ID   ADRB1_HUMAN             Reviewed;         477 AA.
AC   P08588; B0LPE2; Q5T5Y4; Q9UKG7; Q9UKG8;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 224.
DE   RecName: Full=Beta-1 adrenergic receptor {ECO:0000305};
DE   AltName: Full=Beta-1 adrenoreceptor;
DE            Short=Beta-1 adrenoceptor;
GN   Name=ADRB1 {ECO:0000312|HGNC:HGNC:285}; Synonyms=ADRB1R, B1AR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=2825170; DOI=10.1073/pnas.84.22.7920;
RA   Frielle T., Collins S., Daniel K.W., Caron M.G., Lefkowitz R.J.,
RA   Kobilka B.K.;
RT   "Cloning of the cDNA for the human beta 1-adrenergic receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:7920-7924(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-49.
RX   PubMed=10477438;
RX   DOI=10.1002/(sici)1098-1004(1999)14:3<271::aid-humu14>3.0.co;2-q;
RA   Moore J.D., Mason D.A., Green S.A., Hsu J., Liggett S.B.;
RT   "Racial differences in the frequencies of cardiac beta(1)-adrenergic
RT   receptor polymorphisms: analysis of c145A>G and c1165G>C.";
RL   Hum. Mutat. 14:271-271(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-49.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH RAPGEF2, AND MUTAGENESIS OF SER-475 AND VAL-477.
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   [7]
RP   INTERACTION WITH GOPC AND DLG4, MUTAGENESIS OF GLU-474; SER-475; LYS-476
RP   AND VAL-477, AND SUBCELLULAR LOCATION.
RX   PubMed=15358775; DOI=10.1074/jbc.m404876200;
RA   He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.;
RT   "Interaction with cystic fibrosis transmembrane conductance regulator-
RT   associated ligand (CAL) inhibits beta1-adrenergic receptor surface
RT   expression.";
RL   J. Biol. Chem. 279:50190-50196(2004).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21540189; DOI=10.1074/jbc.m111.224071;
RA   Cheng S.B., Quinn J.A., Graeber C.T., Filardo E.J.;
RT   "Down-modulation of the G-protein-coupled estrogen receptor, GPER, from the
RT   cell surface occurs via a trans-Golgi-proteasome pathway.";
RL   J. Biol. Chem. 286:22441-22455(2011).
RN   [9]
RP   VARIANT ARG-389, AND CHARACTERIZATION OF VARIANT ARG-389.
RX   PubMed=10212248; DOI=10.1074/jbc.274.18.12670;
RA   Mason D.A., Moore J.D., Green S.A., Liggett S.B.;
RT   "A gain-of-function polymorphism in a G-protein coupling domain of the
RT   human beta1-adrenergic receptor.";
RL   J. Biol. Chem. 274:12670-12674(1999).
RN   [10]
RP   VARIANT GLY-49.
RX   PubMed=11052857; DOI=10.1053/euhj.1999.1994;
RA   Borjesson M., Magnusson Y., Hjalmarson A., Andersson B.;
RT   "A novel polymorphism in the gene coding for the beta(1)-adrenergic
RT   receptor associated with survival in patients with heart failure.";
RL   Eur. Heart J. 21:1853-1858(2000).
RN   [11]
RP   VARIANT GLY-49, AND POLYMORPHISM.
RX   PubMed=11854867; DOI=10.1086/339621;
RA   Ranade K., Jorgenson E., Sheu W.H.-H., Pei D., Hsiung C.A., Chiang F.-T.,
RA   Chen Y.-D.I., Pratt R., Olshen R.A., Curb D., Cox D.R., Botstein D.,
RA   Risch N.;
RT   "A polymorphism in the beta1 adrenergic receptor is associated with resting
RT   heart rate.";
RL   Am. J. Hum. Genet. 70:935-942(2002).
RN   [12]
RP   VARIANT VAL-187, CHARACTERIZATION OF VARIANT VAL-187, FUNCTION, AND
RP   POLYMORPHISM.
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. Involved in the regulation of sleep/wake behaviors
CC       (PubMed:31473062). {ECO:0000269|PubMed:12391161,
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.
CC       {ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:15358775}.
CC   -!- INTERACTION:
CC       P08588; P30542: ADORA1; NbExp=5; IntAct=EBI-991009, EBI-2903663;
CC       P08588; Q86UL8: MAGI2; NbExp=3; IntAct=EBI-991009, EBI-311035;
CC       P08588; Q5TCQ9: MAGI3; NbExp=5; IntAct=EBI-991009, EBI-310506;
CC       P08588; P31016: Dlg4; Xeno; NbExp=2; IntAct=EBI-991009, EBI-375655;
CC       P08588; P14270: Pde4d; Xeno; NbExp=2; IntAct=EBI-991009, EBI-8333209;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18090};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P18090}. Early
CC       endosome. Note=Colocalizes with RAPGEF2 at the plasma membrane (By
CC       similarity). Localized at the plasma membrane. Found in the Golgi upon
CC       GOPC overexpression. {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.
CC   -!- PTM: Homologous desensitization of the receptor is mediated by its
CC       phosphorylation by beta-adrenergic receptor kinase.
CC   -!- POLYMORPHISM: Genetic variations in ADRB1 are associated with inter-
CC       individual variability in the resting heart rate. This quantitative
CC       trait has been significantly correlated with cardiovascular morbidity
CC       and mortality [MIM:607276]. {ECO:0000269|PubMed:11854867}.
CC   -!- POLYMORPHISM: Genetic variations in ADRB1 are associated with the
CC       familial natural short sleep 2 (FNSS2) phenotype, an autosomal dominant
CC       trait [MIM:618591]. Individuals with this trait require less sleep in
CC       any 24-hour period than is typical for their age group.
CC       {ECO:0000269|PubMed:31473062}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRB1 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/adrb1/";
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DR   EMBL; J03019; AAA51667.1; -; mRNA.
DR   EMBL; AF169006; AAD53696.1; -; Genomic_DNA.
DR   EMBL; AF169007; AAD53697.1; -; Genomic_DNA.
DR   EMBL; AY567837; AAS66983.1; -; Genomic_DNA.
DR   EMBL; EU332832; ABY87521.1; -; Genomic_DNA.
DR   EMBL; AL355543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS7586.1; -.
DR   PIR; A39911; QRHUB1.
DR   RefSeq; NP_000675.1; NM_000684.2.
DR   PDB; 2LSQ; NMR; -; A=197-221.
DR   PDB; 7BTS; X-ray; 3.13 A; A=54-399.
DR   PDB; 7BU6; X-ray; 2.70 A; A=54-399.
DR   PDB; 7BU7; X-ray; 2.60 A; A=54-399.
DR   PDB; 7BVQ; X-ray; 2.50 A; A/B=54-399.
DR   PDBsum; 2LSQ; -.
DR   PDBsum; 7BTS; -.
DR   PDBsum; 7BU6; -.
DR   PDBsum; 7BU7; -.
DR   PDBsum; 7BVQ; -.
DR   AlphaFoldDB; P08588; -.
DR   SMR; P08588; -.
DR   BioGRID; 106662; 10.
DR   CORUM; P08588; -.
DR   DIP; DIP-36294N; -.
DR   IntAct; P08588; 14.
DR   MINT; P08588; -.
DR   STRING; 9606.ENSP00000358301; -.
DR   BindingDB; P08588; -.
DR   ChEMBL; CHEMBL213; -.
DR   DrugBank; DB08558; 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL.
DR   DrugBank; DB08347; 4-{[(2S)-3-(tert-butylamino)-2-hydroxypropyl]oxy}-3H-indole-2-carbonitrile.
DR   DrugBank; DB01193; Acebutolol.
DR   DrugBank; DB00866; Alprenolol.
DR   DrugBank; DB01118; Amiodarone.
DR   DrugBank; DB00182; Amphetamine.
DR   DrugBank; DB01102; Arbutamine.
DR   DrugBank; DB01238; Aripiprazole.
DR   DrugBank; DB09204; Arotinolol.
DR   DrugBank; DB06216; Asenapine.
