ADRB1_MELGA
ID ADRB1_MELGA Reviewed; 483 AA.
AC P07700;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Beta-1 adrenergic receptor;
DE AltName: Full=Beta-1 adrenoreceptor;
DE Short=Beta-1 adrenoceptor;
DE Short=Beta-T;
GN Name=ADRB1;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3018746; DOI=10.1073/pnas.83.18.6795;
RA Yarden Y., Rodriguez H., Wong S.K.-F., Brandt D.R., May D.C., Burnier J.,
RA Harkins R.N., Chen E.Y., Ramachandran J., Ullrich A., Ross E.M.;
RT "The avian beta-adrenergic receptor: primary structure and membrane
RT topology.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6795-6799(1986).
RN [2]
RP STRUCTURE BY NMR OF 345-359.
RX PubMed=7828722; DOI=10.1016/0014-5793(94)01409-t;
RA Jung H., Windhaber R., Palm D., Schnackerz K.D.;
RT "NMR and circular dichroism studies of synthetic peptides derived from the
RT third intracellular loop of the beta-adrenoceptor.";
RL FEBS Lett. 358:133-136(1995).
RN [3] {ECO:0007744|PDB:2VT4}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-367 IN COMPLEX WITH THE
RP ANTAGONIST CYANOPINDOLOL, DISULFIDE BONDS, FUNCTION, AND TOPOLOGY.
RX PubMed=18594507; DOI=10.1038/nature07101;
RA Warne T., Serrano-Vega M.J., Baker J.G., Moukhametzianov R., Edwards P.C.,
RA Henderson R., Leslie A.G.W., Tate C.G., Schertler G.F.X.;
RT "Structure of a beta1-adrenergic G-protein-coupled receptor.";
RL Nature 454:486-491(2008).
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 (PubMed:18594507). In dorsal pons neurons, involved in the
CC regulation of sleep/wake behaviors (By similarity).
CC {ECO:0000250|UniProtKB:P34971, ECO:0000269|PubMed:18594507}.
CC -!- INTERACTION:
CC P07700; P07700: ADRB1; NbExp=3; IntAct=EBI-16038126, EBI-16038126;
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14379; AAA49627.1; -; mRNA.
DR PIR; A25896; A25896.
DR RefSeq; NP_001290104.1; NM_001303175.1.
DR PDB; 1DEP; NMR; -; A=345-359.
DR PDB; 2VT4; X-ray; 2.70 A; A/B/C/D=33-367.
DR PDB; 2Y00; X-ray; 2.50 A; A/B=33-368.
DR PDB; 2Y01; X-ray; 2.60 A; A/B=33-368.
DR PDB; 2Y02; X-ray; 2.60 A; A/B=33-368.
DR PDB; 2Y03; X-ray; 2.85 A; A/B=33-368.
DR PDB; 2Y04; X-ray; 3.05 A; A/B=33-368.
DR PDB; 2YCW; X-ray; 3.00 A; A/B=33-367.
DR PDB; 2YCX; X-ray; 3.25 A; A/B=33-367.
DR PDB; 2YCY; X-ray; 3.15 A; A/B=33-367.
DR PDB; 2YCZ; X-ray; 3.65 A; A/B=33-367.
DR PDB; 3ZPQ; X-ray; 2.80 A; A/B=33-368.
DR PDB; 3ZPR; X-ray; 2.70 A; A/B=33-368.
DR PDB; 4AMI; X-ray; 3.20 A; A/B=33-368.
DR PDB; 4AMJ; X-ray; 2.30 A; A/B=33-368.
DR PDB; 4BVN; X-ray; 2.10 A; A=33-368.
DR PDB; 4GPO; X-ray; 3.50 A; A/B=33-368.
DR PDB; 5A8E; X-ray; 2.40 A; A=33-368.
DR PDB; 5F8U; X-ray; 3.35 A; A/B=33-368.
DR PDB; 6H7J; X-ray; 2.80 A; A/B=44-368.
DR PDB; 6H7L; X-ray; 2.70 A; A/B=44-368.
DR PDB; 6H7M; X-ray; 2.76 A; A/B=44-368.
DR PDB; 6H7N; X-ray; 2.50 A; A/B=44-368.
DR PDB; 6H7O; X-ray; 2.80 A; A/B=44-368.
DR PDB; 6IBL; X-ray; 2.70 A; A/B=44-368.
DR PDB; 6TKO; EM; 3.30 A; A=32-357.
DR PDB; 7JJO; EM; 2.60 A; R=31-367.
DR PDBsum; 1DEP; -.
DR PDBsum; 2VT4; -.
DR PDBsum; 2Y00; -.
DR PDBsum; 2Y01; -.
DR PDBsum; 2Y02; -.
DR PDBsum; 2Y03; -.
