ARF5

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2B6H

Identifiers

Aliases

ARF5, ADP ribosylation factor 5

External IDs

MGI: 99434 HomoloGene: 129625 GeneCards: ARF5

Gene ontology
Molecular function	• nucleotide binding • GTP binding • protein binding • GTPase activity
Cellular component	• cytoplasm • perinuclear region of cytoplasm • plasma membrane • Golgi apparatus • extracellular exosome • intracellular • membrane
Biological process	• protein transport • small GTPase mediated signal transduction • vesicle-mediated transport • retrograde vesicle-mediated transport, Golgi to ER • 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

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.^[3]^[4]

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.^[4]

Interactions

ARF5 has been shown to interact with ARFIP2.^[5]^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: ARF5 ADP-ribosylation factor 5".
↑ 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. ISSN 0021-9258. PMID 9038142. doi:10.1074/jbc.272.9.5421.
↑ 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. ISSN 0006-291X. PMID 11478794. doi:10.1006/bbrc.2001.5330.

External links

Human ARF5 genome location and ARF5 gene details page in the UCSC Genome Browser.

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. PMC 53446 . PMID 2105501. doi:10.1073/pnas.87.3.1238.
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. PMID 8355790. doi:10.1038/364732a0.
Helms JB, Palmer DJ, Rothman JE (1993). "Two distinct populations of ARF bound to Golgi membranes". J. Cell Biol. 121 (4): 751–60. PMC 2119793 . PMID 8491770. doi:10.1083/jcb.121.4.751.
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. PMID 9038142. doi:10.1074/jbc.272.9.5421.
McGuire RE, Daiger SP, Green ED (1997). "Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene". Genomics. 41 (3): 481–4. PMID 9169151. doi:10.1006/geno.1997.4689.
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. PMID 10589680. doi:10.1016/S0092-8674(00)81540-8.
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. PMID 10593962. doi:10.1074/jbc.274.51.36609.
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. PMC 14849 . PMID 10749932. doi:10.1091/mbc.11.4.1315.
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. PMID 10828067. doi:10.1074/jbc.275.22.16827.
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. PMID 11535061. doi:10.1021/bi0107391.
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. PMID 11926829. doi:10.1021/bi016064j.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science. 300 (5620): 767–72. PMC 2882961 . PMID 12690205. doi:10.1126/science.1083423.
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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
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. PMID 16189514. doi:10.1038/nature04209.

PDB gallery

1z6x: Structure Of Human ADP-Ribosylation Factor 4

2b6h: Structure of human ADP-ribosylation factor 5

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ARF5

Interactions

References

External links

Further reading