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Protein

Beta-1 adrenergic receptor

Gene

Adrb1

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381Agonist or antagonistBy similarity
Binding sitei143 – 1431Agonist or antagonistBy similarity

GO - Molecular functioni

  1. beta1-adrenergic receptor activity Source: RGD
  2. dopamine binding Source: RGD
  3. drug binding Source: RGD
  4. epinephrine binding Source: RGD
  5. norepinephrine binding Source: RGD
  6. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  7. receptor signaling protein activity Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
  2. aging Source: RGD
  3. apoptotic process Source: RGD
  4. brown fat cell differentiation Source: Ensembl
  5. diet induced thermogenesis Source: Ensembl
  6. fear response Source: Ensembl
  7. glycogen catabolic process Source: RGD
  8. G-protein coupled receptor signaling pathway Source: RGD
  9. heat generation Source: Ensembl
  10. lipid homeostasis Source: RGD
  11. memory Source: RGD
  12. negative regulation of multicellular organism growth Source: Ensembl
  13. negative regulation of smooth muscle contraction Source: RGD
  14. negative regulation of urine volume Source: RGD
  15. positive regulation of adenylate cyclase activity Source: RGD
  16. positive regulation of apoptotic process Source: RGD
  17. positive regulation of cAMP biosynthetic process Source: RGD
  18. positive regulation of cAMP-mediated signaling Source: UniProtKB
  19. positive regulation of cation channel activity Source: RGD
  20. positive regulation of cell growth involved in cardiac muscle cell development Source: RGD
  21. positive regulation of heart rate Source: RGD
  22. positive regulation of heart rate by epinephrine-norepinephrine Source: Ensembl
  23. positive regulation of long-term synaptic potentiation Source: RGD
  24. positive regulation of Ras GTPase activity Source: UniProtKB
  25. positive regulation of renin secretion into blood stream Source: RGD
  26. positive regulation of saliva secretion Source: RGD
  27. positive regulation of systemic arterial blood pressure Source: RGD
  28. positive regulation of the force of heart contraction by norepinephrine Source: RGD
  29. protein localization to organelle Source: RGD
  30. regulation of calcium ion transport Source: RGD
  31. regulation of cardiac muscle cell contraction Source: RGD
  32. regulation of inhibitory postsynaptic membrane potential Source: RGD
  33. response to cold Source: Ensembl
  34. Rho protein signal transduction Source: RGD
  35. sensory perception of pain Source: RGD
  36. vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure Source: Ensembl
  37. wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_287445. G alpha (s) signalling events.
REACT_294981. Adrenoceptors.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2059. Adrb1.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. 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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555ExtracellularBy similarityAdd
BLAST
Transmembranei56 – 8429Helical; Name=1By similarityAdd
BLAST
Topological domaini85 – 939CytoplasmicBy similarity
Transmembranei94 – 12027Helical; Name=2By similarityAdd
BLAST
Topological domaini121 – 13212ExtracellularBy similarityAdd
BLAST
Transmembranei133 – 15422Helical; Name=3By similarityAdd
BLAST
Topological domaini155 – 17218CytoplasmicBy similarityAdd
BLAST
Transmembranei173 – 19624Helical; Name=4By similarityAdd
BLAST
Topological domaini197 – 22226ExtracellularBy similarityAdd
BLAST
Transmembranei223 – 24826Helical; Name=5By similarityAdd
BLAST
Topological domaini249 – 30860CytoplasmicBy similarityAdd
BLAST
Transmembranei309 – 33830Helical; Name=6By similarityAdd
BLAST
Topological domaini339 – 3435ExtracellularBy similarity
Transmembranei344 – 36623Helical; Name=7By similarityAdd
BLAST
Topological domaini367 – 466100CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. early endosome Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. intracellular membrane-bounded organelle Source: RGD
  5. membrane Source: RGD
  6. nucleus Source: RGD
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi466 – 4661V → A: Abolishes interaction with MAGI3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Beta-1 adrenergic receptorPRO_0000069124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi15 – 151N-linked (GlcNAc...)Curated
Disulfide bondi131 ↔ 216PROSITE-ProRule annotation
Disulfide bondi209 ↔ 215PROSITE-ProRule annotation
Modified residuei296 – 2961Phosphoserine; by PKASequence Analysis
Modified residuei301 – 3011Phosphoserine; by PKASequence Analysis
Lipidationi381 – 3811S-palmitoyl cysteineBy similarity
Modified residuei401 – 4011Phosphoserine; by PKASequence Analysis

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

PRIDEiP18090.