DR PDBsum; 2Y04; -.
DR PDBsum; 2YCW; -.
DR PDBsum; 2YCX; -.
DR PDBsum; 2YCY; -.
DR PDBsum; 2YCZ; -.
DR PDBsum; 3ZPQ; -.
DR PDBsum; 3ZPR; -.
DR PDBsum; 4AMI; -.
DR PDBsum; 4AMJ; -.
DR PDBsum; 4BVN; -.
DR PDBsum; 4GPO; -.
DR PDBsum; 5A8E; -.
DR PDBsum; 5F8U; -.
DR PDBsum; 6H7J; -.
DR PDBsum; 6H7L; -.
DR PDBsum; 6H7M; -.
DR PDBsum; 6H7N; -.
DR PDBsum; 6H7O; -.
DR PDBsum; 6IBL; -.
DR PDBsum; 6TKO; -.
DR PDBsum; 7JJO; -.
DR AlphaFoldDB; P07700; -.
DR SMR; P07700; -.
DR DIP; DIP-60236N; -.
DR IntAct; P07700; 1.
DR GeneID; 100303680; -.
DR KEGG; mgp:100303680; -.
DR CTD; 153; -.
DR InParanoid; P07700; -.
DR OrthoDB; 750855at2759; -.
DR EvolutionaryTrace; P07700; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:AgBase.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004940; F:beta1-adrenergic receptor activity; IDA:AgBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045823; P:positive regulation of heart contraction; IEA:InterPro.
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 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..483
FT /note="Beta-1 adrenergic receptor"
FT /id="PRO_0000069120"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18594507"
FT TRANSMEM 39..67
FT /note="Helical; Name=1"
FT TOPO_DOM 68..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18594507"
FT TRANSMEM 77..103
FT /note="Helical; Name=2"
FT TOPO_DOM 104..115
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18594507"
FT TRANSMEM 116..137
FT /note="Helical; Name=3"
FT TOPO_DOM 138..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18594507"
FT TRANSMEM 156..179
FT /note="Helical; Name=4"
FT TOPO_DOM 180..205
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18594507"
FT TRANSMEM 206..231
FT /note="Helical; Name=5"
FT TOPO_DOM 232..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18594507"
FT TRANSMEM 286..315
FT /note="Helical; Name=6"
FT TOPO_DOM 316..320
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18594507"
FT TRANSMEM 321..343
FT /note="Helical; Name=7"
FT TOPO_DOM 344..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18594507"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="cyanopindolol"
FT /ligand_id="ChEBI:CHEBI:187894"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:18594507,
FT ECO:0007744|PDB:2VT4"
FT BINDING 211
FT /ligand="cyanopindolol"
FT /ligand_id="ChEBI:CHEBI:187894"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:18594507,
FT ECO:0007744|PDB:2VT4"
FT BINDING 329
FT /ligand="cyanopindolol"
FT /ligand_id="ChEBI:CHEBI:187894"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:18594507,
FT ECO:0007744|PDB:2VT4"
FT LIPID 358
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 114..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:18594507"
FT DISULFID 192..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:18594507"
FT HELIX 37..68
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 75..92
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 110..144
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 155..178
FT /evidence="ECO:0007829|PDB:4BVN"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:4BVN"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6TKO"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 217..239
FT /evidence="ECO:0007829|PDB:4BVN"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2Y03"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4AMJ"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:4AMJ"
FT HELIX 279..315
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 322..343
FT /evidence="ECO:0007829|PDB:4BVN"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:4BVN"
SQ SEQUENCE 483 AA; 54078 MW; B11A7E71F6CCE3E4 CRC64;
MGDGWLPPDC GPHNRSGGGG ATAAPTGSRQ VSAELLSQQW EAGMSLLMAL VVLLIVAGNV
LVIAAIGRTQ RLQTLTNLFI TSLACADLVM GLLVVPFGAT LVVRGTWLWG SFLCECWTSL
DVLCVTASIE TLCVIAIDRY LAITSPFRYQ SLMTRARAKV IICTVWAISA LVSFLPIMMH
WWRDEDPQAL KCYQDPGCCD FVTNRAYAIA SSIISFYIPL LIMIFVYLRV YREAKEQIRK
IDRCEGRFYG SQEQPQPPPL PQHQPILGNG RASKRKTSRV MAMREHKALK TLGIIMGVFT
LCWLPFFLVN IVNVFNRDLV PDWLFVFFNW LGYANSAFNP IIYCRSPDFR KAFKRLLCFP
RKADRRLHAG GQPAPLPGGF ISTLGSPEHS PGGTWSDCNG GTRGGSESSL EERHSKTSRS
ESKMEREKNI LATTRFYCTF LGNGDKAVFC TVLRIVKLFE DATCTCPHTH KLKMKWRFKQ
HQA
