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ARF5

From Wikipedia, the free encyclopedia
ARF5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARF5, ADP ribosylation factor 5
External IDsOMIM: 103188; MGI: 99434; HomoloGene: 129625; GeneCards: ARF5; OMA:ARF5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001662

NM_007480

RefSeq (protein)

NP_001653

NP_031506

Location (UCSC)Chr 7: 127.59 – 127.59 MbChr 6: 28.42 – 28.43 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.[5][6]

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.[6]

Interactions

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ARF5 has been shown to interact with ARFIP2.[7][8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000004059Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020440Ensembl, 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. ^ Tsuchiya M, Price SR, Tsai SC, Moss J, Vaughan M (March 1991). "Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells". J Biol Chem. 266 (5): 2772–7. doi:10.1016/S0021-9258(18)49913-9. PMID 1993656.
  6. ^ a b "Entrez Gene: ARF5 ADP-ribosylation factor 5".
  7. ^ 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. 272 (9). UNITED STATES: 5421–9. doi:10.1074/jbc.272.9.5421. ISSN 0021-9258. PMID 9038142.
  8. ^ Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. 285 (5). United States: 1267–73. doi:10.1006/bbrc.2001.5330. ISSN 0006-291X. PMID 11478794.
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Further reading

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