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Protein

Beta-1 adrenergic receptor

Gene

Adrb1

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. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei138Agonist or antagonistBy similarity1
Binding sitei143Agonist 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

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1 adrenergic receptor
Alternative name(s):
Beta-1 adrenoreceptor
Short name:
Beta-1 adrenoceptor
Gene namesi
Name:Adrb1
Synonyms:Adrb1r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:87937 Adrb1

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 – 55ExtracellularBy similarityAdd BLAST55
Transmembranei56 – 84Helical; Name=1By similarityAdd BLAST29
Topological domaini85 – 93CytoplasmicBy similarity9
Transmembranei94 – 120Helical; Name=2By similarityAdd BLAST27
Topological domaini121 – 132ExtracellularBy similarityAdd BLAST12
Transmembranei133 – 154Helical; Name=3By similarityAdd BLAST22
Topological domaini155 – 172CytoplasmicBy similarityAdd BLAST18
Transmembranei173 – 196Helical; Name=4By similarityAdd BLAST24
Topological domaini197 – 222ExtracellularBy similarityAdd BLAST26
Transmembranei223 – 248Helical; Name=5By similarityAdd BLAST26
Topological domaini249 – 308CytoplasmicBy similarityAdd BLAST60
Transmembranei309 – 338Helical; Name=6By similarityAdd BLAST30
Topological domaini339 – 343ExtracellularBy similarity5
Transmembranei344 – 366Helical; Name=7By similarityAdd BLAST23
Topological domaini367 – 466CytoplasmicBy similarityAdd BLAST100

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3440

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000691221 – 466Beta-1 adrenergic receptorAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi15N-linked (GlcNAc...) asparagineCurated1
Disulfide bondi131 ↔ 216PROSITE-ProRule annotation
Disulfide bondi209 ↔ 215PROSITE-ProRule annotation
Modified residuei296Phosphoserine; by PKASequence analysis1
Modified residuei301Phosphoserine; by PKASequence analysis1
Lipidationi381S-palmitoyl cysteineBy similarity1
Modified residuei401Phosphoserine; by PKASequence analysis1
Modified residuei417PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP34971
PRIDEiP34971

PTM databases

iPTMnetiP34971
PhosphoSitePlusiP34971

Expressioni

Gene expression databases

BgeeiENSMUSG00000035283
CleanExiMM_ADRB1
GenevisibleiP34971 MM

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-59567N
IntActiP34971, 6 interactors
MINTiP34971
STRINGi10090.ENSMUSP00000040847

Chemistry databases

BindingDBiP34971

Structurei

3D structure databases

ProteinModelPortaliP34971
SMRiP34971
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni218 – 232Agonist and antagonist bindingBy similarityAdd BLAST15
Regioni326 – 333Agonist and antagonist bindingBy similarity8
Regioni352 – 356Agonist and antagonist bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi463 – 466PDZ-BindingBy similarity4

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00890000139331
HOGENOMiHOG000239242
HOVERGENiHBG106962
InParanoidiP34971
KOiK04141
OMAiNVVKAFH
OrthoDBiEOG091G06VI
TreeFamiTF316350

Family and domain databases

InterProiView protein in InterPro
IPR002233 ADR_fam
IPR000507 ADRB1_rcpt
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR01103 ADRENERGICR
PR00561 ADRENRGCB1AR
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.

P34971-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS
60 70 80 90 100
APLSQQWTAG MGLLLALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL
110 120 130 140 150
ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC
160 170 180 190 200
VIALDRYLAI TSPFRYQSLL TRARARALVC TVWAISALVS FLPILMHWWR
210 220 230 240 250
AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE
260 270 280 290 300
AQKQVKKIDS CERRFLGGPA RPPSPEPSPS PGPPRPADSL ANGRSSKRRP
310 320 330 340 350
SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF
360 370 380 390 400
FNWLGYANSA FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA
410 420 430 440 450
SGCLARAGPP PSPGAPSDDD DDDAGTTPPA RLLEPWTGCN GGTTTVDSDS
460
SLDEPGRQGF SSESKV
Length:466
Mass (Da):50,494
Last modified:July 27, 2011 - v2
Checksum:iE4861E250B62F735
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti65L → V in AAA02929 (PubMed:8395893).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10084 Genomic DNA Translation: AAA02929.1
CH466585 Genomic DNA Translation: EDL01765.1
BC140970 mRNA Translation: AAI40971.1
BC147435 mRNA Translation: AAI47436.1
CCDSiCCDS29919.1
PIRiS36794
RefSeqiNP_031445.2, NM_007419.2
UniGeneiMm.46797

Genome annotation databases

EnsembliENSMUST00000038949; ENSMUSP00000040847; ENSMUSG00000035283
GeneIDi11554
KEGGimmu:11554
UCSCiuc008hze.2 mouse

Similar proteinsi

Entry informationi

Entry nameiADRB1_MOUSE
AccessioniPrimary (citable) accession number: P34971
Secondary accession number(s): B2RVY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 27, 2011
Last modified: June 20, 2018
This is version 158 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, Direct protein sequencing, Reference proteome

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