Beta-1 adrenergic receptor - Rattus norvegicus (Rat)

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P18090 (ADRB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-1 adrenergic receptor

Alternative name(s):
Beta-1 adrenoreceptor
Short name=Beta-1 adrenoceptor

Gene names

Name:	Adrb1
Synonyms:	Adrb1r

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subunit structure	Interacts with GOPC, MAGI3 and DLG4. Ref.3
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Note: Localized at the plasma membrane. Found in the Golgi upon GOPC overexpression By similarity.
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 component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from mutant phenotype PubMed 18306009. Source: RGD adenylate cyclase-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara diet induced thermogenesis Inferred from electronic annotation. Source: Compara fear response Inferred from electronic annotation. Source: Compara glycogen catabolic process Inferred from direct assay PubMed 17911346. Source: RGD heat generation Inferred from electronic annotation. Source: Compara 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: Compara 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 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 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: Compara 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: Compara 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: Compara wound healing Inferred from mutant phenotype PubMed 19320892. Source: RGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 17337326. Source: RGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay PubMed 1686765. Source: RGD nucleus Inferred from direct assay PubMed 16631628. Source: RGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta1-adrenergic receptor activity Inferred from direct assay PubMed 12514203 PubMed 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Magi3	Q9JK71	3	EBI-991303,EBI-696226

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 466

466

Beta-1 adrenergic receptor

PRO_0000069124

Regions

Topological domain

1 – 55

Extracellular By similarity

Transmembrane

56 – 84

Helical; Name=1; By similarity

Topological domain

85 – 93

Cytoplasmic By similarity

Transmembrane

94 – 120

Helical; Name=2; By similarity

Topological domain

121 – 132

Extracellular By similarity

Transmembrane

133 – 154

Helical; Name=3; By similarity

Topological domain

155 – 172

Cytoplasmic By similarity

Transmembrane

173 – 196

Helical; Name=4; By similarity

Topological domain

197 – 222

Extracellular By similarity

Transmembrane

223 – 248

Helical; Name=5; By similarity

Topological domain

249 – 308

Cytoplasmic By similarity

Transmembrane

309 – 338

Helical; Name=6; By similarity

Topological domain

339 – 343

Extracellular By similarity

Transmembrane

344 – 366

Helical; Name=7; By similarity

Topological domain

367 – 466

100

Cytoplasmic By similarity

Region

218 – 232

Agonist and antagonist binding By similarity

Region

326 – 333

Agonist and antagonist binding By similarity

Region

352 – 356

Agonist and antagonist binding By similarity

Motif

463 – 466

PDZ-Binding By similarity

Sites

Binding site

138

Agonist or antagonist By similarity

Binding site

143

Agonist or antagonist By similarity

Amino acid modifications

Modified residue

296

Phosphoserine; by PKA Potential

Modified residue

301

Phosphoserine; by PKA Potential

Modified residue

401

Phosphoserine; by PKA Potential

Lipidation

381

S-palmitoyl cysteine By similarity

Glycosylation

N-linked (GlcNAc...) Probable

Disulfide bond

131 ↔ 216

By similarity

Disulfide bond

209 ↔ 215

By similarity

Experimental info

Mutagenesis

466

V → A: Abolishes interaction with MAGI3. Ref.3

Sequence conflict

162

L → S in BAA00527. Ref.2

Sequence conflict

267

T → S in BAA00527. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P18090 [UniParc].

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

FASTA

466

50,472

        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]	"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.

IPI

IPI00188184.

PIR

S12591.

RefSeq

NP_036833.1. NM_012701.1.

UniGene

Rn.87064.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FF9	model	-	A	34-384	[»]

ProteinModelPortal

P18090.

SMR

P18090. Positions 56-380.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36293N.

IntAct

P18090. 1 interaction.

STRING

10116.ENSRNOP00000022813.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P18090.

Proteomic databases

PRIDE

P18090.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000022813; ENSRNOP00000022813; ENSRNOG00000017002.

GeneID

24925.

KEGG

rno:24925.

UCSC

RGD:2059. rat.

Organism-specific databases

CTD

153.

RGD

2059. Adrb1.

Phylogenomic databases

eggNOG

NOG262978.

GeneTree

ENSGT00680000099833.

HOGENOM

HOG000239242.

HOVERGEN

HBG106962.

InParanoid

P18090.

K04141.

OrthoDB

EOG4WQ12W.

Gene expression databases

Genevestigator

P18090.

GermOnline

ENSRNOG00000017002. Rattus norvegicus.

Family and domain databases

InterPro

IPR000507. Adrgc_rcpt_B1.
IPR002233. Adrnrgc_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR01103. ADRENERGICR.
PR00561. ADRENRGCB1AR.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P18090.

ChEMBL

CHEMBL3252.

NextBio

604879.

Entry information

Entry name

ADRB1_RAT

Accession

Primary (citable) accession number: P18090

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents