ARF1

From Wikipedia, the free encyclopedia

ADP-ribosylation factor 1

PDB rendering based on 1hur.

Available structures: 1hur, 1j2j, 1o3y, 1r8q, 1r8s, 1re0, 1rrf, 1rrg, 1s9d, 1u81, 2j59

Identifiers

Symbol(s)

ARF1;

External IDs

OMIM: 103180 MGI: 99431 HomoloGene: 56086

Gene ontology
Molecular Function:	• nucleotide binding • GTPase activity • receptor signaling protein activity • protein binding • GTP binding
Cellular Component:	• intracellular • 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_001024226 (mRNA)
NP_001019397 (protein)

NM_007476 (mRNA)
NP_031502 (protein)

Location

Chr 1: 226.34 - 226.35 Mb

Chr 11: 59.03 - 59.04 Mb

Pubmed search

[1]

[2]

ADP-ribosylation factor 1, also known as ARF1, is a human gene.

ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a 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), and members of each class share a common gene organization. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.^[1]

[edit] References

^ Entrez Gene: ARF1 ADP-ribosylation factor 1.

[edit] Further reading

Lee CM, Haun RS, Tsai SC, et al. (1992). "Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin.". J. Biol. Chem. 267 (13): 9028-34. PMID 1577740.
Serafini T, Orci L, Amherdt M, et al. (1991). "ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein.". Cell 67 (2): 239-53. PMID 1680566.
Kahn RA, Kern FG, Clark J, et al. (1991). "Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins.". J. Biol. Chem. 266 (4): 2606-14. PMID 1899243.
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.
Bobak DA, Nightingale MS, Murtagh JJ, et al. (1989). "Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin.". Proc. Natl. Acad. Sci. U.S.A. 86 (16): 6101-5. PMID 2474826.
Greasley SE, Jhoti H, Teahan C, et al. (1995). "The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms.". Nat. Struct. Biol. 2 (9): 797-806. PMID 7552752.
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. PMID 7898460.
Greasley S, Jhoti H, Fensome AC, et al. (1995). "Crystallization and preliminary X-ray diffraction studies on ADP-ribosylation factor 1.". J. Mol. Biol. 244 (5): 651-3. doi:10.1006/jmbi.1994.1759. PMID 7990146.
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.
Dascher C, Balch WE (1994). "Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus.". J. Biol. Chem. 269 (2): 1437-48. PMID 8288610.
Rümenapp U, Geiszt M, Wahn F, et al. (1996). "Evidence for ADP-ribosylation-factor-mediated activation of phospholipase D by m3 muscarinic acetylcholine receptor.". Eur. J. Biochem. 234 (1): 240-4. PMID 8529647.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107-13. doi:10.1006/abio.1996.0138. PMID 8619474.
Hirai M, Kusuda J, Hashimoto K (1997). "Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively.". Genomics 34 (2): 263-5. doi:10.1006/geno.1996.0283. PMID 8661066.
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.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353-8. PMID 9110174.
Shome K, Vasudevan C, Romero G (1997). "ARF proteins mediate insulin-dependent activation of phospholipase D.". Curr. Biol. 7 (6): 387-96. PMID 9197239.
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. PMID 9417041.
Betz SF, Schnuchel A, Wang H, et al. (1998). "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1.". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7909-14. PMID 9653114.
Kim JH, Lee SD, Han JM, et al. (1998). "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA.". FEBS Lett. 430 (3): 231-5. PMID 9688545.
Huber I, Cukierman E, Rotman M, et al. (1998). "Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein.". J. Biol. Chem. 273 (38): 24786-91. PMID 9733781.