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Protein

Beta-1 adrenergic receptor

Gene

ADRB1

Organism
Meleagris gallopavo (Common turkey)
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211Agonist or antagonist
Binding sitei126 – 1261Agonist or antagonistBy similarity

GO - Molecular functioni

  1. beta1-adrenergic receptor activity Source: InterPro
  2. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  3. receptor signaling protein activity Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
  2. intracellular signal transduction Source: GOC
  3. positive regulation of cAMP biosynthetic process Source: UniProtKB
  4. positive regulation of cAMP-mediated signaling Source: UniProtKB
  5. positive regulation of heart contraction Source: InterPro
  6. positive regulation of Ras GTPase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1 adrenergic receptor
Alternative name(s):
Beta-1 adrenoreceptor
Short name:
Beta-1 adrenoceptor
Short name:
Beta-T
Gene namesi
Name:ADRB1
OrganismiMeleagris gallopavo (Common turkey)
Taxonomic identifieri9103 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaeMeleagridinaeMeleagris
ProteomesiUP000001645 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838Extracellular1 PublicationAdd
BLAST
Transmembranei39 – 6729Helical; Name=1Add
BLAST
Topological domaini68 – 769Cytoplasmic1 Publication
Transmembranei77 – 10327Helical; Name=2Add
BLAST
Topological domaini104 – 11512Extracellular1 PublicationAdd
BLAST
Transmembranei116 – 13722Helical; Name=3Add
BLAST
Topological domaini138 – 15518Cytoplasmic1 PublicationAdd
BLAST
Transmembranei156 – 17924Helical; Name=4Add
BLAST
Topological domaini180 – 20526Extracellular1 PublicationAdd
BLAST
Transmembranei206 – 23126Helical; Name=5Add
BLAST
Topological domaini232 – 28554Cytoplasmic1 PublicationAdd
BLAST
Transmembranei286 – 31530Helical; Name=6Add
BLAST
Topological domaini316 – 3205Extracellular1 Publication
Transmembranei321 – 34323Helical; Name=7Add
BLAST
Topological domaini344 – 483140Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. early endosome Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Beta-1 adrenergic receptorPRO_0000069120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi14 – 141N-linked (GlcNAc...)Curated
Disulfide bondi114 ↔ 199PROSITE-ProRule annotation1 Publication
Disulfide bondi192 ↔ 198PROSITE-ProRule annotation1 Publication
Lipidationi358 – 3581S-palmitoyl cysteineBy similarity

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

Interactioni

Protein-protein interaction databases

DIPiDIP-60236N.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 6832Combined sources
Helixi70 – 723Combined sources
Helixi75 – 9218Combined sources
Helixi94 – 10411Combined sources
Helixi110 – 14435Combined sources
Helixi146 – 1527Combined sources
Helixi155 – 17824Combined sources
Turni179 – 1824Combined sources
Helixi187 – 1948Combined sources
Helixi205 – 21511Combined sources
Helixi217 – 23923Combined sources
Helixi248 – 2514Combined sources
Helixi279 – 31537Combined sources
Helixi317 – 3193Combined sources
Helixi322 – 34322Combined sources
Helixi347 – 35610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEPNMR-A345-359[»]
2VT4X-ray2.70A/B/C/D33-367[»]
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/B33-367[»]
2YCXX-ray3.25A/B33-367[»]
2YCYX-ray3.15A/B33-367[»]
2YCZX-ray3.65A/B33-367[»]
3ZPQX-ray2.80A/B33-368[»]
3ZPRX-ray2.70A/B33-368[»]
4AMIX-ray3.20A/B33-368[»]
4AMJX-ray2.30A/B33-368[»]
4BVNX-ray2.10A33-368[»]
4GPOX-ray3.50A/B33-368[»]
SMRiP07700. Positions 39-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07700.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 21515Agonist and antagonist bindingAdd
BLAST
Regioni303 – 3108Agonist and antagonist binding
Regioni329 – 3335Agonist and antagonist binding

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

HOVERGENiHBG106962.
InParanoidiP07700.

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.

P07700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDGWLPPDC GPHNRSGGGG ATAAPTGSRQ VSAELLSQQW EAGMSLLMAL
60 70 80 90 100
VVLLIVAGNV LVIAAIGRTQ RLQTLTNLFI TSLACADLVM GLLVVPFGAT
110 120 130 140 150
LVVRGTWLWG SFLCECWTSL DVLCVTASIE TLCVIAIDRY LAITSPFRYQ
160 170 180 190 200
SLMTRARAKV IICTVWAISA LVSFLPIMMH WWRDEDPQAL KCYQDPGCCD
210 220 230 240 250
FVTNRAYAIA SSIISFYIPL LIMIFVYLRV YREAKEQIRK IDRCEGRFYG
260 270 280 290 300
SQEQPQPPPL PQHQPILGNG RASKRKTSRV MAMREHKALK TLGIIMGVFT
310 320 330 340 350
LCWLPFFLVN IVNVFNRDLV PDWLFVFFNW LGYANSAFNP IIYCRSPDFR
360 370 380 390 400
KAFKRLLCFP RKADRRLHAG GQPAPLPGGF ISTLGSPEHS PGGTWSDCNG
410 420 430 440 450
GTRGGSESSL EERHSKTSRS ESKMEREKNI LATTRFYCTF LGNGDKAVFC
460 470 480
TVLRIVKLFE DATCTCPHTH KLKMKWRFKQ HQA
Length:483
Mass (Da):54,078
Last modified:March 31, 1988 - v1
Checksum:iB11A7E71F6CCE3E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14379 mRNA. Translation: AAA49627.1.
PIRiA25896.
RefSeqiNP_001290104.1. NM_001303175.1.
UniGeneiMga.4462.

Genome annotation databases

GeneIDi100303680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14379 mRNA. Translation: AAA49627.1.
PIRiA25896.
RefSeqiNP_001290104.1. NM_001303175.1.
UniGeneiMga.4462.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEPNMR-A345-359[»]
2VT4X-ray2.70A/B/C/D33-367[»]
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/B33-367[»]
2YCXX-ray3.25A/B33-367[»]
2YCYX-ray3.15A/B33-367[»]
2YCZX-ray3.65A/B33-367[»]
3ZPQX-ray2.80A/B33-368[»]
3ZPRX-ray2.70A/B33-368[»]
4AMIX-ray3.20A/B33-368[»]
4AMJX-ray2.30A/B33-368[»]
4BVNX-ray2.10A33-368[»]
4GPOX-ray3.50A/B33-368[»]
SMRiP07700. Positions 39-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60236N.

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100303680.

Phylogenomic databases

HOVERGENiHBG106962.
InParanoidiP07700.

Miscellaneous databases

EvolutionaryTraceiP07700.

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. 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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 345-359.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-367 IN COMPLEX WITH THE ANTAGONIST CYANOPINDOLOL, DISULFIDE BONDS, FUNCTION, TOPOLOGY.

Entry informationi

Entry nameiADRB1_MELGA
AccessioniPrimary (citable) accession number: P07700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1988
Last sequence update: March 31, 1988
Last modified: March 31, 2015
This is version 115 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.