Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P18090 (ADRB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-1 adrenergic receptor
Alternative name(s):
Beta-1 adrenoreceptor
Short name=Beta-1 adrenoceptor
Gene names
Name:Adrb1
Synonyms:Adrb1r
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling.

Subunit structure

Interacts (via C-terminus PDZ motif) with RAPGEF2; the interaction is direct By similarity. Interacts with GOPC, MAGI3 and DLG4. Ref.4

Subcellular location

Cell membrane; Multi-pass membrane protein. Early endosome By similarity. Note: Localized at the plasma membrane. Found in the Golgi upon GOPC overexpression By similarity. Colocalizes with RAPGEF2 at the plasma membrane. Ref.3

Tissue specificity

Expressed in cortical neurons and coronary artery smooth muscle cells (at protein level). Ref.3

Domain

The PDZ domain-binding motif mediates competitive interactions with GOPC, MAGI3 and DLG4 and plays a role in subcellular location of the receptor.

Post-translational modification

Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 12514203. Source: RGD

Rho protein signal transduction

Inferred from mutant phenotype PubMed 18306009. Source: RGD

adenylate cyclase-activating adrenergic receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

aging

Inferred from expression pattern PubMed 19883205. Source: RGD

apoptotic process

Inferred from direct assay PubMed 16820859. Source: RGD

brown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

diet induced thermogenesis

Inferred from electronic annotation. Source: Ensembl

fear response

Inferred from electronic annotation. Source: Ensembl

glycogen catabolic process

Inferred from direct assay PubMed 17911346. Source: RGD

heat generation

Inferred from electronic annotation. Source: Ensembl

lipid homeostasis

Inferred from mutant phenotype PubMed 22457517. Source: RGD

memory

Inferred from mutant phenotype PubMed 17961922. Source: RGD

negative regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle contraction

Inferred from mutant phenotype PubMed 18306009. Source: RGD

negative regulation of urine volume

Inferred from direct assay PubMed 7912752. Source: RGD

positive regulation of Ras GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17143192. Source: RGD

positive regulation of cAMP biosynthetic process

Inferred from mutant phenotype PubMed 18202135. Source: RGD

positive regulation of cAMP-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cation channel activity

Inferred from direct assay PubMed 22505670. Source: RGD

positive regulation of cell growth involved in cardiac muscle cell development

Inferred from mutant phenotype PubMed 18194989. Source: RGD

positive regulation of heart rate

Inferred from mutant phenotype PubMed 9089896. Source: RGD

positive regulation of heart rate by epinephrine-norepinephrine

Inferred from electronic annotation. Source: Ensembl

positive regulation of renin secretion into blood stream

Inferred from mutant phenotype PubMed 15810988. Source: RGD

positive regulation of saliva secretion

Inferred from mutant phenotype PubMed 18275933. Source: RGD

positive regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 18931026. Source: RGD

positive regulation of the force of heart contraction by norepinephrine

Inferred from direct assay PubMed 19133992. Source: RGD

protein localization to organelle

Inferred from direct assay PubMed 22105697. Source: RGD

regulation of calcium ion transport

Inferred from direct assay PubMed 19133992. Source: RGD

regulation of cardiac muscle cell contraction

Inferred from mutant phenotype PubMed 22216755. Source: RGD

regulation of inhibitory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 18262504. Source: RGD

response to cold

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from mutant phenotype PubMed 19283893. Source: RGD

vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from mutant phenotype PubMed 19320892. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17337326. Source: RGD

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 2858976. Source: RGD

membrane

Inferred from direct assay PubMed 1686765. Source: RGD

nucleus

Inferred from direct assay PubMed 16631628. Source: RGD

plasma membrane

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionRas guanyl-nucleotide exchange factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

beta1-adrenergic receptor activity

Inferred from direct assay PubMed 12514203PubMed 6381693. Source: RGD

dopamine binding

Inferred from direct assay PubMed 6381693. Source: RGD

drug binding

Inferred from direct assay PubMed 6289140. Source: RGD

epinephrine binding

Inferred from direct assay PubMed 6381693. Source: RGD

norepinephrine binding

Inferred from direct assay PubMed 6381693. Source: RGD

protein binding

Inferred from physical interaction Ref.4. Source: IntAct

receptor signaling protein activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Magi3Q9JK713EBI-991303,EBI-696226

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Beta-1 adrenergic receptor
PRO_0000069124

