ADRB1_BOVIN
ID ADRB1_BOVIN Reviewed; 467 AA.
AC Q9TT96; Q9TUB4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Beta-1 adrenergic receptor;
DE AltName: Full=Beta-1 adrenoreceptor;
DE Short=Beta-1 adrenoceptor;
GN Name=ADRB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ha S.H., Baik M.G., Choi Y.J.;
RT "Cloning of beta adrenergic receptor from Korean cattle.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-367.
RC STRAIN=Korean; TISSUE=Adipocyte;
RA Ha S.H.;
RT "Cloning and characterization of beta adrenergic receptor from Korean
RT native cattle.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AF188187; AAF21435.1; -; Genomic_DNA.
DR EMBL; AF095852; AAF01674.1; -; Genomic_DNA.
DR RefSeq; NP_919242.1; NM_194266.1.
DR AlphaFoldDB; Q9TT96; -.
DR SMR; Q9TT96; -.
DR STRING; 9913.ENSBTAP00000001639; -.
DR PaxDb; Q9TT96; -.
DR GeneID; 281604; -.
DR KEGG; bta:281604; -.
DR CTD; 153; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9TT96; -.
DR OrthoDB; 750855at2759; -.
DR Proteomes; UP000009136; 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..467
FT /note="Beta-1 adrenergic receptor"
FT /id="PRO_0000069115"
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..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 307..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 337..341
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 342..364
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 365..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 269..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 464..467
FT /note="PDZ-Binding"
FT /evidence="ECO:0000250"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18090"
FT LIPID 380
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 131..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 209..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 122
FT /note="G -> D (in Ref. 1; AAF21435)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="R -> H (in Ref. 1; AAF21435)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="G -> R (in Ref. 1; AAF21435)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="R -> G (in Ref. 1; AAF21435)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="V -> A (in Ref. 1; AAF21435)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="P -> S (in Ref. 1; AAF21435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 50137 MW; D929E79ADDF4039F CRC64;
MGAGVLALGA SEPCNLSSAA PVPDGAATAA RLLVPASPPA SLLTSASEGP PLPSQQWTAG
MGLLMAFIVL LIVVGNVLVL VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV
WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC
TVWAISALVS FLPIFMQWWG DKDAKASRCY NDPECCDFII NEGYAITSSV VSFYVPLCIM
AFVYLRVFRE AQKQVKKIDS CERRFLSGPA RLPSPAPSPG PPLPAATVAN GRANKRRPPR
LVALREQKAL KTLGIIMGVF TLCWLPFFLA NVVKAFHRDL VPDRLFVFFN WLGYANSAFN
PIIYCRSPDF RKAFQRLLCC ARRAACGSHA AAGDPPRALG CLAVARPSPS PGAASDDDDD
DDEDDVGAAP PVRLLEPWAG YNGGAAANSD SSPDEPSRAG CASESKV
