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Protein

Beta-2 adrenergic receptor

Gene

Adrb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.By similarity

Sites

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

GO - Molecular functioni

  • B2 bradykinin receptor binding Source: RGD
  • beta2-adrenergic receptor activity Source: RGD
  • dopamine binding Source: RGD
  • drug binding Source: RGD
  • epinephrine binding Source: RGD
  • G-protein alpha-subunit binding Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • norepinephrine binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

  • adenylate cyclase-activating adrenergic receptor signaling pathway Source: GO_Central
  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: RGD
  • aging Source: RGD
  • associative learning Source: RGD
  • cellular response to hypoxia Source: RGD
  • diaphragm contraction Source: RGD
  • estrous cycle Source: RGD
  • excitatory postsynaptic potential Source: RGD
  • female pregnancy Source: RGD
  • G-protein coupled receptor signaling pathway Source: RGD
  • liver development Source: RGD
  • liver regeneration Source: RGD
  • negative regulation of angiogenesis Source: RGD
  • negative regulation of inflammatory response Source: RGD
  • negative regulation of ossification Source: RGD
  • negative regulation of platelet aggregation Source: RGD
  • negative regulation of smooth muscle contraction Source: GO_Central
  • negative regulation of urine volume Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of ATPase activity Source: RGD
  • positive regulation of autophagosome maturation Source: GO_Central
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of heart contraction Source: RGD
  • positive regulation of lipophagy Source: GO_Central
  • positive regulation of potassium ion transport Source: RGD
  • positive regulation of skeletal muscle tissue growth Source: RGD
  • positive regulation of sodium ion transport Source: RGD
  • positive regulation of the force of heart contraction by epinephrine Source: RGD
  • positive regulation of vasodilation Source: RGD
  • regulation of calcium ion transport Source: RGD
  • regulation of sensory perception of pain Source: RGD
  • response to dexamethasone Source: RGD
  • response to estrogen Source: RGD
  • response to hypoxia Source: RGD
  • response to monoamine Source: RGD
  • response to progesterone Source: RGD
  • response to testosterone Source: RGD
  • synaptic transmission, glutamatergic Source: RGD
  • vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure Source: RGD
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2060. Adrb2.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Early endosome By similarity

  • Note: Colocalizes with VHL on cell membranes. Activated receptors are internalized into endosomes prior to their degradation in lysosomes.By similarity

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

GO - Cellular componenti

  • axon Source: RGD
  • caveola Source: RGD
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • dendritic spine Source: RGD
  • early endosome Source: UniProtKB-SubCell
  • endosome Source: RGD
  • integral component of plasma membrane Source: GO_Central
  • intracellular membrane-bounded organelle Source: RGD
  • membrane Source: RGD
  • neuronal cell body membrane Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • sarcolemma Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3754.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000691361 – 418Beta-2 adrenergic receptorAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi6N-linked (GlcNAc...)Curated1
Glycosylationi15N-linked (GlcNAc...)Curated1
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

PaxDbiP10608.
PRIDEiP10608.

PTM databases

iPTMnetiP10608.
PhosphoSitePlusiP10608.

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

WithEntry#Exp.IntActNotes
Dlg4P310162EBI-7090342,EBI-375655
Gria1P194903EBI-7090342,EBI-371642

GO - Molecular functioni

  • B2 bradykinin receptor binding Source: RGD
  • G-protein alpha-subunit binding Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

IntActiP10608. 5 interactors.
STRINGi10116.ENSRNOP00000026098.

Chemistry databases

BindingDBiP10608.

Structurei

3D structure databases

ProteinModelPortaliP10608.
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.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP10608.
PhylomeDBiP10608.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR000332. ADRB2_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24248:SF21. PTHR24248:SF21. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10608-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPHGNDSDF LLAPNGSRAP GHDITQERDE AWVVGMAILM SVIVLAIVFG
60 70 80 90 100
NVLVITAIAK FERLQTVTNY FITSLACADL VMGLAVVPFG ASHILMKMWN
110 120 130 140 150
FGNFWCEFWT SIDVLCVTAS IETLCVIAVD RYVAITSPFK YQSLLTKNKA
160 170 180 190 200
RVVILMVWIV SGLTSFLPIQ MHWYRATHKQ AIDCYAKETC CDFFTNQAYA
210 220 230 240 250
IASSIVSFYV PLVVMVFVYS RVFQVAKRQL QKIDKSEGRF HAQNLSQVEQ
260 270 280 290 300
DGRSGHGLRS SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIRA
310 320 330 340 350
NLIPKEVYIL LNWLGYVNSA FNPLIYCRSP DFRIAFQELL CLRRSSSKTY
360 370 380 390 400
GNGYSSNSNG RTDYTGEQSA YQLGQEKENE LLCEEAPGME GFVNCQGTVP
410
SLSIDSQGRN CNTNDSPL
Length:418
Mass (Da):46,891
Last modified:July 1, 1989 - v1
Checksum:i907B2882AFC02AC5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti262S → F in AAA89068 (PubMed:2155412).Curated1
Sequence conflicti334I → Y in AAA89068 (PubMed:2155412).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03024 mRNA. Translation: AAA40675.1.
X17607 Genomic DNA. Translation: CAA35609.1.
L39264 Genomic DNA. Translation: AAA89068.1.
U35448 Genomic DNA. Translation: AAC52449.1.
PIRiS10855.
UniGeneiRn.10206.

Genome annotation databases

UCSCiRGD:2060. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03024 mRNA. Translation: AAA40675.1.
X17607 Genomic DNA. Translation: CAA35609.1.
L39264 Genomic DNA. Translation: AAA89068.1.
U35448 Genomic DNA. Translation: AAC52449.1.
PIRiS10855.
UniGeneiRn.10206.

3D structure databases

ProteinModelPortaliP10608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10608. 5 interactors.
STRINGi10116.ENSRNOP00000026098.

Chemistry databases

BindingDBiP10608.
ChEMBLiCHEMBL3754.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP10608.
PhosphoSitePlusiP10608.

Proteomic databases

PaxDbiP10608.
PRIDEiP10608.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2060. rat.

Organism-specific databases

RGDi2060. Adrb2.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP10608.
PhylomeDBiP10608.

Miscellaneous databases

PROiP10608.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR000332. ADRB2_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24248:SF21. PTHR24248:SF21. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADRB2_RAT
AccessioniPrimary (citable) accession number: P10608
Secondary accession number(s): Q6LCR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 146 of the entry and version 1 of the sequence. [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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.