ID   ADRB1_MERUN             Reviewed;          73 AA.
AC   O70430;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Beta-1 adrenergic receptor;
DE   AltName: Full=Beta-1 adrenoreceptor;
DE            Short=Beta-1 adrenoceptor;
DE   Flags: Fragment;
GN   Name=ADRB1;
OS   Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Meriones.
OX   NCBI_TaxID=10047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adipose tissue, Brain, and Stria vascularis;
RX   PubMed=10398761; DOI=10.1007/s002329900538;
RA   Wangemann P., Liu J., Shimozono M., Scofield M.A.;
RT   "Beta1-adrenergic receptors but not beta2-adrenergic or vasopressin
RT   receptors regulate K+ secretion in vestibular dark cells of the inner
RT   ear.";
RL   J. Membr. Biol. 170:67-77(1999).
CC   -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced
CC       activation of adenylate cyclase through the action of G proteins. This
CC       receptor binds epinephrine and norepinephrine with approximately equal
CC       affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated
CC       signaling (By similarity). In dorsal pons neurons, involved in the
CC       regulation of sleep/wake behaviors (By similarity).
CC       {ECO:0000250|UniProtKB:P08588, ECO:0000250|UniProtKB:P34971}.
CC   -!- SUBUNIT: Interacts (via C-terminus PDZ motif) with RAPGEF2; the
CC       interaction is direct. Interacts with GOPC, MAGI3 and DLG4 (By
CC       similarity). {ECO:0000250|UniProtKB:P08588}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18090};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P18090}. Early
CC       endosome {ECO:0000250}. Note=Colocalizes with RAPGEF2 at the plasma
CC       membrane. Found in the Golgi upon GOPC overexpression (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Homologous desensitization of the receptor is mediated by its
CC       phosphorylation by beta-adrenergic receptor kinase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRB1 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF055349; AAC12767.1; -; mRNA.
DR   AlphaFoldDB; O70430; -.
DR   SMR; O70430; -.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISS:UniProtKB.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor;
KW   Membrane; Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..>73
FT                   /note="Beta-1 adrenergic receptor"
FT                   /id="PRO_0000069121"
FT   TRANSMEM        <1..12
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        13..38
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        39..64
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        65..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="cyanopindolol"
FT                   /ligand_id="ChEBI:CHEBI:187894"
FT                   /ligand_note="antagonist"
FT                   /evidence="ECO:0000250|UniProtKB:P07700"
FT   DISULFID        25..31
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
FT   NON_TER         73
SQ   SEQUENCE   73 AA;  8580 MW;  655DFA29C971EF96 CRC64;
     ISALVSFLPI LMHWWRAEND EARRCYNDPK CCDFVTNRAY AIASSVVSFY VPLCIMAFVY
     LRVFREAQKQ VKK