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{{Infobox_gene}}
{{PBB_Controls
'''ADP-ribosylation factor 4''' is a [[protein]] that in humans is encoded by the ''ARF4'' [[gene]].<ref name="pmid2107548">{{cite journal | vauthors = Monaco L, Murtagh JJ, Newman KB, Tsai SC, Moss J, Vaughan M | title = Selective amplification of an mRNA and related pseudogene for a human ADP-ribosylation factor, a guanine nucleotide-dependent protein activator of cholera toxin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 6 | pages = 2206–10  | date = Apr 1990 | pmid = 2107548 | pmc = 53655 | doi = 10.1073/pnas.87.6.2206 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARF4 ADP-ribosylation factor 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=378| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_ARF4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z6x.
| PDB = {{PDB2|1z6x}}, {{PDB2|2b6h}}
| Name = ADP-ribosylation factor 4
| HGNCid = 655
| Symbol = ARF4
| AltSymbols =;
| OMIM = 601177
| ECnumber = 
| Homologene = 55593
| MGIid = 99433
| GeneAtlas_image1 = PBB_GE_ARF4_201097_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARF4_201096_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006888 |text = ER to Golgi vesicle-mediated transport}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 378
    | Hs_Ensembl = ENSG00000168374
    | Hs_RefseqProtein = XP_001132763
    | Hs_RefseqmRNA = XM_001132763
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 57532145
    | Hs_GenLoc_end = 57558175
    | Hs_Uniprot = P18085
    | Mm_EntrezGene = 11843
    | Mm_Ensembl = ENSMUSG00000021877
    | Mm_RefseqmRNA = NM_007479
    | Mm_RefseqProtein = NP_031505
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 25471381
    | Mm_GenLoc_end = 25490442
    | Mm_Uniprot = Q14BR4
  }}
}}
'''ADP-ribosylation factor 4''', also known as '''ARF4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARF4 ADP-ribosylation factor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=378| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
ADP-ribosylation factor 4 (ARF4) 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 5 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1 and ARF3), class II (ARF4 and ARF5) and class III (ARF6). The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains six exons and five introns. The ARF4 is the most divergent member of the human ARFs. Conflicting Map positions at 3p14 or 3p21 have been reported for this gene.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = ADP-ribosylation factor 4 (ARF4) 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 5 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1 and ARF3), class II (ARF4 and ARF5) and class III (ARF6). The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains six exons and five introns. The ARF4 is the most divergent member of the human ARFs. Conflicting Map positions at 3p14 or 3p21 have been reported for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ARF4 ADP-ribosylation factor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=378| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ARF4 has been shown to [[Protein-protein interaction|interact]] with [[Epidermal growth factor receptor]].<ref name=pmid12446727>{{cite journal | vauthors = Kim SW, Hayashi M, Lo JF, Yang Y, Yoo JS, Lee JD | title = ADP-ribosylation factor 4 small GTPase mediates epidermal growth factor receptor-dependent phospholipase D2 activation | journal = J. Biol. Chem. | volume = 278 | issue = 4 | pages = 2661–8  | date = Jan 2003 | pmid = 12446727 | doi = 10.1074/jbc.M205819200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lee FJ, Moss J, Vaughan M | title = Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae | journal = J. Biol. Chem. | volume = 267 | issue = 34 | pages = 24441–5 | year = 1992 | pmid = 1447192 | doi =  }}
| citations =
* {{cite journal | vauthors = Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C | title = Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins | journal = J. Biol. Chem. | volume = 266 | issue = 4 | pages = 2606–14 | year = 1991 | pmid = 1899243 | doi =  }}
*{{cite journal | author=Lee FJ, Moss J, Vaughan M |title=Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24441-5 |year= 1992 |pmid= 1447192 |doi=  }}
* {{cite journal | vauthors = Stearns T, Willingham MC, Botstein D, Kahn RA | title = ADP-ribosylation factor is functionally and physically associated with the Golgi complex | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 3 | pages = 1238–42 | year = 1990 | pmid = 2105501 | pmc = 53446 | doi = 10.1073/pnas.87.3.1238 }}
*{{cite journal | author=Kahn RA, Kern FG, Clark J, ''et al.'' |title=Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins. |journal=J. Biol. Chem. |volume=266 |issue= 4 |pages= 2606-14 |year= 1991 |pmid= 1899243 |doi=  }}
* {{cite journal | vauthors = Vorobieva N, Protopopov A, Protopopova M, Kashuba V, Allikmets RL, Modi W, Zabarovsky ER, Klein G, Kisselev L, Graphodatsky A | title = Localization of human ARF2 and NCK genes and 13 other NotI-linking clones to chromosome 3 by fluorescence in situ hybridization | journal = Cytogenet. Cell Genet. | volume = 68 | issue = 1-2 | pages = 91–4 | year = 1995 | pmid = 7956370 | doi = 10.1159/000133898 }}
*{{cite journal | author=Stearns T, Willingham MC, Botstein D, Kahn RA |title=ADP-ribosylation factor is functionally and physically associated with the Golgi complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 1238-42 |year= 1990 |pmid= 2105501 |doi= }}
* {{cite journal | vauthors = Orcl L, Palmer DJ, Amherdt M, Rothman JE | title = Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol | journal = Nature | volume = 364 | issue = 6439 | pages = 732–4 | year = 1993 | pmid = 8355790 | doi = 10.1038/364732a0 }}
