ARF5

ADP-ribosylation factor 5
PDB rendering based on 1z6x.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2B6H​
Identifiers
Symbol	ARF5
External IDs	OMIM: 103188 MGI: 99434 HomoloGene: 129625 ChEMBL: 5986 GeneCards: ARF5 Gene
Gene ontology Molecular function • GTPase activity • protein binding • GTP binding Cellular component • Golgi apparatus • plasma membrane • perinuclear region of cytoplasm • extracellular exosome Biological process • small GTPase mediated signal transduction • protein transport • vesicle-mediated transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	381	11844
Ensembl	ENSG00000004059	ENSMUSG00000020440
UniProt	P84085	P84084
RefSeq (mRNA)	NM_001662	NM_007480
RefSeq (protein)	NP_001653	NP_031506
Location (UCSC)	Chr 7: 127.59 – 127.59 Mb	Chr 6: 28.42 – 28.43 Mb
PubMed search

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.^[1][2]

ADP-ribosylation factor 5 (ARF5) 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). The members of each class share a common gene organization. The ARF5 gene spans approximately 3.2kb of genomic DNA and contains six exons and five introns.^[2]

Interactions

ARF5 has been shown to interact with ARFIP2.^[3][4]

References

1. Tsuchiya M, Price SR, Tsai SC, Moss J, Vaughan M (March 1991). "Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells". J Biol Chem 266 (5): 2772–7. PMID 1993656.
2. "Entrez Gene: ARF5 ADP-ribosylation factor 5".
3. Kanoh, H; Williger B T; Exton J H (February 1997). "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes". J. Biol. Chem. (UNITED STATES) 272 (9): 5421–9. doi:10.1074/jbc.272.9.5421. ISSN 0021-9258. PMID 9038142.
4. Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. (United States) 285 (5): 1267–73. doi:10.1006/bbrc.2001.5330. ISSN 0006-291X. PMID 11478794.

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.
• 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.
• 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.
• 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.
• McGuire RE, Daiger SP, Green ED (1997). "Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene". Genomics 41 (3): 481–4. doi:10.1006/geno.1997.4689. PMID 9169151.
• 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.
• 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.
• Shin OH, Ross AH, Mihai I, Exton JH (2000). "Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors". J. Biol. Chem. 274 (51): 36609–15. doi:10.1074/jbc.274.51.36609. PMID 10593962.
• Kondo A, Hashimoto S, Yano H; et al. (2000). "A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein Activity, Is Involved in Paxillin Recruitment to Focal Adhesions and Cell Migration". Mol. Biol. Cell 11 (4): 1315–27. doi:10.1091/mbc.11.4.1315. PMC 14849. PMID 10749932.
• 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. doi:10.1074/jbc.275.22.16827. PMID 10828067.
• Shin OH, Couvillon AD, Exton JH (2001). "Arfophilin is a common target of both class II and class III ADP-ribosylation factors". Biochemistry 40 (36): 10846–52. doi:10.1021/bi0107391. PMID 11535061.
• Austin C, Boehm M, Tooze SA (2002). "Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry 41 (14): 4669–77. doi:10.1021/bi016064j. PMID 11926829.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Scherer SW, Cheung J, MacDonald JR; et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.