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ADRB1_CANLF
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   25-MAY-2022, entry version 135.
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; 9612.ENSCAFP00000035025; -.
DR   PaxDb; P79148; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P79148; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004940; F:beta1-adrenergic receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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: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   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000507; ADRB1_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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   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
 
 
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