P34971 (ADRB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 115.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Beta-1 adrenergic receptor Alternative name(s): Beta-1 adrenoreceptor Short name=Beta-1 adrenoceptor | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
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 By similarity. |
| 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 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 466 | 466 | Beta-1 adrenergic receptor | PRO_0000069122 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 55 | 55 | Extracellular By similarity | ||||||||
| Transmembrane | 56 – 84 | 29 | Helical; Name=1; By similarity | ||||||||
| Topological domain | 85 – 93 | 9 | Cytoplasmic By similarity | ||||||||
| Transmembrane | 94 – 120 | 27 | Helical; Name=2; By similarity | ||||||||
| Topological domain | 121 – 132 | 12 | Extracellular By similarity | ||||||||
| Transmembrane | 133 – 154 | 22 | Helical; Name=3; By similarity | ||||||||
| Topological domain | 155 – 172 | 18 | Cytoplasmic By similarity | ||||||||
| Transmembrane | 173 – 196 | 24 | Helical; Name=4; By similarity | ||||||||
| Topological domain | 197 – 222 | 26 | Extracellular By similarity | ||||||||
| Transmembrane | 223 – 248 | 26 | Helical; Name=5; By similarity | ||||||||
| Topological domain | 249 – 308 | 60 | Cytoplasmic By similarity | ||||||||
| Transmembrane | 309 – 338 | 30 | Helical; Name=6; By similarity | ||||||||
| Topological domain | 339 – 343 | 5 | Extracellular By similarity | ||||||||
| Transmembrane | 344 – 366 | 23 | Helical; Name=7; By similarity | ||||||||
| Topological domain | 367 – 466 | 100 | Cytoplasmic By similarity | ||||||||
| Region | 218 – 232 | 15 | Agonist and antagonist binding By similarity | ||||||||
| Region | 326 – 333 | 8 | Agonist and antagonist binding By similarity | ||||||||
| Region | 352 – 356 | 5 | Agonist and antagonist binding By similarity | ||||||||
| Motif | 463 – 466 | 4 | PDZ-Binding By similarity | ||||||||
Sites | |||||||||||
| Binding site | 138 | 1 | Agonist or antagonist By similarity | ||||||||
| Binding site | 143 | 1 | Agonist or antagonist By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 296 | 1 | Phosphoserine; by PKA Potential | ||||||||
| Modified residue | 301 | 1 | Phosphoserine; by PKA Potential | ||||||||
| Modified residue | 401 | 1 | Phosphoserine; by PKA Potential | ||||||||
| Lipidation | 381 | 1 | S-palmitoyl cysteine By similarity | ||||||||
| Glycosylation | 15 | 1 | N-linked (GlcNAc...) Probable | ||||||||
| Disulfide bond | 131 ↔ 216 | By similarity | |||||||||
| Disulfide bond | 209 ↔ 215 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 65 | 1 | L → V in AAA02929. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure of the mouse beta 1-adrenergic receptor gene." Jasper J.R., Link R.E., Chruscinski A.J., Kobilka B.K., Bernstein D. Biochim. Biophys. Acta 1178:307-309(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv. |
| [2] | Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [4] | Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 303-307, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L10084 Genomic DNA. Translation: AAA02929.1. CH466585 Genomic DNA. Translation: EDL01765.1. BC140970 mRNA. Translation: AAI40971.1. BC147435 mRNA. Translation: AAI47436.1. |
| IPI | IPI00119827. |
| PIR | S36794. |
| RefSeq | NP_031445.2. NM_007419.2. |
| UniGene | Mm.46797. |
3D structure databases | |
| ProteinModelPortal | P34971. |
| SMR | P34971. Positions 53-380. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-59567N. |
| STRING | 10090.ENSMUSP00000040847. |
Protein family/group databases | |
| GPCRDB | Search... |
PTM databases | |
| PhosphoSite | P34971. |
Proteomic databases | |
| PRIDE | P34971. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000038949; ENSMUSP00000040847; ENSMUSG00000035283. |
| GeneID | 11554. |
| KEGG | mmu:11554. |
Organism-specific databases | |
| CTD | 153. |
| MGI | MGI:87937. Adrb1. |
Phylogenomic databases | |
| eggNOG | NOG262978. |
| GeneTree | ENSGT00680000099833. |
| HOGENOM | HOG000239242. |
| HOVERGEN | HBG106962. |
| InParanoid | B2RVY4. |
| KO | K04141. |
| OMA | DRPRASG. |
| OrthoDB | EOG4WQ12W. |
Gene expression databases | |
| Bgee | P34971. |
| CleanEx | MM_ADRB1. |
| Genevestigator | P34971. |
| GermOnline | ENSMUSG00000035283. Mus musculus. |
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 | P34971. |
| ChEMBL | CHEMBL3440. |
| NextBio | 279050. |
| SOURCE | Search... |
Entry information
| Entry name | ADRB1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P34971 Secondary accession number(s): B2RVY4 | ||||||||
| Entry history |
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| 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 |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
