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Protein

Beta-2 adrenergic receptor

Gene

Adrb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei113Agonist or antagonistBy similarity1
Binding sitei118Agonist or antagonistBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-MMU-390696 Adrenoceptors
R-MMU-418555 G alpha (s) signalling events
R-MMU-5689880 Ub-specific processing proteases
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-2 adrenergic receptor
Alternative name(s):
Beta-2 adrenoreceptor
Short name:
Beta-2 adrenoceptor
Gene namesi
Name:Adrb2
Synonyms:Adrb2r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:87938 Adrb2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 34ExtracellularBy similarityAdd BLAST34
Transmembranei35 – 58Helical; Name=1By similarityAdd BLAST24
Topological domaini59 – 71CytoplasmicBy similarityAdd BLAST13
Transmembranei72 – 95Helical; Name=2By similarityAdd BLAST24
Topological domaini96 – 106ExtracellularBy similarityAdd BLAST11
Transmembranei107 – 129Helical; Name=3By similarityAdd BLAST23
Topological domaini130 – 150CytoplasmicBy similarityAdd BLAST21
Transmembranei151 – 174Helical; Name=4By similarityAdd BLAST24
Topological domaini175 – 196ExtracellularBy similarityAdd BLAST22
Transmembranei197 – 220Helical; Name=5By similarityAdd BLAST24
Topological domaini221 – 274CytoplasmicBy similarityAdd BLAST54
Transmembranei275 – 298Helical; Name=6By similarityAdd BLAST24
Topological domaini299 – 305ExtracellularBy similarity7
Transmembranei306 – 329Helical; Name=7By similarityAdd BLAST24
Topological domaini330 – 418CytoplasmicBy similarityAdd BLAST89

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3707

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000691341 – 418Beta-2 adrenergic receptorAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi6N-linked (GlcNAc...) asparagineCurated1
Glycosylationi15N-linked (GlcNAc...) asparagineCurated1
Disulfide bondi106 ↔ 191PROSITE-ProRule annotation
Modified residuei141PhosphotyrosineBy similarity1
Disulfide bondi184 ↔ 190PROSITE-ProRule annotation
Modified residuei246PhosphoserineBy similarity1
Modified residuei261Phosphoserine; by PKASequence analysis1
Modified residuei262Phosphoserine; by PKASequence analysis1
Lipidationi341S-palmitoyl cysteineBy similarity1
Modified residuei345Phosphoserine; by PKABy similarity1
Modified residuei346Phosphoserine; by PKABy similarity1
Modified residuei355Phosphoserine; by BARKCurated1
Modified residuei356Phosphoserine; by BARKCurated1
Modified residuei3874-hydroxyprolineBy similarity1
Modified residuei4004-hydroxyprolineBy similarity1

Post-translational modificationi

Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (By similarity).By similarity
Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.
Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor.By similarity
Polyubiquitinated. Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation. Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and resensitization after prolonged agonist stimulation. USP20 and USP33 are constitutively associated and are dissociated immediately after agonist stimulation. Ubiquitination by the VHL-E3 ligase complex is oxygen-dependent (By similarity).By similarity
Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP18762
PRIDEiP18762

PTM databases

iPTMnetiP18762
PhosphoSitePlusiP18762
SwissPalmiP18762

Expressioni

Gene expression databases

BgeeiENSMUSG00000045730
CleanExiMM_ADRB2
GenevisibleiP18762 MM

Interactioni

Subunit structurei

Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC, USP20 and USP33. Interacts with VHL; the interaction, which is increased on hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation. Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating VHL-E3 ligase-mediated ubiquitination. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. Interacts with CNIH4. Interacts with ARRDC3.By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

CORUMiP18762
DIPiDIP-59568N
IntActiP18762, 9 interactors
MINTiP18762
STRINGi10090.ENSMUSP00000062256

Chemistry databases

BindingDBiP18762

Structurei

3D structure databases

ProteinModelPortaliP18762
SMRiP18762
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni193 – 207Agonist and antagonist bindingBy similarityAdd BLAST15
Regioni286 – 293Agonist and antagonist bindingBy similarity8
Regioni312 – 316Agonist and antagonist bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi415 – 418PDZ-binding4

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00890000139331
HOGENOMiHOG000239242
HOVERGENiHBG106962
InParanoidiP18762
KOiK04142
OMAiGRFHAQN
OrthoDBiEOG091G06VI
TreeFamiTF316350

Family and domain databases

CDDicd15957 7tmA_Beta2_AR, 1 hit
InterProiView protein in InterPro
IPR002233 ADR_fam
IPR000332 ADRB2_rcpt
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
PANTHERiPTHR24248:SF21 PTHR24248:SF21, 1 hit
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR01103 ADRENERGICR
PR00562 ADRENRGCB2AR
PR00237 GPCRRHODOPSN
SMARTiView protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

Sequencei

Sequence statusi: Complete.

P18762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPHGNDSDF LLAPNGSRAP DHDVTQERDE AWVVGMAILM SVIVLAIVFG
60 70 80 90 100
NVLVITAIAK FERLQTVTNY FIISLACADL VMGLAVVPFG ASHILMKMWN
110 120 130 140 150
FGNFWCEFWT SIDVLCVTAS IETLCVIAVD RYVAITSPFK YQSLLTKNKA
160 170 180 190 200
RVVILMVWIV SGLTSFLPIQ MHWYRATHKK AIDCYTEETC CDFFTNQAYA
210 220 230 240 250
IASSIVSFYV PLVVMVFVYS RVFQVAKRQL QKIDKSEGRF HAQNLSQVEQ
260 270 280 290 300
DGRSGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIRD
310 320 330 340 350
NLIPKEVYIL LNWLGYVNSA FNPLIYCRSP DFRIAFQELL CLRRSSSKTY
360 370 380 390 400
GNGYSSNSNG RTDYTGEPNT CQLGQEREQE LLCEDPPGME GFVNCQGTVP
410
SLSVDSQGRN CSTNDSPL
Length:418
Mass (Da):46,998
Last modified:July 27, 2011 - v2
Checksum:i51D1EC73D7619D58
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21D → H in CAA33664 (PubMed:2549959).Curated1
Sequence conflicti94 – 95IL → TS in CAA33664 (PubMed:2549959).Curated2
Sequence conflicti254S → T in CAA33664 (PubMed:2549959).Curated1
Sequence conflicti347 – 348SK → FE in CAA33664 (PubMed:2549959).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15643 Genomic DNA Translation: CAA33664.1
AK080241 mRNA Translation: BAC37856.1
CH466528 Genomic DNA Translation: EDL09746.1
BC032883 mRNA Translation: AAH32883.1
CCDSiCCDS29289.1
PIRiS00260
RefSeqiNP_031446.2, NM_007420.3
UniGeneiMm.5598

Genome annotation databases

EnsembliENSMUST00000053640; ENSMUSP00000062256; ENSMUSG00000045730
GeneIDi11555
KEGGimmu:11555
UCSCiuc008fcy.2 mouse

Similar proteinsi

Entry informationi

Entry nameiADRB2_MOUSE
AccessioniPrimary (citable) accession number: P18762
Secondary accession number(s): Q8BH38
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 27, 2011
Last modified: July 18, 2018
This is version 181 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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