ADRB1_FELCA
ID ADRB1_FELCA Reviewed; 474 AA.
AC Q9TST6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Beta-1 adrenergic receptor;
DE AltName: Full=Beta-1 adrenoreceptor;
DE Short=Beta-1 adrenoceptor;
GN Name=ADRB1;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cully D.F., Tremml G., Zachwieja S.;
RT "Felis domesticus beta adrenergic receptor subtype 1.";
RL Submitted (OCT-1999) 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; AF192344; AAF04303.1; -; Genomic_DNA.
DR RefSeq; NP_001009375.1; NM_001009375.1.
DR AlphaFoldDB; Q9TST6; -.
DR SMR; Q9TST6; -.
DR PRIDE; Q9TST6; -.
DR Ensembl; ENSFCAT00000053422; ENSFCAP00000042036; ENSFCAG00000045161.
DR GeneID; 493971; -.
DR KEGG; fca:493971; -.
DR CTD; 153; -.
DR VGNC; VGNC:109579; ADRB1.
DR GeneTree; ENSGT00940000161953; -.
DR InParanoid; Q9TST6; -.
DR OrthoDB; 750855at2759; -.
DR Proteomes; UP000011712; Chromosome D2.
DR Bgee; ENSFCAG00000045161; Expressed in prefrontal cortex and 10 other tissues.
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:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0031694; F:alpha-2A adrenergic receptor binding; IEA:Ensembl.
DR GO; GO:0004940; F:beta1-adrenergic receptor activity; IBA:GO_Central.
DR GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS: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; IEA:Ensembl.
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: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; ISS:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
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..474
FT /note="Beta-1 adrenergic receptor"
FT /id="PRO_0000069117"
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..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 316..345
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 346..350
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 351..373
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 374..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 399..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 471..474
FT /note="PDZ-Binding"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18090"
FT LIPID 388
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 474 AA; 50533 MW; 2FC97EDE4CFB7C3F CRC64;
MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVPASPSA SPLTPTSEGP APLSQQWTAG
IGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVM
RGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC
TVWAISALVS FLPILMHWWR AEGDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM
AFVYLRVFRE AQKQVKKIDS CERRFLSGPA RPPSPAPAPG SPRPAATAAA AAAAAPLANG
RISKRRPSRL VALREQKALK TLGIIMGVFT LCWLPFFLAN VVKAFHRDLV PDRLFVFFNW
LGYANSAFNP IIYCRSPDFR KAFQRLLCFA RRAARGGHAA AGDRPRASGC LPGTRPPPSP
GAASDEDDDD DVGAAPPARL LEPWAGCNGG AAAADSDSSL DEPGRPAGAS ESKV
