ADRB3_RAT
ID ADRB3_RAT Reviewed; 400 AA.
AC P26255;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
GN Name=Adrb3; Synonyms=Adrb3r;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1721063; DOI=10.1016/s0021-9258(18)54391-x;
RA Muzzin P., Revelli J.-P., Kuhne F., Gocayne J.D., McCombie W.R.,
RA Venter J.C., Giacobino J.-P., Fraser C.M.;
RT "An adipose tissue-specific beta-adrenergic receptor. Molecular cloning and
RT down-regulation in obesity.";
RL J. Biol. Chem. 266:24053-24058(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1684635;
RA Granneman J.G., Lahners K.N., Chaudhry A.;
RT "Molecular cloning and expression of the rat beta 3-adrenergic receptor.";
RL Mol. Pharmacol. 40:895-899(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8382630; DOI=10.1016/0014-5793(93)80516-w;
RA Bensaid M., Kaghad M., Rodriguez M., le Fur G., Caput D.;
RT "The rat beta 3-adrenergic receptor gene contains an intron.";
RL FEBS Lett. 318:223-226(1993).
CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced
CC activation of adenylate cyclase through the action of G proteins. Beta-
CC 3 is involved in the regulation of lipolysis and thermogenesis.
CC -!- SUBUNIT: Interacts with ARRDC3. {ECO:0000250|UniProtKB:P13945}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: White and brown adipose tissues, and digestive
CC tract.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRB3 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M74716; AAA74470.1; -; mRNA.
DR EMBL; S73473; AAB20702.1; -; mRNA.
DR EMBL; S56481; AAB25520.1; -; mRNA.
DR EMBL; S56152; AAB25521.1; -; Genomic_DNA.
DR PIR; A41679; A41679.
DR PIR; A53281; A53281.
DR RefSeq; NP_037240.2; NM_013108.2.
DR AlphaFoldDB; P26255; -.
DR SMR; P26255; -.
DR STRING; 10116.ENSRNOP00000016907; -.
DR BindingDB; P26255; -.
DR ChEMBL; CHEMBL4031; -.
DR DrugCentral; P26255; -.
DR GuidetoPHARMACOLOGY; 30; -.
DR GlyGen; P26255; 2 sites.
DR iPTMnet; P26255; -.
DR PhosphoSitePlus; P26255; -.
DR PaxDb; P26255; -.
DR Ensembl; ENSRNOT00000016907; ENSRNOP00000016907; ENSRNOG00000012674.
DR GeneID; 25645; -.
DR KEGG; rno:25645; -.
DR UCSC; RGD:2061; rat.
DR CTD; 155; -.
DR RGD; 2061; Adrb3.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000158663; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; P26255; -.
DR OMA; WPHENSS; -.
DR OrthoDB; 614199at2759; -.
DR PhylomeDB; P26255; -.
DR TreeFam; TF316350; -.
DR Reactome; R-RNO-390696; Adrenoceptors.
DR PRO; PR:P26255; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000012674; Expressed in colon and 10 other tissues.
DR Genevisible; P26255; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISS:HGNC-UCL.
DR GO; GO:0031699; F:beta-3 adrenergic receptor binding; ISO:RGD.
DR GO; GO:0004939; F:beta-adrenergic receptor activity; ISS:HGNC-UCL.
DR GO; GO:0015052; F:beta3-adrenergic receptor activity; ISS:HGNC-UCL.
DR GO; GO:0051379; F:epinephrine binding; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0051380; F:norepinephrine binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:HGNC-UCL.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0002024; P:diet induced thermogenesis; ISO:RGD.
DR GO; GO:0042755; P:eating behavior; IDA:RGD.
DR GO; GO:0031649; P:heat generation; ISO:RGD.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000681; ADRB3_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00563; ADRENRGCB3AR.
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; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..400
FT /note="Beta-3 adrenergic receptor"
FT /id="PRO_0000069148"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 61..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 131..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 153..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 176..200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 290..311
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 312..323
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 324..344
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 345..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 243..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 358
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 186..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 234..235
FT /note="LL -> FV (in Ref. 1; AAA74470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 43146 MW; D588540C4B2CE813 CRC64;
MAPWPHKNGS LAFWSDAPTL DPSAANTSGL PGVPWAAALA GALLALATVG GNLLVITAIA
RTPRLQTITN VFVTSLATAD LVVGLLVMPP GATLALTGHW PLGATGCELW TSVDVLCVTA
SIETLCALAV DRYLAVTNPL RYGTLVTKRR ARAAVVLVWI VSATVSFAPI MSQWWRVGAD
AEAQECHSNP RCCSFASNMP YALLSSSVSF YLPLLVMLFV YARVFVVAKR QRRLLRRELG
RFPPEESPRS PSRSPSPATV GTPTASDGVP SCGRRPARLL PLGEHRALRT LGLIMGIFSL
CWLPFFLANV LRALVGPSLV PSGVFIALNW LGYANSAFNP LIYCRSPDFR DAFRRLLCSY
GGRGPEEPRV VTFPASPVAS RQNSPLNRFD GYEGERPFPT
