ARF5

From Wikipedia, the free encyclopedia

ADP-ribosylation factor 5

PDB rendering based on 1z6x.

Available structures: 1z6x, 2b6h

Identifiers

Symbol(s)

ARF5;

External IDs

OMIM: 103188 MGI: 99434 HomoloGene: 81688

Gene ontology
Molecular Function:	• nucleotide binding • GTPase activity • GTP binding
Cellular Component:	• intracellular • cytoplasm • plasma membrane
Biological Process:	• ER to Golgi vesicle-mediated transport • small GTPase mediated signal transduction • protein transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001662 (mRNA)
NP_001653 (protein)

XM_988159 (mRNA)
XP_993253 (protein)

Location

Chr 7: 127.02 - 127.02 Mb

Chr 6: 28.37 - 28.38 Mb

Pubmed search

[1]

[2]

ADP-ribosylation factor 5, also known as ARF5, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ARF5 ADP-ribosylation factor 5.

[edit] 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.
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. 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. 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. 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. 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.
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.
Kondo A, Hashimoto S, Yano H, et al. (2000). "A new paxillin-binding protein, PAG3/Papalpha/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. 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. 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. 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. 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. 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. 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. 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.