery

1e0s: SMALL G PROTEIN ARF6-GDP

2a5d: Structural basis for the activation of cholera toxin by human ARF6-GTP

2a5f: Cholera toxin A1 subunit bound to its substrate, NAD+, and its human protein activator, ARF6

2a5g: Cholera toxin A1 subunit bound to ARF6(Q67L)

2j5x: STRUCTURE OF THE SMALL G PROTEIN ARF6 IN COMPLEX WITH GTPGAMMAS

External links [link]

ARF6+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

Ikeda S, Ushio-Fukai M, Zuo L, et al. (2005). "Novel role of ARF6 in vascular endothelial growth factor-induced signaling and angiogenesis". Circ. Res. 96 (4): 467–75. DOI:10.1161/01.RES.0000158286.51045.16. PMID 15692085.

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)	SERCA (ATP2A1, ATP2A2, ATP2A3) Plasma membrane (ATP2B1, ATP2B2, ATP2B3, ATP2B4) SPCA (ATP2C1, ATP2C2)

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi (GNAI1, GNAI2, GNAI3) G_αq/11 (GNAQ, GNA11) G_α12/13 (GNA12, GNA13) Transducin (GNAT1, GNAT2)

3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 (CDC42, TC10, TCL) RhoUV (RhoU, RhoV) Rac (Rac1, 2, 3, RhoG) RhoBTB (1, 2) RhoH Rho (A, B, C) Rnd (1, 2, 3) RhoDF (RhoF, RhoD) other: Ras (HRAS, KRAS, NRAS) Rab (RAB23, RAB27) Arf (ARF6, SAR1B, ARL13B, ARL6) Ran Rheb Rap

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic (IF-2, EF-Tu, EF-G) Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

B
enzm
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- 15-18
2.1
- 2
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2.7.10
2.7.11-12
3.1
- 2
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- 4
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- 7
3.1.3.48
3.4.21
- 22
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4.1
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5.1
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6.1-3
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This article on a gene on chromosome 14 is a stub. You can help Wikipedia by expanding it.

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