Regions

Topological domain1 – 5555Extracellular By similarity
Transmembrane56 – 8429Helical; Name=1; By similarity
Topological domain85 – 939Cytoplasmic By similarity
Transmembrane94 – 12027Helical; Name=2; By similarity
Topological domain121 – 13212Extracellular By similarity
Transmembrane133 – 15422Helical; Name=3; By similarity
Topological domain155 – 17218Cytoplasmic By similarity
Transmembrane173 – 19624Helical; Name=4; By similarity
Topological domain197 – 22226Extracellular By similarity
Transmembrane223 – 24826Helical; Name=5; By similarity
Topological domain249 – 30860Cytoplasmic By similarity
Transmembrane309 – 33830Helical; Name=6; By similarity
Topological domain339 – 3435Extracellular By similarity
Transmembrane344 – 36623Helical; Name=7; By similarity
Topological domain367 – 466100Cytoplasmic By similarity
Region218 – 23215Agonist and antagonist binding By similarity
Region326 – 3338Agonist and antagonist binding By similarity
Region352 – 3565Agonist and antagonist binding By similarity
Motif463 – 4664PDZ-Binding By similarity

Sites

Binding site1381Agonist or antagonist By similarity
Binding site1431Agonist or antagonist By similarity

Amino acid modifications

Modified residue2961Phosphoserine; by PKA Potential
Modified residue3011Phosphoserine; by PKA Potential
Modified residue4011Phosphoserine; by PKA Potential
Lipidation3811S-palmitoyl cysteine By similarity
Glycosylation151N-linked (GlcNAc...) Probable
Disulfide bond131 ↔ 216 By similarity
Disulfide bond209 ↔ 215 By similarity

Experimental info

Mutagenesis4661V → A: Abolishes interaction with MAGI3. Ref.4
Sequence conflict1621L → S in BAA00527. Ref.2
Sequence conflict2671T → S in BAA00527. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P18090 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 2955CB024944A12B

FASTA46650,472
        10         20         30         40         50         60 
MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS APLSQQWTAG 

        70         80         90        100        110        120 
MGLLLALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV 

       130        140        150        160        170        180 
WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TLPFRYQSLL TRARARALVC 

       190        200        210        220        230        240 
TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM 

       250        260        270        280        290        300 
AFVYLRVFRE AQKQVKKIDS CERRFLTGPP RPPSPAPSPS PGPPRPADSL ANGRSSKRRP 

       310        320        330        340        350        360 
SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF FNWLGYANSA 

       370        380        390        400        410        420 
FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA SGCLARAGPP PSPGAPSDDD 

       430        440        450        460 
DDDAGATPPA RLLEPWAGCN GGTTTVDSDS SLDEPGRQGF SSESKV 

« Hide

References

[1]"Molecular cloning and expression of the rat beta 1-adrenergic receptor gene."
Machida C.A., Bunzow J.R., Searles R.P., van Tol H.H.M., Tester B., Neve K.A., Teal P., Nipper V., Civelli O.
J. Biol. Chem. 265:12960-12965(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Primary structure of the rat beta-1 adrenergic receptor gene."
Shimomura H., Terada A.
Nucleic Acids Res. 18:4591-4591(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Direct binding of the beta1 adrenergic receptor to the cyclic AMP-dependent guanine nucleotide exchange factor CNrasGEF leads to Ras activation."
Pak Y., Pham N., Rotin D.
Mol. Cell. Biol. 22:7942-7952(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Proteomic analysis of beta1-adrenergic receptor interactions with PDZ scaffold proteins."
He J., Bellini M., Inuzuka H., Xu J., Xiong Y., Yang X., Castleberry A.M., Hall R.A.
J. Biol. Chem. 281:2820-2827(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAGI3, MUTAGENESIS OF VAL-466.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05561 Genomic DNA. Translation: AAA40792.1.
D00634 Genomic DNA. Translation: BAA00527.1.
PIRS12591.
RefSeqNP_036833.1. NM_012701.1.
UniGeneRn.87064.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FF9model-A34-384[»]
ProteinModelPortalP18090.
SMRP18090. Positions 56-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36293N.
IntActP18090. 1 interaction.
STRING10116.ENSRNOP00000022813.

Chemistry

BindingDBP18090.
ChEMBLCHEMBL3252.
GuidetoPHARMACOLOGY28.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP18090.

Proteomic databases

PRIDEP18090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022813; ENSRNOP00000022813; ENSRNOG00000017002.
GeneID24925.
KEGGrno:24925.
UCSCRGD:2059. rat.

Organism-specific databases

CTD153.
RGD2059. Adrb1.

Phylogenomic databases

eggNOGNOG262978.
GeneTreeENSGT00720000108411.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP18090.
KOK04141.
OrthoDBEOG7BS4BS.
PhylomeDBP18090.
TreeFamTF316350.

Gene expression databases

GenevestigatorP18090.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR002233. ADR_fam.
IPR000507. ADRB1_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01103. ADRENERGICR.
PR00561. ADRENRGCB1AR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604879.
PROP18090.

Entry information

Entry nameADRB1_RAT
AccessionPrimary (citable) accession number: P18090
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 11, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries