ADRB1_RAT
ID ADRB1_RAT Reviewed; 466 AA.
AC P18090;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 182.
DE RecName: Full=Beta-1 adrenergic receptor;
DE AltName: Full=Beta-1 adrenoreceptor;
DE Short=Beta-1 adrenoceptor;
GN Name=Adrb1; Synonyms=Adrb1r;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1695899; DOI=10.1016/s0021-9258(19)38253-5;
RA Machida C.A., Bunzow J.R., Searles R.P., van Tol H.H.M., Tester B.,
RA Neve K.A., Teal P., Nipper V., Civelli O.;
RT "Molecular cloning and expression of the rat beta 1-adrenergic receptor
RT gene.";
RL J. Biol. Chem. 265:12960-12965(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2167473; DOI=10.1093/nar/18.15.4591;
RA Shimomura H., Terada A.;
RT "Primary structure of the rat beta-1 adrenergic receptor gene.";
RL Nucleic Acids Res. 18:4591-4591(1990).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12391161; DOI=10.1128/mcb.22.22.7942-7952.2002;
RA Pak Y., Pham N., Rotin D.;
RT "Direct binding of the beta1 adrenergic receptor to the cyclic AMP-
RT dependent guanine nucleotide exchange factor CNrasGEF leads to Ras
RT activation.";
RL Mol. Cell. Biol. 22:7942-7952(2002).
RN [4]
RP INTERACTION WITH MAGI3, AND MUTAGENESIS OF VAL-466.
RX PubMed=16316992; DOI=10.1074/jbc.m509503200;
RA He J., Bellini M., Inuzuka H., Xu J., Xiong Y., Yang X., Castleberry A.M.,
RA Hall R.A.;
RT "Proteomic analysis of beta1-adrenergic receptor interactions with PDZ
RT scaffold proteins.";
RL J. Biol. Chem. 281:2820-2827(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Interacts with GOPC, MAGI3 and
CC DLG4. {ECO:0000250, ECO:0000269|PubMed:16316992}.
CC -!- INTERACTION:
CC P18090; Q9JK71: Magi3; NbExp=3; IntAct=EBI-991303, EBI-696226;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12391161};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12391161}. Early
CC endosome {ECO:0000250}. Note=Localized at the plasma membrane. Found in
CC the Golgi upon GOPC overexpression (By similarity). Colocalizes with
CC RAPGEF2 at the plasma membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cortical neurons and coronary artery
CC smooth muscle cells (at protein level). {ECO:0000269|PubMed:12391161}.
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.
CC -!- PTM: Homologous desensitization of the receptor is mediated by its
CC phosphorylation by beta-adrenergic receptor kinase.
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; J05561; AAA40792.1; -; Genomic_DNA.
DR EMBL; D00634; BAA00527.1; -; Genomic_DNA.
DR PIR; S12591; S12591.
DR RefSeq; NP_036833.1; NM_012701.1.
DR AlphaFoldDB; P18090; -.
DR SMR; P18090; -.
DR DIP; DIP-36293N; -.
DR IntAct; P18090; 2.
DR STRING; 10116.ENSRNOP00000022813; -.
DR BindingDB; P18090; -.
DR ChEMBL; CHEMBL3252; -.
DR DrugCentral; P18090; -.
DR GlyGen; P18090; 1 site.
DR iPTMnet; P18090; -.
DR PhosphoSitePlus; P18090; -.
DR PaxDb; P18090; -.
DR GeneID; 24925; -.
DR KEGG; rno:24925; -.
DR UCSC; RGD:2059; rat.
DR CTD; 153; -.
DR RGD; 2059; Adrb1.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P18090; -.
DR OrthoDB; 750855at2759; -.
DR PhylomeDB; P18090; -.
DR TreeFam; TF316350; -.
DR Reactome; R-RNO-390696; Adrenoceptors.
DR PRO; PR:P18090; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0031694; F:alpha-2A adrenergic receptor binding; ISO:RGD.
DR GO; GO:0043176; F:amine binding; IPI:RGD.
DR GO; GO:0004940; F:beta1-adrenergic receptor activity; IDA:RGD.
DR GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
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:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IDA:RGD.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0002024; P:diet induced thermogenesis; ISO:RGD.
DR GO; GO:0042596; P:fear response; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:RGD.
DR GO; GO:0031649; P:heat generation; ISO:RGD.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:RGD.
DR GO; GO:0055088; P:lipid homeostasis; IMP:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0045986; P:negative regulation of smooth muscle contraction; IMP:RGD.
DR GO; GO:0035811; P:negative regulation of urine volume; IDA:RGD.
DR GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IMP:RGD.
DR GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IDA:RGD.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IDA:RGD.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
DR GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; ISO:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IDA:RGD.
DR GO; GO:1900135; P:positive regulation of renin secretion into blood stream; IMP:RGD.
DR GO; GO:0046878; P:positive regulation of saliva secretion; IMP:RGD.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:RGD.
DR GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; ISO:RGD.
DR GO; GO:0003061; P:positive regulation of the force of heart contraction by norepinephrine; IDA:RGD.
DR GO; GO:0033365; P:protein localization to organelle; IDA:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:RGD.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IDA:RGD.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISS:UniProtKB.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR GO; GO:0042060; P:wound healing; IMP:RGD.
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 1: Evidence at protein level;
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..466
FT /note="Beta-1 adrenergic receptor"
FT /id="PRO_0000069124"
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..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 309..338
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 339..343
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 344..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 367..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 264..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 463..466
FT /note="PDZ-Binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 268..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 301
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 401
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 381
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"
FT MUTAGEN 466
FT /note="V->A: Abolishes interaction with MAGI3."
FT /evidence="ECO:0000269|PubMed:16316992"
FT CONFLICT 162
FT /note="L -> S (in Ref. 2; BAA00527)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="T -> S (in Ref. 2; BAA00527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 50472 MW; 2955CB024944A12B CRC64;
MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS APLSQQWTAG
MGLLLALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV
WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TLPFRYQSLL TRARARALVC
TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM
AFVYLRVFRE AQKQVKKIDS CERRFLTGPP RPPSPAPSPS PGPPRPADSL ANGRSSKRRP
SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF FNWLGYANSA
FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA SGCLARAGPP PSPGAPSDDD
DDDAGATPPA RLLEPWAGCN GGTTTVDSDS SLDEPGRQGF SSESKV
