ARR3 arrestin 3 [Bos taurus (domestic cattle)] - Gene

Summary

Official Symbol: ARR3provided by VGNC
Official Full Name: arrestin 3provided by VGNC
Primary source: VGNC:VGNC:26168
See related: BGD:BT20864; Ensembl:ENSBTAG00000012856
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Orthologs: human mouse all
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Genomic context

Location:: chromosome: X

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2024_12	current	ARS-UCD2.0 (GCF_002263795.3)	X	NC_037357.1 (80162283..80175186, complement)

Chromosome X - NC_037357.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:: NC_037357.1 Chromosome X Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Dominette sequence data
BioProject: PRJNA294306
Analysis date: Tue Dec 17 08:57:05 2024

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Inositol hexakisphosphate (IP6) binds to the arrestin-3 phosphate sensor, and is stabilized by trimerization. Analysis of the trimerization surface, which is also the receptor-binding surface, suggests a feature called the finger loop as a key region of the activation sensor.
Title: Structural basis of arrestin-3 activation and signaling.
Several mutations in the two parts of the central "crest" of the arrestin molecule, middle-loop and C-loop, enhanced or reduced arrestin-3 interactions with several GPCRs in receptor subtype and functional state-specific manner.
Title: Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors.
K2A mutations in arrestin-1, -2, and -3 significantly reduced their binding to active phosphorhodopsin.
Title: Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.
multiple residues on the non-receptor-binding side of arrestin-3 are crucial for JNK3 activation
Title: Identification of arrestin-3-specific residues necessary for JNK3 kinase activation.
Both nonvisual arrestin-2 and arrestin-3 are shown to directly bind Jun kinase (JNK)3alpha2 and its upstream activator Map kinase kinase (MKK)4; the affinity of arrestin-3 for these kinases is higher than that of arrestin-2.
Title: Nonvisual arrestins function as simple scaffolds assembling the MKK4-JNK3α2 signaling complex.
the first crystal structure of arrestin-3, solved at 3.0 A resolution. Receptor binding.
Title: Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes.
SUMOylation sites in arrestin-3; arrestin-3 SUMOylation mediates beta(2)AR internalization
Title: Small ubiquitin-like modifier modification of arrestin-3 regulates receptor trafficking.
The nature of the changes in arrestin 3 distribution observed upon activation of adenosine receptors correlates with receptor sensitivity to G-protein-coupled receptor kinase-mediated phosphorylation and rapid internalization.
Title: Subtype-specific regulation of receptor internalization and recycling by the carboxyl-terminal domains of the human A1 and rat A3 adenosine receptors: consequences for agonist-stimulated translocation of arrestin3.
microtubule interaction may play a role in keeping p44 arrestin away from rhodopsin in dark-adapted photoreceptors
Title: Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors.

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General gene information

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Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables G protein-coupled receptor binding	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in G protein-coupled receptor internalization	IEA Inferred from Electronic Annotation more info	PubMed
involved_in signal transduction	IEA Inferred from Electronic Annotation more info	PubMed
involved_in visual perception	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: arrestin-C

Names: X-arrestin; cArr; cone arrestin; retinal cone arrestin-3

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.