ARF1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARF1, ADP ribosylation factor 1, PVNH8
External IDsOMIM: 103180 MGI: 99431 HomoloGene: 133930 GeneCards: ARF1
Orthologs
SpeciesHumanMouse
Entrez

375

11840

Ensembl

ENSG00000143761

ENSMUSG00000048076

UniProt

P84077

P84078

RefSeq (mRNA)

NM_001658
NM_001024226
NM_001024227
NM_001024228

NM_001130408
NM_007476

RefSeq (protein)

NP_001019397
NP_001019398
NP_001019399
NP_001649

NP_001123880
NP_031502

Location (UCSC)Chr 1: 228.08 – 228.1 MbChr 11: 59.1 – 59.12 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene.[5]

Function

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.[6]

The major mechanism of action of Brefeldin A is through inhibition of ARF1.

Interactions

ARF1 has been shown to interact with:

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000143761 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000048076 - 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.
  5. Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M (June 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. doi:10.1016/S0021-9258(19)50383-0. PMID 1577740.
  6. "Entrez Gene: ARF1 ADP-ribosylation factor 1".
  7. Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September 2003). "ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor". J. Biol. Chem. 278 (36): 33818–30. doi:10.1074/jbc.M305825200. PMID 12799371.
  8. Fischer KD, Helms JB, Zhao L, Wieland FT (April 2000). "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods. 20 (4): 455–64. doi:10.1006/meth.2000.0958. PMID 10720466.
  9. Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP". EMBO J. 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. PMC 306616. PMID 10921873.
  10. Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (April 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". J. Cell Biol. 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.
  11. Puertollano R, Randazzo PA, Presley JF, Hartnell LM, Bonifacino JS (April 2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell. 105 (1): 93–102. doi:10.1016/s0092-8674(01)00299-9. PMID 11301005. S2CID 1158816.
  12. Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH (July 2001). "Actin directly interacts with phospholipase D, inhibiting its activity". J. Biol. Chem. 276 (30): 28252–60. doi:10.1074/jbc.M008521200. PMID 11373276.
  13. Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH (July 2000). "Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner". J. Biol. Chem. 275 (28): 21295–301. doi:10.1074/jbc.M002463200. PMID 10801846.

Further reading


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