ARR3

Today, we want to address the topic of ARR3, an aspect that has gained relevance in recent times and that arouses the interest of a wide spectrum of the public. From its origins to its impact on modern society, ARR3 has been the subject of debate, reflection and study. Throughout history, ARR3 has influenced various areas of life, from politics to culture, and its relevance has continued to grow. In this article, we will explore the different facets of ARR3, examining its evolution over time and its impact today. We hope that this analysis provides a broader and enriching view on ARR3, offering our readers a deeper understanding of this topic of universal interest.

Protein-coding gene in humans

ARR3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1XEH, 2A34
Identifiers
Aliases	ARR3, ARRX, cArr, arrestin 3 retinal (X-arrestin), arrestin 3, MYP26
External IDs	OMIM: 301770; MGI: 2159617; HomoloGene: 3182; GeneCards: ARR3; OMA:ARR3 - orthologs
Gene location (Human) Chr. X chromosome (human)[1] Band Xq13.1 Start 70,268,305 bp[1] End 70,281,840 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X|X C3 Start 99,649,103 bp[2] End 99,662,099 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle retina retinal pigment epithelium sural nerve stromal cell of endometrium rectum mononuclear cell monocyte skin of abdomen skin of leg Top expressed in neural layer of retina epithelium of lens morula retinal pigment epithelium embryo blastocyst primary visual cortex zygote superior frontal gyrus outer nuclear layer More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphoprotein binding opsin binding protein binding G protein-coupled receptor binding Cellular component photoreceptor inner segment cytoplasm photoreceptor outer segment synapse Biological process regulation of protein phosphorylation endocytosis signal transduction visual perception response to stimulus G protein-coupled receptor internalization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 407 170735 Ensembl ENSG00000120500 ENSMUSG00000060890 UniProt P36575 Q9EQP6 RefSeq (mRNA) NM_004312 NM_133205 RefSeq (protein) NP_004303 NP_573468 Location (UCSC) Chr X: 70.27 – 70.28 Mb Chr X: 99.65 – 99.66 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Arrestin-C, also known as retinal cone arrestin-3, is a protein that in humans is encoded by the ARR3 gene.^[5][6]

See also

• Arrestin

References

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000120500 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000060890 – Ensembl, 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. ^ Murakami A, Yajima T, Sakuma H, McLaren MJ, Inana G (Dec 1993). "X-arrestin: a new retinal arrestin mapping to the X chromosome". FEBS Lett. 334 (2): 203–9. doi:10.1016/0014-5793(93)81712-9. PMID 8224247.
6. ^ "Entrez Gene: ARR3 arrestin 3, retinal (X-arrestin)".

Further reading

• Craft CM, Whitmore DH, Wiechmann AF (1994). "Cone arrestin identified by targeting expression of a functional family". J. Biol. Chem. 269 (6): 4613–9. doi:10.1016/S0021-9258(17)41820-5. PMID 8308033.
• Sakuma H, Inana G, Murakami A, et al. (1996). "Immunolocalization of X-arrestin in human cone photoreceptors". FEBS Lett. 382 (1–2): 105–10. doi:10.1016/0014-5793(96)00163-9. PMID 8612728.
• ter Haar E, Musacchio A, Harrison SC, Kirchhausen T (1998). "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker". Cell. 95 (4): 563–73. doi:10.1016/S0092-8674(00)81623-2. PMC 4428171. PMID 9827808.
• Orsini MJ, Benovic JL (1999). "Characterization of dominant negative arrestins that inhibit beta2-adrenergic receptor internalization by distinct mechanisms". J. Biol. Chem. 273 (51): 34616–22. doi:10.1074/jbc.273.51.34616. PMID 9852134.
• Sakuma H, Murakami A, Fujimaki T, Inana G (1999). "Isolation and characterization of the human X-arrestin gene". Gene. 224 (1–2): 87–95. doi:10.1016/S0378-1119(98)00510-1. PMID 9931451.
• John SK, Smith JE, Aguirre GD, Milam AH (2000). "Loss of cone molecular markers in rhodopsin-mutant human retinas with retinitis pigmentosa". Mol. Vis. 6: 204–15. PMID 11063754.
• Chen Z, Dupré DJ, Le Gouill C, et al. (2002). "Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif". J. Biol. Chem. 277 (9): 7356–62. doi:10.1074/jbc.M110058200. PMID 11729201.
• Kim YM, Barak LS, Caron MG, Benovic JL (2002). "Regulation of arrestin-3 phosphorylation by casein kinase II". J. Biol. Chem. 277 (19): 16837–46. doi:10.1074/jbc.M201379200. PMID 11877451.
• 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.
• Zhu X, Li A, Brown B, et al. (2002). "Mouse cone arrestin expression pattern: light induced translocation in cone photoreceptors". Mol. Vis. 8: 462–71. PMID 12486395.
• Zhang H, Cuenca N, Ivanova T, et al. (2003). "Identification and light-dependent translocation of a cone-specific antigen, cone arrestin, recognized by monoclonal antibody 7G6". Invest. Ophthalmol. Vis. Sci. 44 (7): 2858–67. doi:10.1167/iovs.03-0072. hdl:10045/13046. PMID 12824223.
• Krishnamurthy H, Galet C, Ascoli M (2004). "The association of arrestin-3 with the follitropin receptor depends on receptor activation and phosphorylation". Mol. Cell. Endocrinol. 204 (1–2): 127–40. doi:10.1016/S0303-7207(03)00088-1. PMID 12850288. S2CID 25222855.
• Zhu X, Brown B, Li A, et al. (2003). "GRK1-dependent phosphorylation of S and M opsins and their binding to cone arrestin during cone phototransduction in the mouse retina". J. Neurosci. 23 (14): 6152–60. doi:10.1523/JNEUROSCI.23-14-06152.2003. PMC 6740345. PMID 12853434.
• Ermakova NA, Alekberova ZS, Prokaeva TB (2004). "Autoimmunity to S-Antigen and Retinal Vasculitis in Patients with Behçet's Disease". Adamantiades-Behçet's Disease. Advances in Experimental Medicine and Biology. Vol. 528. pp. 279–81. doi:10.1007/0-306-48382-3_56. ISBN 978-0-306-47757-7. PMID 12918707.
• 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.
• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. Bibcode:2005Natur.434..325R. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
• 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.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links

• Human ARR3 genome location and ARR3 gene details page in the UCSC Genome Browser.

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