ADRB1_XENLA
ID ADRB1_XENLA Reviewed; 385 AA.
AC O42574;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Beta-1 adrenergic receptor;
DE AltName: Full=Beta-1 adrenoreceptor;
DE Short=Beta-1 adrenoceptor;
DE Short=x-BETA1AR;
GN Name=adrb1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9395292; DOI=10.1016/s0014-5793(97)01278-7;
RA Devic E., Paquereau L., Kaghad M., Steinberg R., Caput D., Audigier Y.;
RT "Early expression of a beta1-adrenergic receptor and catecholamines in
RT Xenopus oocytes and embryos.";
RL FEBS Lett. 417:184-190(1997).
CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced
CC activation of adenylate cyclase through the action of G proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Early
CC endosome {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; Y09213; CAA70415.1; -; mRNA.
DR RefSeq; NP_001084152.1; NM_001090683.1.
DR AlphaFoldDB; O42574; -.
DR SMR; O42574; -.
DR PRIDE; O42574; -.
DR GeneID; 399337; -.
DR CTD; 399337; -.
DR Xenbase; XB-GENE-6254043; adrb1.L.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004940; F:beta1-adrenergic receptor activity; IEA:InterPro.
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:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045823; P:positive regulation of heart contraction; IEA:InterPro.
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..385
FT /note="Beta-1 adrenergic receptor"
FT /id="PRO_0000069126"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 62..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 98..109
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TOPO_DOM 132..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 227..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 268..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..302
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 303..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 326..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 340
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 187..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 385 AA; 43309 MW; 0153D05AE49E0C1B CRC64;
MGDGWGPMEC RNRSGTPTTV PSPMHPLPEL THQWTMGMTM FMAAIILLIV MGNIMVIVAI
GRNQRLQTLT NVFITSLACA DLIMGLFVVP LGATLVVSGR WLYGSIFCEF WTSVDVLCVT
ASIETLCVIS IDRYIAITSP FRYQSLLTKG RAKGIVCSVW GISALVSFLP IMMHWWRDTG
DPLAMKCYED PGCCDFVTNR AYAIASSIIS FYFPLIIMIF VYIRVFKEAQ KQMKKIDKCE
GRFSHSHVLS HGRSSRRILS KILVAKEQKA LKTLGIIMGT FTLCWLPFFL ANVVNVFYRN
LIPDKLFLFL NWLGYANSAF NPIIYCRSPD FRKAFKRLLC CPKKADRHLH TTGELSRYSG
GFVNSLDTNA LGMCSECNGV RTSLD
