P34971 · ADRB1_MOUSE
- ProteinBeta-1 adrenergic receptor
- GeneAdrb1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling (By similarity).
Involved in the regulation of sleep/wake behaviors (PubMed:31473062).
Involved in the regulation of sleep/wake behaviors (PubMed:31473062).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-1 adrenergic receptor
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP34971
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Colocalizes with RAPGEF2 at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-55 | Extracellular | ||||
Sequence: MGAGALALGASEPCNLSSAAPLPDGAATAARLLVLASPPASLLPPASEGSAPLSQ | ||||||
Transmembrane | 56-84 | Helical; Name=1 | ||||
Sequence: QWTAGMGLLLALIVLLIVVGNVLVIVAIA | ||||||
Topological domain | 85-93 | Cytoplasmic | ||||
Sequence: KTPRLQTLT | ||||||
Transmembrane | 94-120 | Helical; Name=2 | ||||
Sequence: NLFIMSLASADLVMGLLVVPFGATIVV | ||||||
Topological domain | 121-132 | Extracellular | ||||
Sequence: WGRWEYGSFFCE | ||||||
Transmembrane | 133-154 | Helical; Name=3 | ||||
Sequence: LWTSVDVLCVTASIETLCVIAL | ||||||
Topological domain | 155-172 | Cytoplasmic | ||||
Sequence: DRYLAITSPFRYQSLLTR | ||||||
Transmembrane | 173-196 | Helical; Name=4 | ||||
Sequence: ARARALVCTVWAISALVSFLPILM | ||||||
Topological domain | 197-222 | Extracellular | ||||
Sequence: HWWRAESDEARRCYNDPKCCDFVTNR | ||||||
Transmembrane | 223-248 | Helical; Name=5 | ||||
Sequence: AYAIASSVVSFYVPLCIMAFVYLRVF | ||||||
Topological domain | 249-308 | Cytoplasmic | ||||
Sequence: REAQKQVKKIDSCERRFLGGPARPPSPEPSPSPGPPRPADSLANGRSSKRRPSRLVALRE | ||||||
Transmembrane | 309-338 | Helical; Name=6 | ||||
Sequence: QKALKTLGIIMGVFTLCWLPFFLANVVKAF | ||||||
Topological domain | 339-343 | Extracellular | ||||
Sequence: HRDLV | ||||||
Transmembrane | 344-366 | Helical; Name=7 | ||||
Sequence: PDRLFVFFNWLGYANSAFNPIIY | ||||||
Topological domain | 367-466 | Cytoplasmic | ||||
Sequence: CRSPDFRKAFQRLLCCARRAACRRRAAHGDRPRASGCLARAGPPPSPGAPSDDDDDDAGTTPPARLLEPWTGCNGGTTTVDSDSSLDEPGRQGFSSESKV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 187 | In knockin mouse model, decreases protein levels. Mice exhibit a short sleep phenotype. Changes the electrophysiological properties of dorsal pons neurons. | ||||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000069122 | 1-466 | Beta-1 adrenergic receptor | |||
Sequence: MGAGALALGASEPCNLSSAAPLPDGAATAARLLVLASPPASLLPPASEGSAPLSQQWTAGMGLLLALIVLLIVVGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARALVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPEPSPSPGPPRPADSLANGRSSKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRDLVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAACRRRAAHGDRPRASGCLARAGPPPSPGAPSDDDDDDAGTTPPARLLEPWTGCNGGTTTVDSDSSLDEPGRQGFSSESKV | ||||||
Glycosylation | 15 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 131↔216 | |||||
Sequence: CELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARALVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCC | ||||||
Disulfide bond | 209↔215 | |||||
Sequence: CYNDPKC | ||||||
Modified residue | 296 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 301 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Lipidation | 381 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 401 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 417 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
In brain, expressed by glutamatergic and GABAergic neurons of the dorsal pons (at protein level).
Gene expression databases
Interaction
Subunit
Interacts (via C-terminus PDZ motif) with RAPGEF2; the interaction is direct. Interacts with GOPC, MAGI3 and DLG4 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P34971 | Adrb2 P18762 | 2 | EBI-7764182, EBI-491143 | |
BINARY | P34971 | Pde4d Q01063 | 3 | EBI-7764182, EBI-7764239 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 264-302 | Disordered | ||||
Sequence: RFLGGPARPPSPEPSPSPGPPRPADSLANGRSSKRRPSR | ||||||
Compositional bias | 270-286 | Pro residues | ||||
Sequence: ARPPSPEPSPSPGPPRP | ||||||
Region | 398-466 | Disordered | ||||
Sequence: PRASGCLARAGPPPSPGAPSDDDDDDAGTTPPARLLEPWTGCNGGTTTVDSDSSLDEPGRQGFSSESKV | ||||||
Compositional bias | 438-466 | Polar residues | ||||
Sequence: GCNGGTTTVDSDSSLDEPGRQGFSSESKV | ||||||
Motif | 463-466 | PDZ-Binding | ||||
Sequence: ESKV |
Domain
The PDZ domain-binding motif mediates competitive interactions with GOPC, MAGI3 and DLG4 and plays a role in subcellular location of the receptor.
Sequence similarities
Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)50,494
- Last updated2011-07-27 v2
- ChecksumE4861E250B62F735
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 65 | in Ref. 1; AAA02929 | ||||
Sequence: L → V | ||||||
Compositional bias | 270-286 | Pro residues | ||||
Sequence: ARPPSPEPSPSPGPPRP | ||||||
Compositional bias | 438-466 | Polar residues | ||||
Sequence: GCNGGTTTVDSDSSLDEPGRQGFSSESKV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L10084 EMBL· GenBank· DDBJ | AAA02929.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH466585 EMBL· GenBank· DDBJ | EDL01765.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC140970 EMBL· GenBank· DDBJ | AAI40971.1 EMBL· GenBank· DDBJ | mRNA | ||
BC147435 EMBL· GenBank· DDBJ | AAI47436.1 EMBL· GenBank· DDBJ | mRNA |