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P07700 (ADRB1_MELGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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·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
Short name=Beta-T
Gene names
Name:ADRB1
OrganismMeleagris gallopavo (Common turkey) [Reference proteome]
Taxonomic identifier9103 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaeMeleagridinaeMeleagris

Protein attributes

Sequence length483 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. Ref.3

Subcellular location

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

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_processadenylate cyclase-activating adrenergic receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from sequence or structural similarity. Source: GOC

positive regulation of Ras GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of heart contraction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentearly endosome

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionRas guanyl-nucleotide exchange factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

beta1-adrenergic receptor activity

Inferred from electronic annotation. Source: InterPro

receptor signaling protein activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Beta-1 adrenergic receptor
PRO_0000069120

Regions

Topological domain1 – 3838Extracellular Ref.3
Transmembrane39 – 6729Helical; Name=1
Topological domain68 – 769Cytoplasmic Ref.3
Transmembrane77 – 10327Helical; Name=2
Topological domain104 – 11512Extracellular Ref.3
Transmembrane116 – 13722Helical; Name=3
Topological domain138 – 15518Cytoplasmic Ref.3
Transmembrane156 – 17924Helical; Name=4
Topological domain180 – 20526Extracellular Ref.3
Transmembrane206 – 23126Helical; Name=5
Topological domain232 – 28554Cytoplasmic Ref.3
Transmembrane286 – 31530Helical; Name=6
Topological domain316 – 3205Extracellular Ref.3
Transmembrane321 – 34323Helical; Name=7
Topological domain344 – 483140Cytoplasmic Ref.3
Region201 – 21515Agonist and antagonist binding
Region303 – 3108Agonist and antagonist binding
Region329 – 3335Agonist and antagonist binding

Sites

Binding site1211Agonist or antagonist
Binding site1261Agonist or antagonist By similarity

Amino acid modifications

Lipidation3581S-palmitoyl cysteine By similarity
Glycosylation141N-linked (GlcNAc...) Probable
Disulfide bond114 ↔ 199 Ref.3
Disulfide bond192 ↔ 198 Ref.3

Secondary structure

.................................... 483
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07700 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: B11A7E71F6CCE3E4

FASTA48354,078
        10         20         30         40         50         60 
MGDGWLPPDC GPHNRSGGGG ATAAPTGSRQ VSAELLSQQW EAGMSLLMAL VVLLIVAGNV 

        70         80         90        100        110        120 
LVIAAIGRTQ RLQTLTNLFI TSLACADLVM GLLVVPFGAT LVVRGTWLWG SFLCECWTSL 

       130        140        150        160        170        180 
DVLCVTASIE TLCVIAIDRY LAITSPFRYQ SLMTRARAKV IICTVWAISA LVSFLPIMMH 

       190        200        210        220        230        240 
WWRDEDPQAL KCYQDPGCCD FVTNRAYAIA SSIISFYIPL LIMIFVYLRV YREAKEQIRK 

       250        260        270        280        290        300 
IDRCEGRFYG SQEQPQPPPL PQHQPILGNG RASKRKTSRV MAMREHKALK TLGIIMGVFT 

       310        320        330        340        350        360 
LCWLPFFLVN IVNVFNRDLV PDWLFVFFNW LGYANSAFNP IIYCRSPDFR KAFKRLLCFP 

       370        380        390        400        410        420 
RKADRRLHAG GQPAPLPGGF ISTLGSPEHS PGGTWSDCNG GTRGGSESSL EERHSKTSRS 

       430        440        450        460        470        480 
ESKMEREKNI LATTRFYCTF LGNGDKAVFC TVLRIVKLFE DATCTCPHTH KLKMKWRFKQ 


HQA 

« Hide

References

[1]"The avian beta-adrenergic receptor: primary structure and membrane topology."
Yarden Y., Rodriguez H., Wong S.K.-F., Brandt D.R., May D.C., Burnier J., Harkins R.N., Chen E.Y., Ramachandran J., Ullrich A., Ross E.M.
Proc. Natl. Acad. Sci. U.S.A. 83:6795-6799(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor."
Jung H., Windhaber R., Palm D., Schnackerz K.D.
FEBS Lett. 358:133-136(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 345-359.
[3]"Structure of a beta1-adrenergic G-protein-coupled receptor."
Warne T., Serrano-Vega M.J., Baker J.G., Moukhametzianov R., Edwards P.C., Henderson R., Leslie A.G.W., Tate C.G., Schertler G.F.X.
Nature 454:486-491(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-367 IN COMPLEX WITH THE ANTAGONIST CYANOPINDOLOL, DISULFIDE BONDS, FUNCTION, TOPOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14379 mRNA. Translation: AAA49627.1.
PIRA25896.
UniGeneMga.4462.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEPNMR-A345-359[»]
2VT4X-ray2.70A/B/C/D33-368[»]
2Y00X-ray2.50A/B33-368[»]
2Y01X-ray2.60A/B33-368[»]
2Y02X-ray2.60A/B33-368[»]
2Y03X-ray2.85A/B33-368[»]
2Y04X-ray3.05A/B33-368[»]
2YCWX-ray3.00A/B33-368[»]
2YCXX-ray3.25A/B33-368[»]
2YCYX-ray3.15A/B33-368[»]
2YCZX-ray3.65A/B33-368[»]
3ZPQX-ray2.80A/B33-368[»]
3ZPRX-ray2.70A/B33-368[»]
4AMIX-ray3.20A/B33-368[»]
4AMJX-ray2.30A/B33-368[»]
4GPOX-ray3.50A/B33-368[»]
ProteinModelPortalP07700.
SMRP07700. Positions 39-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60236N.

Protein family/group databases

GPCRDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG106962.

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]
PANTHERPTHR24248. PTHR24248. 1 hit.
PTHR24248:SF3. PTHR24248:SF3. 1 hit.
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

EvolutionaryTraceP07700.

Entry information

Entry nameADRB1_MELGA
AccessionPrimary (citable) accession number: P07700
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 105 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