DR   DrugBank; DB00335; Atenolol.
DR   DrugBank; DB09013; Befunolol.
DR   DrugBank; DB00195; Betaxolol.
DR   DrugBank; DB00217; Bethanidine.
DR   DrugBank; DB01295; Bevantolol.
DR   DrugBank; DB00612; Bisoprolol.
DR   DrugBank; DB08807; Bopindolol.
DR   DrugBank; DB06726; Bufuralol.
DR   DrugBank; DB08808; Bupranolol.
DR   DrugBank; DB00248; Cabergoline.
DR   DrugBank; DB00521; Carteolol.
DR   DrugBank; DB01136; Carvedilol.
DR   DrugBank; DB04846; Celiprolol.
DR   DrugBank; DB01407; Clenbuterol.
DR   DrugBank; DB00785; Cryptenamine.
DR   DrugBank; DB01151; Desipramine.
DR   DrugBank; DB11273; Dihydroergocornine.
DR   DrugBank; DB13345; Dihydroergocristine.
DR   DrugBank; DB11278; DL-Methylephedrine.
DR   DrugBank; DB00841; Dobutamine.
DR   DrugBank; DB04855; Dronedarone.
DR   DrugBank; DB06262; Droxidopa.
DR   DrugBank; DB01363; Ephedra sinica root.
DR   DrugBank; DB01364; Ephedrine.
DR   DrugBank; DB00668; Epinephrine.
DR   DrugBank; DB01049; Ergoloid mesylate.
DR   DrugBank; DB00187; Esmolol.
DR   DrugBank; DB01288; Fenoterol.
DR   DrugBank; DB00983; Formoterol.
DR   DrugBank; DB00221; Isoetharine.
DR   DrugBank; DB01064; Isoprenaline.
DR   DrugBank; DB00598; Labetalol.
DR   DrugBank; DB00555; Lamotrigine.
DR   DrugBank; DB09351; Levobetaxolol.
DR   DrugBank; DB01210; Levobunolol.
DR   DrugBank; DB00408; Loxapine.
DR   DrugBank; DB01365; Mephentermine.
DR   DrugBank; DB01214; Metipranolol.
DR   DrugBank; DB00264; Metoprolol.
DR   DrugBank; DB08893; Mirabegron.
DR   DrugBank; DB01203; Nadolol.
DR   DrugBank; DB04861; Nebivolol.
DR   DrugBank; DB00368; Norepinephrine.
DR   DrugBank; DB00540; Nortriptyline.
DR   DrugBank; DB00334; Olanzapine.
DR   DrugBank; DB01580; Oxprenolol.
DR   DrugBank; DB00715; Paroxetine.
DR   DrugBank; DB01359; Penbutolol.
DR   DrugBank; DB00397; Phenylpropanolamine.
DR   DrugBank; DB00960; Pindolol.
DR   DrugBank; DB01291; Pirbuterol.
DR   DrugBank; DB01297; Practolol.
DR   DrugBank; DB01182; Propafenone.
DR   DrugBank; DB00571; Propranolol.
DR   DrugBank; DB00852; Pseudoephedrine.
DR   DrugBank; DB01917; Putrescine.
DR   DrugBank; DB11124; Racepinephrine.
DR   DrugBank; DB00243; Ranolazine.
DR   DrugBank; DB00867; Ritodrine.
DR   DrugBank; DB01001; Salbutamol.
DR   DrugBank; DB00938; Salmeterol.
DR   DrugBank; DB00489; Sotalol.
DR   DrugBank; DB03566; Spermidine.
DR   DrugBank; DB00127; Spermine.
DR   DrugBank; DB00871; Terbutaline.
DR   DrugBank; DB00373; Timolol.
DR   DrugBank; DB00726; Trimipramine.
DR   DrugBank; DB09068; Vortioxetine.
DR   DrugBank; DB13781; Xamoterol.
DR   DrugCentral; P08588; -.
DR   GuidetoPHARMACOLOGY; 28; -.
DR   TCDB; 9.A.14.3.11; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; P08588; 1 site, No reported glycans.
DR   GlyGen; P08588; 1 site.
