ID ADRB1_CANLF Reviewed; 473 AA.
AC P79148;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Beta-1 adrenergic receptor;
DE AltName: Full=Beta-1 adrenoreceptor;
DE Short=Beta-1 adrenoceptor;
GN Name=ADRB1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9220370; DOI=10.3109/10799899709039152;
RA Huang R.-R.C., Rapoport D., Schaeffer M.-T., Cascieri M.A., Fong T.M.;
RT "Molecular cloning of the dog beta 1 and beta 2 adrenergic receptors.";
RL J. Recept. Signal Transduct. 17:599-607(1997).
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). Involved in the regulation of sleep/wake
CC behaviors (By similarity). {ECO:0000250|UniProtKB:P08588,
CC 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 -!- DOMAIN: The PDZ domain-binding motif mediates competitive interactions
CC with GOPC, MAGI3 and DLG4 and plays a role in subcellular location of
CC the receptor. {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; U73207; AAB93648.1; -; Genomic_DNA.
DR AlphaFoldDB; P79148; -.
DR SMR; P79148; -.
DR STRING; 9615.ENSCAFP00000035025; -.
DR GlyCosmos; P79148; 1 site, No reported glycans.
DR PaxDb; 9612-ENSCAFP00000035025; -.
DR Ensembl; ENSCAFT00805030605; ENSCAFP00805024009; ENSCAFG00805016891.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P79148; -.
DR Proteomes; UP000002254; Unplaced.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Unplaced.
DR Proteomes; UP000805418; Unplaced.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004940; F:beta1-adrenergic receptor activity; ISS:UniProtKB.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IBA:GO_Central.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISS:UniProtKB.
DR CDD; cd15958; 7tmA_Beta1_AR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000507; ADRB1_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24248:SF54; BETA-1 ADRENERGIC RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00561; ADRENRGCB1AR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Beta-1 adrenergic receptor"
FT /id="PRO_0000069116"
FT TOPO_DOM 1..55
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 56..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 85..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 94..120
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 121..132
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 133..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 155..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 197..222
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 223..248
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 249..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 317..346
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 347..351
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 352..374
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 375..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 270..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 470..473
FT /note="PDZ-Binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 270..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18090"
FT LIPID 389
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 131..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 209..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 473 AA; 50061 MW; 361357F7DF9DBD7E CRC64;
MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVPASPSA SPLAPTSEGP APLSQQWTAG
IGLLMALIVL LIVAGNVLVI AAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVM
RGRWEYGSFL CELWTSVDVL CVTASIETLC VIALDRYLAI TAPFRYQSLL TRARARALVC
TVWAISALVS FLPILMHWWR AGGDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM
AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPAPPPAPA PAPPPAPGSP RPAAAAPLAN
GRVGRRRPSR LVALREQKAL KTLGIIMGVF TLCWLPFFLA NVVKAFHRDL VPDRLFVFFN
WLGYANSAFN PIIYCRSPDF RRAFQRLLCC ARRAARGSHG AAGDPPRARP PPSPGAASDD
DDDDEDDAGA GAGAAPPARL LEPWAGCNGG AAADSDSSLD GAGSPAGASE SRV
//