PTM databases

PhosphoSiteiP18090.

Expressioni

Tissue specificityi

Expressed in cortical neurons and coronary artery smooth muscle cells (at protein level).1 Publication

Gene expression databases

GenevestigatoriP18090.

Interactioni

Subunit structurei

Interacts (via C-terminus PDZ motif) with RAPGEF2; the interaction is direct (By similarity). Interacts with GOPC, MAGI3 and DLG4.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Magi3Q9JK713EBI-991303,EBI-696226

Protein-protein interaction databases

DIPiDIP-36293N.
IntActiP18090. 1 interaction.
STRINGi10116.ENSRNOP00000022813.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FF9model-A34-384[»]
ProteinModelPortaliP18090.
SMRiP18090. Positions 56-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 23215Agonist and antagonist bindingBy similarityAdd
BLAST
Regioni326 – 3338Agonist and antagonist bindingBy similarity
Regioni352 – 3565Agonist and antagonist bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi463 – 4664PDZ-BindingBy similarity

Domaini

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

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

eggNOGiNOG262978.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP18090.
KOiK04141.
OrthoDBiEOG7BS4BS.
PhylomeDBiP18090.
TreeFamiTF316350.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR000507. ADRB1_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00561. ADRENRGCB1AR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18090-1 [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 TLPFRYQSLL TRARARALVC TVWAISALVS FLPILMHWWR
210 220 230 240 250
AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE
260 270 280 290 300
AQKQVKKIDS CERRFLTGPP RPPSPAPSPS 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 DDDAGATPPA RLLEPWAGCN GGTTTVDSDS
460
SLDEPGRQGF SSESKV
Length:466
Mass (Da):50,472
Last modified:October 31, 1990 - v1
Checksum:i2955CB024944A12B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621L → S in BAA00527 (PubMed:2167473).Curated
Sequence conflicti267 – 2671T → S in BAA00527 (PubMed:2167473).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05561 Genomic DNA. Translation: AAA40792.1.
D00634 Genomic DNA. Translation: BAA00527.1.
PIRiS12591.
RefSeqiNP_036833.1. NM_012701.1.
UniGeneiRn.87064.

Genome annotation databases

GeneIDi24925.
KEGGirno:24925.
UCSCiRGD:2059. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05561 Genomic DNA. Translation: AAA40792.1.
D00634 Genomic DNA. Translation: BAA00527.1.
PIRiS12591.
RefSeqiNP_036833.1. NM_012701.1.
UniGeneiRn.87064.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FF9model-A34-384[»]
ProteinModelPortaliP18090.
SMRiP18090. Positions 56-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36293N.
IntActiP18090. 1 interaction.
STRINGi10116.ENSRNOP00000022813.

Chemistry

BindingDBiP18090.
ChEMBLiCHEMBL2095166.
GuidetoPHARMACOLOGYi28.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP18090.

Proteomic databases

PRIDEiP18090.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24925.
KEGGirno:24925.
UCSCiRGD:2059. rat.

Organism-specific databases

CTDi153.
RGDi2059. Adrb1.

Phylogenomic databases

eggNOGiNOG262978.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP18090.
KOiK04141.
OrthoDBiEOG7BS4BS.
PhylomeDBiP18090.
TreeFamiTF316350.

Enzyme and pathway databases

ReactomeiREACT_287445. G alpha (s) signalling events.
REACT_294981. Adrenoceptors.

Miscellaneous databases

NextBioi604879.
PROiP18090.

Gene expression databases

GenevestigatoriP18090.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR000507. ADRB1_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00561. ADRENRGCB1AR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1989) [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(1989) [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(2001) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGI3, MUTAGENESIS OF VAL-466.

Entry informationi

Entry nameiADRB1_RAT
AccessioniPrimary (citable) accession number: P18090
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1990
Last sequence update: October 31, 1990
Last modified: March 31, 2015
This is version 136 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.