*{{cite journal  | author=Monaco L, Murtagh JJ, Newman KB, ''et al.'' |title=Selective amplification of an mRNA and related pseudogene for a human ADP-ribosylation factor, a guanine nucleotide-dependent protein activator of cholera toxin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 6 |pages= 2206-10 |year= 1990 |pmid= 2107548 |doi=  }}
* {{cite journal | vauthors = Helms JB, Palmer DJ, Rothman JE | title = Two distinct populations of ARF bound to Golgi membranes | journal = J. Cell Biol. | volume = 121 | issue = 4 | pages = 751–60 | year = 1993 | pmid = 8491770 | pmc = 2119793 | doi = 10.1083/jcb.121.4.751 }}
*{{cite journal | author=Vorobieva N, Protopopov A, Protopopova M, ''et al.'' |title=Localization of human ARF2 and NCK genes and 13 other NotI-linking clones to chromosome 3 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 91-4 |year= 1994 |pmid= 7956370 |doi= }}
* {{cite journal | vauthors = Pardinas J, Pang Z, Houghton J, Palejwala V, Donnelly RJ, Hubbard K, Small MB, Ozer HL | title = Differential gene expression in SV40-mediated immortalization of human fibroblasts | journal = J. Cell. Physiol. | volume = 171 | issue = 3 | pages = 325–35 | year = 1997 | pmid = 9180902 | doi = 10.1002/(SICI)1097-4652(199706)171:3<325::AID-JCP11>3.0.CO;2-9 }}
*{{cite journal | author=Orcl L, Palmer DJ, Amherdt M, Rothman JE |title=Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. |journal=Nature |volume=364 |issue= 6439 |pages= 732-4 |year= 1993 |pmid= 8355790 |doi= 10.1038/364732a0 }}
* {{cite journal | vauthors = Kim HS | title = Human ADP-ribosylation factor 4 (ARF4) gene. Map position 3p14.1 | journal = Chromosome Res. | volume = 6 | issue = 8 | pages = 663 | year = 1998 | pmid = 10099884 | doi = 10.1023/A:1009230216005 }}
*{{cite journal | author=Helms JB, Palmer DJ, Rothman JE |title=Two distinct populations of ARF bound to Golgi membranes. |journal=J. Cell Biol. |volume=121 |issue= 4 |pages= 751-60 |year= 1993 |pmid= 8491770 |doi= }}
* {{cite journal | vauthors = Lebeda RA, Haun RS | title = Cloning and characterization of the human ADP-ribosylation factor 4 gene | journal = Gene | volume = 237 | issue = 1 | pages = 209–14 | year = 1999 | pmid = 10524252 | doi = 10.1016/S0378-1119(99)00290-5 }}
*{{cite journal | author=Pardinas J, Pang Z, Houghton J, ''et al.'' |title=Differential gene expression in SV40-mediated immortalization of human fibroblasts. |journal=J. Cell. Physiol. |volume=171 |issue= 3 |pages= 325-35 |year= 1997 |pmid= 9180902 |doi= 10.1002/(SICI)1097-4652(199706)171:3<325::AID-JCP11>3.0.CO;2-9 }}
* {{cite journal | vauthors = Shin OH, Ross AH, Mihai I, Exton JH | title = Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors | journal = J. Biol. Chem. | volume = 274 | issue = 51 | pages = 36609–15 | year = 1999 | pmid = 10593962 | doi = 10.1074/jbc.274.51.36609 }}
*{{cite journal | author=Kim HS |title=Human ADP-ribosylation factor 4 (ARF4) gene. Map position 3p14.1. |journal=Chromosome Res. |volume=6 |issue= 8 |pages= 663 |year= 1999 |pmid= 10099884 |doi= }}
* {{cite journal | vauthors = Nevrivy DJ, Peterson VJ, Avram D, Ishmael JE, Hansen SG, Dowell P, Hruby DE, Dawson MI, Leid M | title = Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors | journal = J. Biol. Chem. | volume = 275 | issue = 22 | pages = 16827–36 | year = 2000 | pmid = 10828067 | doi = 10.1074/jbc.275.22.16827 }}
*{{cite journal | author=Lebeda RA, Haun RS |title=Cloning and characterization of the human ADP-ribosylation factor 4 gene. |journal=Gene |volume=237 |issue= 1 |pages= 209-14 |year= 1999 |pmid= 10524252 |doi= }}
* {{cite journal | vauthors = Prekeris R, Davies JM, Scheller RH | title = Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins | journal = J. Biol. Chem. | volume = 276 | issue = 42 | pages = 38966–70 | year = 2001 | pmid = 11481332 | doi = 10.1074/jbc.M106133200 }}
*{{cite journal | author=Shin OH, Ross AH, Mihai I, Exton JH |title=Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36609-15 |year= 2000 |pmid= 10593962 |doi= }}
* {{cite journal | vauthors = Kim SW, Hayashi M, Lo JF, Yang Y, Yoo JS, Lee JD | title = ADP-ribosylation factor 4 small GTPase mediates epidermal growth factor receptor-dependent phospholipase D2 activation | journal = J. Biol. Chem. | volume = 278 | issue = 4 | pages = 2661–8 | year = 2003 | pmid = 12446727 | doi = 10.1074/jbc.M205819200 }}
*{{cite journal | author=Nevrivy DJ, Peterson VJ, Avram D, ''et al.'' |title=Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16827-36 |year= 2000 |pmid= 10828067 |doi= }}
* {{cite journal | vauthors = Katayama T, Imaizumi K, Yoneda T, Taniguchi M, Honda A, Manabe T, Hitomi J, Oono K, Baba K, Miyata S, Matsuzaki S, Takatsuji K, Tohyama M | title = Role of ARF4L in recycling between endosomes and the plasma membrane | journal = Cell. Mol. Neurobiol. | volume = 24 | issue = 1 | pages = 137–47 | year = 2004 | pmid = 15049518 | doi = 10.1023/B:CEMN.0000012719.12015.ec }}
*{{cite journal | author=Prekeris R, Davies JM, Scheller RH |title=Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 38966-70 |year= 2001 |pmid= 11481332 |doi= 10.1074/jbc.M106133200 }}
*{{cite journal | author=Kim SW, Hayashi M, Lo JF, ''et al.'' |title=ADP-ribosylation factor 4 small GTPase mediates epidermal growth factor receptor-dependent phospholipase D2 activation. |journal=J. Biol. Chem. |volume=278 |issue= 4 |pages= 2661-8 |year= 2003 |pmid= 12446727 |doi= 10.1074/jbc.M205819200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Katayama T, Imaizumi K, Yoneda T, ''et al.'' |title=Role of ARF4L in recycling between endosomes and the plasma membrane. |journal=Cell. Mol. Neurobiol. |volume=24 |issue= 1 |pages= 137-47 |year= 2004 |pmid= 15049518 |doi= }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC gene info|ARF4}}
{{PDB Gallery|geneid=378}}
 
