// Workers AI · dad joke modeIs ARF4 a dog gene? Because it's paws-4.

ARF4
Identifiers
Aliases	ARF4, ARF2, ADP ribosylation factor 4
External IDs	OMIM: 601177; MGI: 99433; GeneCards: ARF4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Z6X
Gene location (Human) Chr. Chromosome 3 (human) Band 3p14.3 Start 57,571,363 bp End 57,598,220 bp
Gene location (Mouse) Chr. Chromosome 14 (mouse) Band 14 A3|14 16.09 cM Start 26,359,229 bp End 26,386,239 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibia parietal pleura visceral pleura germinal epithelium corpus epididymis mucosa of sigmoid colon pancreatic epithelial cell parotid gland epithelium of nasopharynx stromal cell of endometrium Top expressed in genital tubercle tail of embryo ventricular zone right kidney esophagus embryo embryo lip yolk sac dentate gyrus of hippocampal formation granule cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding epidermal growth factor receptor binding GTP binding protein binding GTPase activity Cellular component cytosol Golgi apparatus membrane dendritic spine intracellular anatomical structure ruffle membrane extracellular exosome extracellular matrix cytoplasm plasma membrane glutamatergic synapse Biological process protein ADP-ribosylation small GTPase mediated signal transduction negative regulation of apoptotic process regulation of reactive oxygen species metabolic process endoplasmic reticulum to Golgi vesicle-mediated transport activation of phospholipase D activity protein transport cell migration vesicle-mediated transport positive regulation of transcription by RNA polymerase II retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum transport dendritic spine development intracellular protein transport Golgi to plasma membrane transport epidermal growth factor receptor signaling pathway brain development learning apical protein localization establishment or maintenance of epithelial cell apical/basal polarity response to axon injury regulation of synapse organization protein localization to cilium regulation of postsynapse organization Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 378 11843 Ensembl ENSG00000168374 ENSMUSG00000021877 UniProt P18085 P61750 RefSeq (mRNA) NM_001660 NM_007479 RefSeq (protein) NP_001651 NP_031505 Location (UCSC) Chr 3: 57.57 – 57.6 Mb Chr 14: 26.36 – 26.39 Mb PubMed search
Wikidata
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ADP-ribosylation factor 4 is a protein that in humans is encoded by the ARF4 gene.

Gene

ADP-ribosylation factor 4 (ARF4) is a member of the human ARF gene family.

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, this gene 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.

Function

These genes encode small Guanine-nucleotide binding proteins (G proteins) that play a role in vesicular trafficking and as activators of phospholipase D.

Clinical significance

ARF4 stimulates the ADP-ribosyltransferase activity of cholera toxin.

Interactions

ARF4 has been shown to interact with Epidermal growth factor receptor and with RVxP motifs.

Further reading

• Lee FJ, Moss J, Vaughan M (1992). "Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae". The Journal of Biological Chemistry. 267 (34): 24441–24445. doi:10.1016/S0021-9258(18)35786-7. PMID 1447192.
• Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C (1991). "Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins". The Journal of Biological Chemistry. 266 (4): 2606–2614. doi:10.1016/S0021-9258(18)52288-2. PMID 1899243.
• Stearns T, Willingham MC, Botstein D, Kahn RA (1990). "ADP-ribosylation factor is functionally and physically associated with the Golgi complex". Proceedings of the National Academy of Sciences of the United States of America. 87 (3): 1238–1242. Bibcode:1990PNAS...87.1238S. doi:10.1073/pnas.87.3.1238. PMC 53446. PMID 2105501.
• Vorobieva N, Protopopov A, Protopopova M, Kashuba V, Allikmets RL, Modi W, et al. (1995). "Localization of human ARF2 and NCK genes and 13 other NotI-linking clones to chromosome 3 by fluorescence in situ hybridization". Cytogenetics and Cell Genetics. 68 (1–2): 91–94. doi:10.1159/000133898. PMID 7956370.
• 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): 732–734. 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". The Journal of Cell Biology. 121 (4): 751–760. doi:10.1083/jcb.121.4.751. PMC 2119793. PMID 8491770.
• Pardinas J, Pang Z, Houghton J, Palejwala V, Donnelly RJ, Hubbard K, et al. (1997). "Differential gene expression in SV40-mediated immortalization of human fibroblasts". Journal of Cellular Physiology. 171 (3): 325–335. doi:10.1002/(SICI)1097-4652(199706)171:3<325::AID-JCP11>3.0.CO;2-9. PMID 9180902. S2CID 3026138.
• Kim HS (1998). "Human ADP-ribosylation factor 4 (ARF4) gene. Map position 3p14.1". Chromosome Research. 6 (8): 663. doi:10.1023/A:1009230216005. PMID 10099884. S2CID 31829743.
• Lebeda RA, Haun RS (1999). "Cloning and characterization of the human ADP-ribosylation factor 4 gene". Gene. 237 (1): 209–214. doi:10.1016/S0378-1119(99)00290-5. PMID 10524252.
• Shin OH, Ross AH, Mihai I, Exton JH (1999). "Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors". The Journal of Biological Chemistry. 274 (51): 36609–36615. doi:10.1074/jbc.274.51.36609. PMID 10593962.
• Nevrivy DJ, Peterson VJ, Avram D, Ishmael JE, Hansen SG, Dowell P, 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". The Journal of Biological Chemistry. 275 (22): 16827–16836. doi:10.1074/jbc.275.22.16827. PMID 10828067.
• Prekeris R, Davies JM, Scheller RH (2001). "Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins". The Journal of Biological Chemistry. 276 (42): 38966–38970. doi:10.1074/jbc.M106133200. PMID 11481332.
• Katayama T, Imaizumi K, Yoneda T, Taniguchi M, Honda A, Manabe T, et al. (2004). "Role of ARF4L in recycling between endosomes and the plasma membrane". Cellular and Molecular Neurobiology. 24 (1): 137–147. doi:10.1023/B:CEMN.0000012719.12015.ec. PMC 11529921. PMID 15049518. S2CID 6273028.

External links

• Human ARF4 genome location and ARF4 gene details page in the UCSC Genome Browser.