ID   ADRB1_MOUSE             Reviewed;         466 AA.
AC   P34971; B2RVY4;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Beta-1 adrenergic receptor;
DE   AltName: Full=Beta-1 adrenoreceptor;
DE            Short=Beta-1 adrenoceptor;
GN   Name=Adrb1; Synonyms=Adrb1r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=8395893; DOI=10.1016/0167-4889(93)90209-8;
RA   Jasper J.R., Link R.E., Chruscinski A.J., Kobilka B.K., Bernstein D.;
RT   "Primary structure of the mouse beta 1-adrenergic receptor gene.";
RL   Biochim. Biophys. Acta 1178:307-309(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 303-307, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   MUTAGENESIS OF ALA-187, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=31473062; DOI=10.1016/j.neuron.2019.07.026;
RA   Shi G., Xing L., Wu D., Bhattacharyya B.J., Jones C.R., McMahon T.,
RA   Chong S.Y.C., Chen J.A., Coppola G., Geschwind D., Krystal A., Ptacek L.J.,
RA   Fu Y.H.;
RT   "A rare mutation of beta1-adrenergic receptor affects sleep/wake
RT   behaviors.";
RL   Neuron 0:0-0(2019).
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 (PubMed:31473062). {ECO:0000250|UniProtKB:P08588,
CC       ECO:0000269|PubMed:31473062}.
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   -!- INTERACTION:
CC       P34971; P18762: Adrb2; NbExp=2; IntAct=EBI-7764182, EBI-491143;
CC       P34971; Q01063: Pde4d; NbExp=3; IntAct=EBI-7764182, EBI-7764239;
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   -!- TISSUE SPECIFICITY: In brain, expressed by glutamatergic and GABAergic
CC       neurons of the dorsal pons (at protein level).
CC       {ECO:0000269|PubMed:31473062}.
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.
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; L10084; AAA02929.1; -; Genomic_DNA.
DR   EMBL; CH466585; EDL01765.1; -; Genomic_DNA.
DR   EMBL; BC140970; AAI40971.1; -; mRNA.
DR   EMBL; BC147435; AAI47436.1; -; mRNA.
DR   CCDS; CCDS29919.1; -.
DR   PIR; S36794; S36794.
DR   RefSeq; NP_031445.2; NM_007419.2.
DR   AlphaFoldDB; P34971; -.
DR   SMR; P34971; -.
DR   DIP; DIP-59567N; -.
DR   IntAct; P34971; 6.
DR   MINT; P34971; -.
DR   STRING; 10090.ENSMUSP00000040847; -.
DR   BindingDB; P34971; -.
DR   ChEMBL; CHEMBL3440; -.
DR   GlyCosmos; P34971; 1 site, No reported glycans.
DR   GlyGen; P34971; 1 site.
DR   iPTMnet; P34971; -.
DR   PhosphoSitePlus; P34971; -.
DR   PaxDb; 10090-ENSMUSP00000040847; -.
DR   ProteomicsDB; 296186; -.
DR   Antibodypedia; 31906; 357 antibodies from 37 providers.
DR   DNASU; 11554; -.
DR   Ensembl; ENSMUST00000038949.6; ENSMUSP00000040847.5; ENSMUSG00000035283.6.
DR   GeneID; 11554; -.
DR   KEGG; mmu:11554; -.
DR   UCSC; uc008hze.2; mouse.
DR   AGR; MGI:87937; -.
DR   CTD; 153; -.
DR   MGI; MGI:87937; Adrb1.
DR   VEuPathDB; HostDB:ENSMUSG00000035283; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000161953; -.
DR   HOGENOM; CLU_009579_11_0_1; -.
DR   InParanoid; P34971; -.
DR   OMA; AGTWSDC; -.
DR   OrthoDB; 2900736at2759; -.
DR   PhylomeDB; P34971; -.
DR   TreeFam; TF316350; -.
DR   Reactome; R-MMU-390696; Adrenoceptors.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 11554; 2 hits in 78 CRISPR screens.
DR   PRO; PR:P34971; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P34971; Protein.
DR   Bgee; ENSMUSG00000035283; Expressed in parotid gland and 141 other cell types or tissues.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IMP:MGI.
DR   GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0031694; F:alpha-2A adrenergic receptor binding; ISO:MGI.
DR   GO; GO:0043176; F:amine binding; ISO:MGI.
DR   GO; GO:0004940; F:beta1-adrenergic receptor activity; IDA:MGI.
DR   GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
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; IMP:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IGI:MGI.
DR   GO; GO:0002024; P:diet induced thermogenesis; IGI:MGI.
DR   GO; GO:0042596; P:fear response; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0005980; P:glycogen catabolic process; ISO:MGI.
DR   GO; GO:0031649; P:heat generation; IGI:MGI.
DR   GO; GO:0060080; P:inhibitory postsynaptic potential; ISO:MGI.
DR   GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
DR   GO; GO:0007613; P:memory; ISO:MGI.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IGI:MGI.
DR   GO; GO:0045986; P:negative regulation of smooth muscle contraction; ISO:MGI.
DR   GO; GO:0035811; P:negative regulation of urine volume; ISO:MGI.
DR   GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
DR   GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IMP:MGI.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; ISO:MGI.
DR   GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IDA:MGI.
DR   GO; GO:0003061; P:positive regulation of the force of heart contraction by norepinephrine; ISO:MGI.
DR   GO; GO:0033365; P:protein localization to organelle; ISO:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISO:MGI.
DR   GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IGI:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
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.
DR   Genevisible; P34971; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond; Endosome;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..466
FT                   /note="Beta-1 adrenergic receptor"
FT                   /id="PRO_0000069122"
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        270..286
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..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:0000250|UniProtKB:P18090"
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         187
FT                   /note="A->V: In knockin mouse model, decreases protein
FT                   levels. Mice exhibit a short sleep phenotype. Changes the
FT                   electrophysiological properties of dorsal pons neurons."
FT                   /evidence="ECO:0000269|PubMed:31473062"
FT   CONFLICT        65
FT                   /note="L -> V (in Ref. 1; AAA02929)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   466 AA;  50494 MW;  E4861E250B62F735 CRC64;
     MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS APLSQQWTAG
     MGLLLALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV
     WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC
     TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM
     AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPSPEPSPS PGPPRPADSL ANGRSSKRRP
     SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF FNWLGYANSA
     FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA SGCLARAGPP PSPGAPSDDD
     DDDAGTTPPA RLLEPWTGCN GGTTTVDSDS SLDEPGRQGF SSESKV
//