ARF3

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ADP-ribosylation factor 3
Protein ARF3 PDB 1hur.png
PDB rendering based on 1hur.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbol ARF3
External IDs OMIM103190 MGI99432 HomoloGene68195 GeneCards: ARF3 Gene
RNA expression pattern
PBB GE ARF3 200734 s at tn.png
PBB GE ARF3 211622 s at tn.png
PBB GE ARF3 200011 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 377 11842
Ensembl ENSG00000134287 ENSMUSG00000051853
UniProt P61204 P61205
RefSeq (mRNA) NM_001659 NM_007478
RefSeq (protein) NP_001650 NP_031504
Location (UCSC) Chr 12:
49.3 – 49.35 Mb
Chr 15:
98.74 – 98.76 Mb
PubMed search [1] [2]

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.[1][2]

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.[2]

Interactions[edit]

ARF3 has been shown to interact with ARFIP2,[3] GGA3,[4][5] GGA1,[4][5] ARFIP1[3][6] and KIF23.[7]

References[edit]

  1. ^ Hirai M, Kusuda J, Hashimoto K (February 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. 
  2. ^ a b "Entrez Gene: ARF3 ADP-ribosylation factor 3". 
  3. ^ a b 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. (UNITED STATES) 272 (9): 5421–9. doi:10.1074/jbc.272.9.5421. ISSN 0021-9258. PMID 9038142. 
  4. ^ a b Boman, Annette L; Salo Paul D; Hauglund Melissa J; Strand Nicole L; Rensink Shelly J; Zhdankina Olga (September 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell (United States) 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. ISSN 1059-1524. PMC 124144. PMID 12221117. 
  5. ^ a b Boman, A L; Zhang C j; Zhu X; Kahn R A (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol. Biol. Cell (UNITED STATES) 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. ISSN 1059-1524. PMC 14844. PMID 10749927. 
  6. ^ Williger, B T; Provost J J; Ho W T; Milstine J; Exton J H (July 1999). "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D". FEBS Lett. (NETHERLANDS) 454 (1-2): 85–9. doi:10.1016/S0014-5793(99)00771-1. ISSN 0014-5793. PMID 10413101. 
  7. ^ Boman, A L; Kuai J; Zhu X; Chen J; Kuriyama R; Kahn R A (October 1999). "Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion". Cell Motil. Cytoskeleton (UNITED STATES) 44 (2): 119–32. doi:10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C. ISSN 0886-1544. PMID 10506747. 

Further reading[edit]