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]
^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.
^Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. United States. 285 (5): 1267–73. doi:10.1006/bbrc.2001.5330. ISSN 0006-291X. PMID 11478794.
External linksEdit
Human ARF5 genome location and ARF5 gene details page in the UCSC Genome Browser.
Further readingEdit
Lee FJ, Moss J, Vaughan M (1992). "Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae". J. Biol. Chem. 267 (34): 24441–5. doi:10.1016/S0021-9258(18)35786-7. PMID 1447192.
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. Bibcode:1990PNAS...87.1238S. doi:10.1073/pnas.87.3.1238. PMC53446. PMID 2105501.
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol". Nature. 364 (6439): 732–4. Bibcode:1993Natur.364..732O. doi:10.1038/364732a0. PMID 8355790. S2CID 4348442.
Helms JB, Palmer DJ, Rothman JE (1993). "Two distinct populations of ARF bound to Golgi membranes". J. Cell Biol. 121 (4): 751–60. doi:10.1083/jcb.121.4.751. PMC2119793. PMID 8491770.
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. doi:10.1074/jbc.272.9.5421. PMID 9038142.
McGuire RE, Daiger SP, Green ED (1997). "Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene". Genomics. 41 (3): 481–4. doi:10.1006/geno.1997.4689. PMID 9169151.
Andreev J, Simon JP, Sabatini DD, et al. (1999). "Identification of a New Pyk2 Target Protein with Arf-GAP Activity". Mol. Cell. Biol. 19 (3): 2338–50. doi:10.1128/MCB.19.3.2338. PMC84026. PMID 10022920.
Honda A, Nogami M, Yokozeki T, et al. (1999). "Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation". Cell. 99 (5): 521–32. doi:10.1016/S0092-8674(00)81540-8. PMID 10589680. S2CID 10031591.
Shin OH, Ross AH, Mihai I, Exton JH (2000). "Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors". J. Biol. Chem. 274 (51): 36609–15. doi:10.1074/jbc.274.51.36609. PMID 10593962.
Kondo A, Hashimoto S, Yano H, et al. (2000). "A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein Activity, Is Involved in Paxillin Recruitment to Focal Adhesions and Cell Migration". Mol. Biol. Cell. 11 (4): 1315–27. doi:10.1091/mbc.11.4.1315. PMC14849. PMID 10749932.
Nevrivy DJ, Peterson VJ, Avram D, et al. (2000). "Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors". J. Biol. Chem. 275 (22): 16827–36. doi:10.1074/jbc.275.22.16827. PMID 10828067.
Shin OH, Couvillon AD, Exton JH (2001). "Arfophilin is a common target of both class II and class III ADP-ribosylation factors". Biochemistry. 40 (36): 10846–52. doi:10.1021/bi0107391. PMID 11535061.
Austin C, Boehm M, Tooze SA (2002). "Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry. 41 (14): 4669–77. doi:10.1021/bi016064j. PMID 11926829.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science. 300 (5620): 767–72. Bibcode:2003Sci...300..767S. doi:10.1126/science.1083423. PMC2882961. PMID 12690205.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.
arf5, ribosylation, factor, protein, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes2b6hidentifiersaliases, ribosylation, factor, 5external, idsomim, 103188, 99434, homologene, 129625, genecards, gene, location, hum. ADP ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene 5 6 ARF5Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes2B6HIdentifiersAliasesARF5 ADP ribosylation factor 5External IDsOMIM 103188 MGI 99434 HomoloGene 129625 GeneCards ARF5Gene location Human Chr Chromosome 7 human 1 Band7q32 1Start127 588 386 bp 1 End127 591 700 bp 1 Gene location Mouse Chr Chromosome 6 mouse 2 Band6 6 A3 3Start28 423 559 bp 2 End28 426 601 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inprefrontal cortexBrodmann area 9skin of abdomenbody of pancreassuperior frontal gyrusnucleus accumbensputamenmonocytecaudate nucleusright uterine tubeTop expressed inlipsuperior frontal gyrusyolk sacentorhinal cortexspermatocyteduodenumthymusstomachesophagusintestinal villusMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionnucleotide binding GTP binding protein binding GTPase activityCellular componentcytoplasm perinuclear region of cytoplasm plasma membrane Golgi apparatus extracellular exosome intracellular anatomical structure membraneBiological processprotein transport small GTPase mediated signal transduction vesicle mediated transport retrograde vesicle mediated transport Golgi to endoplasmic reticulum transport intracellular protein transport Golgi to plasma membrane transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez38111844EnsemblENSG00000004059ENSMUSG00000020440UniProtP84085P84084RefSeq mRNA NM 001662NM 007480RefSeq protein NP 001653NP 031506Location UCSC Chr 7 127 59 127 59 MbChr 6 28 42 28 43 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseADP 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 Contents 1 Interactions 2 References 3 External links 4 Further readingInteractions EditARF5 has been shown to interact with ARFIP2 7 8 References Edit a b c GRCh38 Ensembl release 89 ENSG00000004059 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000020440 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 a b Entrez Gene ARF5 ADP ribosylation factor 5 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 Shin O H Exton J H August 2001 Differential binding of arfaptin 2 POR1 to ADP ribosylation factors and Rac1 Biochem Biophys Res Commun United States 285 5 1267 73 doi 10 1006 bbrc 2001 5330 ISSN 0006 291X PMID 11478794 External links EditHuman ARF5 genome location and ARF5 gene details page in the UCSC Genome Browser Further reading EditLee FJ Moss J Vaughan M 1992 Human and Giardia ADP ribosylation factors ARFs complement ARF function in Saccharomyces cerevisiae J Biol Chem 267 34 24441 5 doi 10 1016 S0021 9258 18 35786 7 PMID 1447192 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 Bibcode 1990PNAS 87 1238S doi 10 1073 pnas 87 3 1238 PMC 53446 PMID 2105501 Orcl L Palmer DJ Amherdt M Rothman JE 1993 Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol Nature 364 6439 732 4 Bibcode 1993Natur 364 732O doi 10 1038 364732a0 PMID 8355790 S2CID 4348442 Helms JB Palmer DJ Rothman JE 1993 Two distinct populations of ARF bound to Golgi membranes J Cell Biol 121 4 751 60 doi 10 1083 jcb 121 4 751 PMC 2119793 PMID 8491770 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 doi 10 1074 jbc 272 9 5421 PMID 9038142 McGuire RE Daiger SP Green ED 1997 Localization and characterization of the human ADP ribosylation factor 5 ARF5 gene Genomics 41 3 481 4 doi 10 1006 geno 1997 4689 PMID 9169151 Andreev J Simon JP Sabatini DD et al 1999 Identification of a New Pyk2 Target Protein with Arf GAP Activity Mol Cell Biol 19 3 2338 50 doi 10 1128 MCB 19 3 2338 PMC 84026 PMID 10022920 Honda A Nogami M Yokozeki T et al 1999 Phosphatidylinositol 4 phosphate 5 kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation Cell 99 5 521 32 doi 10 1016 S0092 8674 00 81540 8 PMID 10589680 S2CID 10031591 Shin OH Ross AH Mihai I Exton JH 2000 Identification of arfophilin a target protein for GTP bound class II ADP ribosylation factors J Biol Chem 274 51 36609 15 doi 10 1074 jbc 274 51 36609 PMID 10593962 Kondo A Hashimoto S Yano H et al 2000 A New Paxillin binding Protein PAG3 Papa KIAA0400 Bearing an ADP Ribosylation Factor GTPase activating Protein Activity Is Involved in Paxillin Recruitment to Focal Adhesions and Cell Migration Mol Biol Cell 11 4 1315 27 doi 10 1091 mbc 11 4 1315 PMC 14849 PMID 10749932 Nevrivy DJ Peterson VJ Avram D et al 2000 Interaction of GRASP a protein encoded by a novel retinoic acid induced gene with members of the cytohesin family of guanine nucleotide exchange factors J Biol Chem 275 22 16827 36 doi 10 1074 jbc 275 22 16827 PMID 10828067 Shin OH Couvillon AD Exton JH 2001 Arfophilin is a common target of both class II and class III ADP ribosylation factors Biochemistry 40 36 10846 52 doi 10 1021 bi0107391 PMID 11535061 Austin C Boehm M Tooze SA 2002 Site specific cross linking reveals a differential direct interaction of class 1 2 and 3 ADP ribosylation factors with adaptor protein complexes 1 and 3 Biochemistry 41 14 4669 77 doi 10 1021 bi016064j PMID 11926829 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Scherer SW Cheung J MacDonald JR et al 2003 Human Chromosome 7 DNA Sequence and Biology Science 300 5620 767 72 Bibcode 2003Sci 300 767S doi 10 1126 science 1083423 PMC 2882961 PMID 12690205 Gerhard DS Wagner L Feingold EA et al 2004 The Status Quality and Expansion of the NIH Full Length cDNA Project The Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Rual JF Venkatesan K Hao T et al 2005 Towards a proteome scale map of the human protein protein interaction network Nature 437 7062 1173 8 Bibcode 2005Natur 437 1173R doi 10 1038 nature04209 PMID 16189514 S2CID 4427026 This article on a gene on human chromosome 7 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title ARF5 amp oldid 1079573567, wikipedia, wiki, book, books, library,
