ARF3

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.[5][6]

ARF3
Identifiers
AliasesARF3, ADP ribosylation factor 3
External IDsOMIM: 103190 MGI: 99432 HomoloGene: 68195 GeneCards: ARF3
Orthologs
SpeciesHumanMouse
Entrez

377

11842

Ensembl

ENSG00000134287

ENSMUSG00000051853

UniProt

P61204

P61205

RefSeq (mRNA)

NM_001659

NM_007478
NM_001355510

RefSeq (protein)

NP_001650

NP_031504
NP_001342439

Location (UCSC)Chr 12: 48.94 – 48.96 MbChr 15: 98.63 – 98.66 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

ADP-ribosylation factor 3 (ARF3) 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) and members of each class share a common gene organization. The ARF3 gene contains five exons and four introns.[6]

Interactions

ARF3 has been shown to interact with:

References

  1. GRCh38: Ensembl release 89: ENSG00000134287 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000051853 - 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. Hirai M, Kusuda J, Hashimoto K (June 1996). "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.
  6. "Entrez Gene: ARF3 ADP-ribosylation factor 3".
  7. Kanoh H, Williger BT, Exton JH (February 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.
  8. Williger BT, Provost JJ, Ho WT, Milstine J, Exton JH (July 1999). "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D". FEBS Lett. 454 (1–2): 85–9. doi:10.1016/s0014-5793(99)00771-1. PMID 10413101. S2CID 40655171.
  9. Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O (September 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144. PMID 12221117.
  10. Boman AL, Zhang Cj, Zhu X, Kahn RA (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol. Biol. Cell. 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. PMC 14844. PMID 10749927.
  11. Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (October 1999). "Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion". Cell Motil. Cytoskeleton. 44 (2): 119–32. doi:10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C. PMID 10506747.

Further reading


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