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ARF5
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2B6H
Identifiers
Aliases	ARF5, ADP ribosylation factor 5
External IDs	OMIM: 103188; MGI: 99434; HomoloGene: 129625; GeneCards: ARF5; OMA:ARF5 - orthologs
Gene location (Human)
Chr.	Chromosome 7 (human)
End	127,591,700 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	28,426,601 bp
RNA expression pattern
	Top expressed in
	prefrontal cortex; ; Brodmann area 9; ; skin of leg; ; right frontal lobe; ; skin of abdomen; ; body of pancreas; ; right hemisphere of cerebellum; ; primary visual cortex; ; superior frontal gyrus; ; granulocyte;
	Top expressed in
	lip; ; dentate gyrus of hippocampal formation granule cell; ; granulocyte; ; primary visual cortex; ; superior frontal gyrus; ; ventricular zone; ; perirhinal cortex; ; right kidney; ; yolk sac; ; entorhinal cortex;
	More reference expression data
	More reference expression data
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 anatomical structure; membrane;
Biological process	protein transport; 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
Orthologs
	381
	11844
	ENSG00000004059
	ENSMUSG00000020440
	P84085
	P84084
	NM_001662
	NM_007480
	NP_001653
	NP_031506
	Wikidata
View/Edit Human	View/Edit Mouse

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.^[5]^[6]

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.^[6]

Interactions

ARF5 has been shown to interact with ARFIP2.^[7]^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000004059 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020440 – 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.
^ 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. doi:10.1016/S0021-9258(18)49913-9. PMID 1993656.
^ ^a ^b "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. 272 (9). UNITED STATES: 5421–9. doi:10.1074/jbc.272.9.5421. ISSN 0021-9258. PMID 9038142.
^ Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. 285 (5). United States: 1267–73. doi:10.1006/bbrc.2001.5330. ISSN 0006-291X. PMID 11478794.

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. doi:10.1016/S0021-9258(18)35786-7. 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. Bibcode:1990PNAS...87.1238S. 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. Bibcode:1993Natur.364..732O. doi:10.1038/364732a0. PMID 8355790. S2CID 4348442.
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. doi:10.1128/MCB.19.3.2338. 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. S2CID 10031591.
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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2003Sci...300..767S. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000004059 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020440 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1993656-5] 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. doi:10.1016/S0021-9258(18)49913-9. PMID 1993656.

[entrez-6] "Entrez Gene: ARF5 ADP-ribosylation factor 5".

[pmid9038142-7] 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. 272 (9). UNITED STATES: 5421–9. doi:10.1074/jbc.272.9.5421. ISSN 0021-9258. PMID 9038142.

[pmid11478794-8] Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. 285 (5). United States: 1267–73. doi:10.1006/bbrc.2001.5330. ISSN 0006-291X. PMID 11478794.

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ARF5

Interactions

References

External links

Further reading

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