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P07700

- ADRB1_MELGA

UniProt

P07700 - ADRB1_MELGA

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Protein
Beta-1 adrenergic receptor
Gene
ADRB1
Organism
Meleagris gallopavo (Common turkey)
Status
Reviewed - 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 antagonist By similarity

GO - Molecular functioni

  1. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  2. beta1-adrenergic receptor activity Source: InterPro
  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 Ras GTPase activity Source: UniProtKB
  4. positive regulation of cAMP biosynthetic process Source: UniProtKB
  5. positive regulation of cAMP-mediated signaling Source: UniProtKB
  6. positive regulation of heart contraction Source: InterPro
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaeMeleagridinaeMeleagris
ProteomesiUP000001645: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838Extracellular1 Publication
Add
BLAST
Transmembranei39 – 6729Helical; Name=1
Add
BLAST
Topological domaini68 – 769Cytoplasmic1 Publication
Transmembranei77 – 10327Helical; Name=2
Add
BLAST
Topological domaini104 – 11512Extracellular1 Publication
Add
BLAST
Transmembranei116 – 13722Helical; Name=3
Add
BLAST
Topological domaini138 – 15518Cytoplasmic1 Publication
Add
BLAST
Transmembranei156 – 17924Helical; Name=4
Add
BLAST
Topological domaini180 – 20526Extracellular1 Publication
Add
BLAST
Transmembranei206 – 23126Helical; Name=5
Add
BLAST
Topological domaini232 – 28554Cytoplasmic1 Publication
Add
BLAST
Transmembranei286 – 31530Helical; Name=6
Add
BLAST
Topological domaini316 – 3205Extracellular1 Publication
Transmembranei321 – 34323Helical; Name=7
Add
BLAST
Topological domaini344 – 483140Cytoplasmic1 Publication
Add
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 receptor
PRO_0000069120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi14 – 141N-linked (GlcNAc...) Inferred
Disulfide bondi114 ↔ 1991 Publication
Disulfide bondi192 ↔ 1981 Publication
Lipidationi358 – 3581S-palmitoyl cysteine By 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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP07700.
SMRiP07700. Positions 39-359.

Miscellaneous databases

EvolutionaryTraceiP07700.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG106962.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
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

MGDGWLPPDC GPHNRSGGGG ATAAPTGSRQ VSAELLSQQW EAGMSLLMAL    50
VVLLIVAGNV LVIAAIGRTQ RLQTLTNLFI TSLACADLVM GLLVVPFGAT 100
LVVRGTWLWG SFLCECWTSL DVLCVTASIE TLCVIAIDRY LAITSPFRYQ 150
SLMTRARAKV IICTVWAISA LVSFLPIMMH WWRDEDPQAL KCYQDPGCCD 200
FVTNRAYAIA SSIISFYIPL LIMIFVYLRV YREAKEQIRK IDRCEGRFYG 250
SQEQPQPPPL PQHQPILGNG RASKRKTSRV MAMREHKALK TLGIIMGVFT 300
LCWLPFFLVN IVNVFNRDLV PDWLFVFFNW LGYANSAFNP IIYCRSPDFR 350
KAFKRLLCFP RKADRRLHAG GQPAPLPGGF ISTLGSPEHS PGGTWSDCNG 400
GTRGGSESSL EERHSKTSRS ESKMEREKNI LATTRFYCTF LGNGDKAVFC 450
TVLRIVKLFE DATCTCPHTH KLKMKWRFKQ HQA 483
Length:483
Mass (Da):54,078
Last modified:April 1, 1988 - v1
Checksum:iB11A7E71F6CCE3E4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14379 mRNA. Translation: AAA49627.1.
PIRiA25896.
UniGeneiMga.4462.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14379 mRNA. Translation: AAA49627.1 .
PIRi A25896.
UniGenei Mga.4462.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DEP NMR - A 345-359 [» ]
2VT4 X-ray 2.70 A/B/C/D 33-367 [» ]
2Y00 X-ray 2.50 A/B 33-368 [» ]
2Y01 X-ray 2.60 A/B 33-368 [» ]
2Y02 X-ray 2.60 A/B 33-368 [» ]
2Y03 X-ray 2.85 A/B 33-368 [» ]
2Y04 X-ray 3.05 A/B 33-368 [» ]
2YCW X-ray 3.00 A/B 33-367 [» ]
2YCX X-ray 3.25 A/B 33-367 [» ]
2YCY X-ray 3.15 A/B 33-367 [» ]
2YCZ X-ray 3.65 A/B 33-367 [» ]
3ZPQ X-ray 2.80 A/B 33-368 [» ]
3ZPR X-ray 2.70 A/B 33-368 [» ]
4AMI X-ray 3.20 A/B 33-368 [» ]
4AMJ X-ray 2.30 A/B 33-368 [» ]
4BVN X-ray 2.10 A 33-368 [» ]
4GPO X-ray 3.50 A/B 33-368 [» ]
ProteinModelPortali P07700.
SMRi P07700. Positions 39-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60236N.

Protein family/group databases

GPCRDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG106962.

Miscellaneous databases

EvolutionaryTracei P07700.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR002233. ADR_fam.
IPR000507. ADRB1_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view ]
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR01103. ADRENERGICR.
PR00561. ADRENRGCB1AR.
PR00237. GPCRRHODOPSN.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1995) [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: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 9, 2014
This is version 108 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

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