ARR3

Arrestin 3, retinal (X-arrestin)

Rendering based on PDB 1XEH.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1XEH, 2A34

Identifiers

Symbols

ARR3 ; ARRX

External IDs

OMIM: 301770 MGI: 2159617 HomoloGene: 3182 GeneCards: ARR3 Gene

Gene ontology
Molecular function	• opsin binding • protein binding • phosphoprotein binding
Cellular component	• photoreceptor outer segment • photoreceptor inner segment • cytoplasm • synapse
Biological process	• regulation of protein phosphorylation • endocytosis • signal transduction • visual perception
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
69.49 – 69.5 Mb

Chr X:
100.61 – 100.62 Mb

PubMed search

Arrestin-C also known as retinal cone arrestin-3 is a protein that in humans is encoded by the ARR3 gene.^[1]^[2]

References

↑ 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.
↑ "Entrez Gene: ARR3 arrestin 3, retinal (X-arrestin)".

Craft CM, Whitmore DH, Wiechmann AF (1994). "Cone arrestin identified by targeting expression of a functional family.". J. Biol. Chem. 269 (6): 4613–9. 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. 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. 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. 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.
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. PMID 12853434.
Ermakova NA, Alekberova ZS, Prokaeva TB (2003). "Autoimmunity to S-antigen and retinal vasculitis in patients with Behçet's disease.". Adv. Exp. Med. Biol. 528: 279–81. doi:10.1007/0-306-48382-3_56. 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. 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. doi:10.1038/nature04209. PMID 16189514.
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.

Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)

Arrestin

Membrane-spanning 4A

MS4A1
MS4A2
MS4A3
MS4A4A
MS4A4E
MS4A5
MS4A6A
MS4A6E
MS4A7
MS4A8B
MS4A9
MS4A10
MS4A12
MS4A13
MS4A14
MS4A15
MS4A18

Myelin

Pulmonary surfactant

Tetraspanin

TSPAN1
TSPAN2
TSPAN3
TSPAN4
TSPAN5
TSPAN6
TSPAN7
TSPAN8
TSPAN9
TSPAN10
TSPAN11
TSPAN12
TSPAN13
TSPAN14
TSPAN15
TSPAN16
TSPAN17
TSPAN18
TSPAN19
TSPAN20
TSPAN21
TSPAN22
TSPAN23
TSPAN24
TSPAN25
TSPAN26
TSPAN27
TSPAN28
TSPAN29
TSPAN30
TSPAN31
TSPAN32
TSPAN33
TSPAN34

Other/ungrouped

see also other cell membrane protein disorders

Index of cells

Description	Structure nucleus chromosome genetics Organelles peroxisome cytoskeleton centrosome epithelia cilia mitochondria Membranes proteins cell adhesions Membrane transport ion channels vesicular transport solute carrier ABC transporters ATPase oxidoreduction-driven

Disease	Structural peroxisome cytoskeleton cilia mitochondria nucleus scleroprotein Membrane channelopathy solute carrier ATPase ABC transporters other extracellular ligands cell surface receptors intracellular signalling Vesicular transport Pore-forming toxins

ARR3

See also

References

Further reading