ADRB3_MOUSE
ID ADRB3_MOUSE Reviewed; 400 AA.
AC P25962; A2RS74; Q9QZ98;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
GN Name=Adrb3; Synonyms=Adrb3r, B3bar;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SWR/J;
RX PubMed=1718744; DOI=10.1002/j.1460-2075.1991.tb04940.x;
RA Nahmias C., Blin N., Elalouf J.-M., Mattei M.-G., Strosberg A.D.,
RA Emorine L.J.;
RT "Molecular characterization of the mouse beta 3-adrenergic receptor:
RT relationship with the atypical receptor of adipocytes.";
RL EMBO J. 10:3721-3727(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=8389293; DOI=10.1111/j.1432-1033.1993.tb17861.x;
RA van Spronsen A., Nahmias C., Krief S., Briend-Sutren M.-M., Strosberg A.D.,
RA Emorine L.J.;
RT "The promoter and intron/exon structure of the human and mouse beta 3-
RT adrenergic-receptor genes.";
RL Eur. J. Biochem. 213:1117-1124(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=C57BL/6J; TISSUE=Brown adipose tissue;
RX PubMed=10455305; DOI=10.1038/sj.bjp.0702688;
RA Evans B.A., Papaioannou M., Hamilton S., Summers R.J.;
RT "Alternative splicing generates two isoforms of the beta3-adrenoceptor
RT which are differentially expressed in mouse tissues.";
RL Br. J. Pharmacol. 127:1525-1531(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 378-400.
RC TISSUE=Adipose tissue;
RX PubMed=1336117;
RA Granneman J.G., Lahners K.N., Rao D.D.;
RT "Rodent and human beta 3-adrenergic receptor genes contain an intron within
RT the protein-coding block.";
RL Mol. Pharmacol. 42:964-970(1992).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P25962-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P25962-2; Sequence=VSP_001864;
CC -!- TISSUE SPECIFICITY: White and brown adipose tissues, and digestive
CC tract. Isoform B highest in brain.
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; X72862; CAA51384.1; -; Genomic_DNA.
DR EMBL; X60438; CAA42966.1; -; Genomic_DNA.
DR EMBL; AF193027; AAF05768.1; -; mRNA.
DR EMBL; BC132000; AAI32001.1; -; mRNA.
DR EMBL; S53290; AAB24836.1; -; mRNA.
DR CCDS; CCDS22213.1; -. [P25962-1]
DR PIR; I77910; I77910.
DR PIR; S32804; S32804.
DR RefSeq; NP_038490.2; NM_013462.3. [P25962-1]
DR RefSeq; XP_006509050.1; XM_006508987.3.
DR RefSeq; XP_006509051.1; XM_006508988.3.
DR RefSeq; XP_011240418.1; XM_011242116.2.
DR RefSeq; XP_011240419.1; XM_011242117.2.
DR RefSeq; XP_017168014.1; XM_017312525.1.
DR AlphaFoldDB; P25962; -.
DR SMR; P25962; -.
DR BioGRID; 198008; 1.
DR IntAct; P25962; 1.
DR MINT; P25962; -.
DR STRING; 10090.ENSMUSP00000080162; -.
DR BindingDB; P25962; -.
DR ChEMBL; CHEMBL4030; -.
DR DrugCentral; P25962; -.
DR GuidetoPHARMACOLOGY; 30; -.
DR GlyGen; P25962; 2 sites.
DR iPTMnet; P25962; -.
DR PhosphoSitePlus; P25962; -.
DR SwissPalm; P25962; -.
DR jPOST; P25962; -.
DR PaxDb; P25962; -.
DR PeptideAtlas; P25962; -.
DR PRIDE; P25962; -.
DR ProteomicsDB; 296187; -. [P25962-1]
DR ProteomicsDB; 296188; -. [P25962-2]
DR DNASU; 11556; -.
DR Ensembl; ENSMUST00000081438; ENSMUSP00000080162; ENSMUSG00000031489. [P25962-1]
DR Ensembl; ENSMUST00000117565; ENSMUSP00000113732; ENSMUSG00000031489. [P25962-2]
DR Ensembl; ENSMUST00000121838; ENSMUSP00000113006; ENSMUSG00000031489. [P25962-1]
DR GeneID; 11556; -.
DR KEGG; mmu:11556; -.
DR UCSC; uc009lie.1; mouse. [P25962-1]
DR UCSC; uc009lig.1; mouse. [P25962-2]
DR CTD; 155; -.
DR MGI; MGI:87939; Adrb3.
DR VEuPathDB; HostDB:ENSMUSG00000031489; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000158663; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; P25962; -.
DR OMA; WPHENSS; -.
DR OrthoDB; 614199at2759; -.
DR PhylomeDB; P25962; -.
DR TreeFam; TF316350; -.
DR Reactome; R-MMU-390696; Adrenoceptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 11556; 1 hit in 73 CRISPR screens.
DR PRO; PR:P25962; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P25962; protein.
DR Bgee; ENSMUSG00000031489; Expressed in thoracic mammary gland and 92 other tissues.
DR ExpressionAtlas; P25962; baseline and differential.
DR Genevisible; P25962; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISS:HGNC-UCL.
DR GO; GO:0031699; F:beta-3 adrenergic receptor binding; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0051380; F:norepinephrine binding; ISO:MGI.
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:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IGI:MGI.
DR GO; GO:0002024; P:diet induced thermogenesis; IGI:MGI.
DR GO; GO:0042755; P:eating behavior; ISO:MGI.
DR GO; GO:0031649; P:heat generation; IGI:MGI.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IGI:MGI.
DR GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IDA:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IGI:MGI.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..400
FT /note="Beta-3 adrenergic receptor"
FT /id="PRO_0000069146"
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 241..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..400
FT /note="Disordered"
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 VAR_SEQ 388..400
FT /note="RFDGYEGARPFPT -> SSLLREPRHLYTCLGYP (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10455305,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_001864"
SQ SEQUENCE 400 AA; 43006 MW; 374E072C01DFA32E CRC64;
MAPWPHRNGS LALWSDAPTL DPSAANTSGL PGVPWAAALA GALLALATVG GNLLVIIAIA
RTPRLQTITN VFVTSLAAAD LVVGLLVMPP GATLALTGHW PLGETGCELW TSVDVLCVTA
SIETLCALAV DRYLAVTNPL RYGTLVTKRR ARAAVVLVWI VSAAVSFAPI MSQWWRVGAD
AEAQECHSNP RCCSFASNMP YALLSSSVSF YLPLLVMLFV YARVFVVAKR QRHLLRRELG
RFSPEESPPS PSRSPSPATG GTPAAPDGVP PCGRRPARLL PLREHRALRT LGLIMGIFSL
CWLPFFLANV LRALAGPSLV PSGVFIALNW LGYANSAFNP VIYCRSPDFR DAFRRLLCSY
GGRGPEEPRA VTFPASPVEA RQSPPLNRFD GYEGARPFPT
