ADRB1_PIG
ID ADRB1_PIG Reviewed; 468 AA.
AC Q28998; O46575;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Beta-1 adrenergic receptor;
DE AltName: Full=Beta-1 adrenoreceptor;
DE Short=Beta-1 adrenoceptor;
GN Name=ADRB1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9655595; DOI=10.2527/1998.7661720x;
RA Cao H., Bidwell C.A., Williams S.K., Liang W., Mills S.E.;
RT "Nucleotide sequence of the coding region for the porcine beta1-adrenergic
RT receptor gene.";
RL J. Anim. Sci. 76:1720-1721(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-468.
RC TISSUE=Heart;
RX PubMed=10229356; DOI=10.2527/1999.773611x;
RA McNeel R.L., Mersmann H.J.;
RT "Distribution and quantification of beta1-, beta2-, and beta3-adrenergic
RT receptor subtype transcripts in porcine tissues.";
RL J. Anim. Sci. 77:611-621(1999).
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; AF042454; AAB97525.1; -; Genomic_DNA.
DR EMBL; U56425; AAC06330.1; -; mRNA.
DR RefSeq; NP_001116546.1; NM_001123074.1.
DR AlphaFoldDB; Q28998; -.
DR SMR; Q28998; -.
DR STRING; 9823.ENSSSCP00000011344; -.
DR BindingDB; Q28998; -.
DR ChEMBL; CHEMBL4351; -.
DR PaxDb; Q28998; -.
DR PRIDE; Q28998; -.
DR GeneID; 397355; -.
DR KEGG; ssc:397355; -.
DR CTD; 153; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q28998; -.
DR OrthoDB; 750855at2759; -.
DR PRO; PR:Q28998; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 2: Evidence at transcript 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..468
FT /note="Beta-1 adrenergic receptor"
FT /id="PRO_0000069123"
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..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 196..221
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 222..247
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 248..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 310..339
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 340..344
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 345..367
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 368..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 267..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 465..468
FT /note="PDZ-Binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 269..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18090"
FT LIPID 382
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..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 208..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 173
FT /note="A -> AR (in Ref. 2; AAC06330)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="L -> V (in Ref. 2; AAC06330)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..328
FT /note="CWL -> WWV (in Ref. 2; AAC06330)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="R -> A (in Ref. 2; AAC06330)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="T -> S (in Ref. 2; AAC06330)"
FT /evidence="ECO:0000305"
FT CONFLICT 463..464
FT /note="AS -> SF (in Ref. 2; AAC06330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 50098 MW; 93C3AEE78B703225 CRC64;
MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVPASPPA SLLTPASEGS VQLSQQWTAG
MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV
WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRAARALVCT
VWAISALVSF LPILMHWWRD KGAEARRCYN DPKCCDFVTN RAYAIASSVV SFYVPLCIMA
FVYLRVFREA QKQVKKIDSC ERRFLGSPAR PPSPAPSPGS PLPAAAAAAP VANGRTSKRR
PSRLVALREQ KALKTLGIIM GVFTLCWLPF FLANVVKAFH RDLVPDRLFV FFNWLGYANS
AFNPIIYCRS PDFRKAFQRL LCCARRVARG SCAAAGDGPR ASGCLAVARP PPSPGAASDD
DDDEEDVGAA PPAPLLEPWA GYNGGAARDS DSSLDERTPG GRASESKV