 
{{gene-3-stub}}

Latest revision as of 02:16, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

ADP-ribosylation factor 4 is a protein that in humans is encoded by the ARF4 gene.[1][2]

Function

ADP-ribosylation factor 4 (ARF4) 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 5 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1 and ARF3), class II (ARF4 and ARF5) and class III (ARF6). The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains six exons and five introns. The ARF4 is the most divergent member of the human ARFs. Conflicting Map positions at 3p14 or 3p21 have been reported for this gene.[2]

Interactions

ARF4 has been shown to interact with Epidermal growth factor receptor.[3]

References

  1. ↑ Monaco L, Murtagh JJ, Newman KB, Tsai SC, Moss J, Vaughan M (Apr 1990). "Selective amplification of an mRNA and related pseudogene for a human ADP-ribosylation factor, a guanine nucleotide-dependent protein activator of cholera toxin". Proc. Natl. Acad. Sci. U.S.A. 87 (6): 2206–10. doi:10.1073/pnas.87.6.2206. PMC 53655. PMID 2107548.
  2. ↑ 2.0 2.1 "Entrez Gene: ARF4 ADP-ribosylation factor 4".
  3. ↑ Kim SW, Hayashi M, Lo JF, Yang Y, Yoo JS, Lee JD (Jan 2003). "ADP-ribosylation factor 4 small GTPase mediates epidermal growth factor receptor-dependent phospholipase D2 activation". J. Biol. Chem. 278 (4): 2661–8. doi:10.1074/jbc.M205819200. PMID 12446727.

Further reading

External links


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