DR   iPTMnet; P08588; -.
DR   PhosphoSitePlus; P08588; -.
DR   SwissPalm; P08588; -.
DR   BioMuta; ADRB1; -.
DR   DMDM; 48429211; -.
DR   jPOST; P08588; -.
DR   PaxDb; 9606-ENSP00000358301; -.
DR   PeptideAtlas; P08588; -.
DR   ABCD; P08588; 1 sequenced antibody.
DR   Antibodypedia; 31906; 357 antibodies from 37 providers.
DR   DNASU; 153; -.
DR   Ensembl; ENST00000369295.4; ENSP00000358301.2; ENSG00000043591.6.
DR   GeneID; 153; -.
DR   KEGG; hsa:153; -.
DR   MANE-Select; ENST00000369295.4; ENSP00000358301.2; NM_000684.3; NP_000675.1.
DR   UCSC; uc001lba.4; human.
DR   AGR; HGNC:285; -.
DR   CTD; 153; -.
DR   DisGeNET; 153; -.
DR   GeneCards; ADRB1; -.
DR   HGNC; HGNC:285; ADRB1.
DR   HPA; ENSG00000043591; Tissue enhanced (heart muscle, lung, placenta).
DR   MalaCards; ADRB1; -.
DR   MIM; 109630; gene.
DR   MIM; 607276; phenotype.
DR   neXtProt; NX_P08588; -.
DR   OpenTargets; ENSG00000043591; -.
DR   PharmGKB; PA38; -.
DR   VEuPathDB; HostDB:ENSG00000043591; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000161953; -.
DR   HOGENOM; CLU_009579_11_0_1; -.
DR   InParanoid; P08588; -.
DR   OrthoDB; 2900736at2759; -.
DR   PhylomeDB; P08588; -.
DR   TreeFam; TF316350; -.
DR   PathwayCommons; P08588; -.
DR   Reactome; R-HSA-390696; Adrenoceptors.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   SignaLink; P08588; -.
DR   SIGNOR; P08588; -.
DR   BioGRID-ORCS; 153; 13 hits in 1154 CRISPR screens.
DR   GeneWiki; Beta-1_adrenergic_receptor; -.
DR   GenomeRNAi; 153; -.
DR   Pharos; P08588; Tclin.
DR   PRO; PR:P08588; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P08588; Protein.
DR   Bgee; ENSG00000043591; Expressed in heart right ventricle and 140 other cell types or tissues.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0098992; C:neuronal dense core vesicle; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0031694; F:alpha-2A adrenergic receptor binding; IPI:BHF-UCL.
DR   GO; GO:0004939; F:beta-adrenergic receptor activity; TAS:ProtInc.
DR   GO; GO:0004940; F:beta1-adrenergic receptor activity; IDA:UniProtKB.
DR   GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR   GO; GO:0042596; P:fear response; IEA:Ensembl.
DR   GO; GO:0031649; P:heat generation; IEA:Ensembl.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IBA:GO_Central.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IBA:GO_Central.
DR   GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IEA:Ensembl.
DR   GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEA:Ensembl.
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; P08588; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; 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..477
FT                   /note="Beta-1 adrenergic receptor"
FT                   /id="PRO_0000069118"
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..319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        320..349
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        350..354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        355..377
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        378..477
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          269..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           474..477
FT                   /note="PDZ-Binding"
FT   COMPBIAS        270..294
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         312
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         412
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18090"
FT   LIPID           392
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   VARIANT         26
FT                   /note="A -> V (in dbSNP:rs34844626)"
FT                   /id="VAR_055909"
FT   VARIANT         29
FT                   /note="A -> T (in dbSNP:rs35720093)"
FT                   /id="VAR_055910"
FT   VARIANT         31
FT                   /note="R -> Q (in dbSNP:rs35230616)"
FT                   /id="VAR_055911"
FT   VARIANT         49
FT                   /note="S -> G (correlated with low mean resting heart rate
FT                   and decreased mortality risk in patients with congestive
FT                   heart failure; dbSNP:rs1801252)"
FT                   /evidence="ECO:0000269|PubMed:10477438,
FT                   ECO:0000269|PubMed:11052857, ECO:0000269|PubMed:11854867,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_009879"
FT   VARIANT         187
FT                   /note="A -> V (found in individuals with short sleep;
FT                   results in decreased adenylate cyclase-activating
FT                   adrenergic receptor signaling; decreased protein stability;
FT                   dbSNP:rs776439595)"
FT                   /evidence="ECO:0000269|PubMed:31473062"
FT                   /id="VAR_082587"
FT   VARIANT         389
FT                   /note="G -> R (increased beta1-adrenergic receptor
FT                   activity; increased basal activity and increased coupling
FT                   to heterotrimeric G protein Gs that stimulates the adenylyl
FT                   cyclase; dbSNP:rs1801253)"
FT                   /evidence="ECO:0000269|PubMed:10212248"
FT                   /id="VAR_009880"
FT   VARIANT         399
FT                   /note="R -> H (in dbSNP:rs36052953)"
FT                   /id="VAR_055912"
FT   VARIANT         405
FT                   /note="H -> Y (in dbSNP:rs35705839)"
FT                   /id="VAR_055913"
FT   MUTAGEN         474
FT                   /note="E->A,D: Loss of interaction with GOPC."
FT                   /evidence="ECO:0000269|PubMed:15358775"
FT   MUTAGEN         474
FT                   /note="E->K: Loss of interaction with GOPC; when associated
FT                   with A-477."
FT                   /evidence="ECO:0000269|PubMed:15358775"
FT   MUTAGEN         475
FT                   /note="S->A: Loss of interaction with GOPC. Loss of
FT                   interaction with RAPGEF2. Abolishes agonist-induced Ras
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:12391161,
FT                   ECO:0000269|PubMed:15358775"
FT   MUTAGEN         475
FT                   /note="S->D: Loss of interaction with RAPGEF2."
FT                   /evidence="ECO:0000269|PubMed:12391161,
FT                   ECO:0000269|PubMed:15358775"
FT   MUTAGEN         475
FT                   /note="S->T: Partial loss of interaction with GOPC."
FT                   /evidence="ECO:0000269|PubMed:12391161,
FT                   ECO:0000269|PubMed:15358775"
FT   MUTAGEN         476
FT                   /note="K->A: Partial loss of interaction with GOPC."
FT                   /evidence="ECO:0000269|PubMed:15358775"
FT   MUTAGEN         477
FT                   /note="V->A,F,L,I,M: Loss of interaction with GOPC."
FT                   /evidence="ECO:0000269|PubMed:12391161,
FT                   ECO:0000269|PubMed:15358775"
FT   MUTAGEN         477
FT                   /note="V->A: Loss of interaction with RAPGEF2. Abolishes
FT                   agonist-induced Ras activation."
FT                   /evidence="ECO:0000269|PubMed:12391161,
FT                   ECO:0000269|PubMed:15358775"
FT   HELIX           54..85
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           92..110
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           112..121
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           127..161
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           163..169
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           172..195
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   TURN            196..199
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           204..210
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:2LSQ"
FT   HELIX           222..232
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           234..253
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           316..349
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           351..353
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           356..377
FT                   /evidence="ECO:0007829|PDB:7BVQ"
FT   HELIX           381..391
FT                   /evidence="ECO:0007829|PDB:7BVQ"
SQ   SEQUENCE   477 AA;  51224 MW;  1D15E6390B5364B8 CRC64;
     MGAGVLVLGA SEPGNLSSAA PLPDGAATAA RLLVPASPPA SLLPPASESP EPLSQQWTAG
     MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV
     WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARGLVC
     TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM
     AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPSPSPSPV PAPAPPPGPP RPAAAAATAP
     LANGRAGKRR PSRLVALREQ KALKTLGIIM GVFTLCWLPF FLANVVKAFH RELVPDRLFV
     FFNWLGYANS AFNPIIYCRS PDFRKAFQGL LCCARRAARR RHATHGDRPR ASGCLARPGP
     PPSPGAASDD DDDDVVGATP PARLLEPWAG CNGGAAADSD SSLDEPCRPG FASESKV
//