[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Brain; PubMed=1517224 [NCBI, ExPASy, EBI, Israel, Japan] Attramadal H., Arriza J.L., Aoki C., Dawson T.M., Codina J., Kwatra M.M., Snyder S.H., Caron M.G., Lefkowitz R.J.; "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family."; J. Biol. Chem. 267:17882-17890(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 295-410. TISSUE=Pineal gland; PubMed=8308033 [NCBI, ExPASy, EBI, Israel, Japan] Craft C.M., Whitmore D.H., Wiechmann A.F.; "Cone arrestin identified by targeting expression of a functional family."; J. Biol. Chem. 269:4613-4619(1994).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-386. STRAIN=Sprague-Dawley; TISSUE=Retina; DOI=10.1046/j.1460-9568.1998.00271.x; PubMed=9767391 [NCBI, ExPASy, EBI, Israel, Japan] Komori N., Cain S.D., Roch J.-M., Miller K.E., Matsumoto H.; "Differential expression of alternative splice variants of beta-arrestin-1 and -2 in rat central nervous system and peripheral tissues."; Eur. J. Neurosci. 10:2607-2616(1998).

Comments

FUNCTION: Regulates beta-adrenergic receptor function. Beta-arrestins seem to bind phosphorylated beta-adrenergic receptors, thereby causing a significant impairment of their capacity to activate G(S) proteins.
INTERACTION:
P31749:AKT1 (xeno); NbExp=2; IntAct=EBI-1636616, EBI-296087;
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity).
TISSUE SPECIFICITY: Predominantly localized in neuronal tissues and in the spleen.
SIMILARITY: Belongs to the arrestin family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M91590; AAA74460.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC087578; AAH87578.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03627; AAA17551.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF051457; AAC28617.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A59279; A59279.

NP_037043.1; -.

3D structure databases

HSSP

P17870; 1G4M. [HSSP ENTRY / PDB]

ModBase

P29067.

Protein-protein interaction databases

IntAct

P29067; -.

PTM databases

PhosphoSite

P29067; -.

Organism-specific databases

RGD

2157; Arrb2.

Gene expression databases

GermOnline

ENSRNOG00000019308; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0050896;	Biological process: response to stimulus (inferred from electronic annotation from UniProtKB-KW).
GO:0007600;	Biological process: sensory perception (inferred from electronic annotation from InterPro).
GO:0007165;	Biological process: signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000698; Arrestin.
IPR011022; Arrestin-like_C.
IPR011021; Arrestin-like_N.
IPR014752; Arrestin_C.
IPR014753; Arrestin_N.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.640; Arrestin_C; 1.
G3DSA:2.60.40.840; Arrestin_N; 1.

PANTHER

PTHR11792; Arrestin; 1.

Pfam

PF02752; Arrestin_C; 1.
PF00339; Arrestin_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00309; ARRESTIN.

ProDom

PD002099; Arrestin; 2.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00295; ARRESTINS; 1.

Genome annotation databases

Ensembl

ENSRNOG00000019308; Rattus norvegicus. [Contig view]

GeneID

25388; -.

KEGG

rno:25388; -.

Phylogenomic databases

HOVERGEN

P29067; -.

Other

NextBio

606447; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Nucleus; Phosphoprotein; Sensory transduction.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 410`	`410`	`Beta-arrestin-2.`	`PRO_0000205201`
`MOTIF`	`390 400`	`11`	`Nuclear export signal (By similarity).`
`MOD_RES`	`48 48`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 410 AA [This is the length of the unprocessed precursor]

Molecular weight: 46340 Da [This is the MW of the unprocessed precursor]

CRC64: 0DFA6A897C2B86BA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGEKPGTRVF KKSSPNCKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK DRKVFVTLTC 

        70         80         90        100        110        120 
AFRYGREDLD VLGLSFRKDL FIATYQAFPP MPNPPRPPTR LQDRLLKKLG QHAHPFFFTI 

       130        140        150        160        170        180 
PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF CAKSIEEKSH KRNSVRLIIR KVQFAPETPG 

       190        200        210        220        230        240 
PQPSAETTRH FLMSDRRSLH LEASLDKELY YHGEPLNVNV HVTNNSAKTV KKIRVSVRQY 

       250        260        270        280        290        300 
ADICLFSTAQ YKCPVAQLEQ DDQVSPSSTF CKVYTITPLL SDNREKRGLA LDGQLKHEDT 

       310        320        330        340        350        360 
NLASSTIVKE GANKEVLGIL VSYRVKVKLV VSRGGDVSVE LPFVLMHPKP HDHITLPRPQ 

       370        380        390        400        410 
SAPREIDIPV DTNLIEFDTN YATDDDIVFE DFARLRLKGM KDDDCDDQFC

P29067 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools