ADRB3_MACMU
ID ADRB3_MACMU Reviewed; 418 AA.
AC Q28524;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
GN Name=ADRB3; Synonyms=B3AR;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9133593; DOI=10.1016/s0378-1119(96)00796-2;
RA Walston J., Lowe A., Silver K., Yang Y., Bodkin N.L., Hansen B.C.,
RA Shuldiner A.R.;
RT "The beta3-adrenergic receptor in the obesity and diabetes prone rhesus
RT monkey is very similar to human and contains arginine at codon 64.";
RL Gene 188:207-213(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Thompson G.M., Kelly L.J., Candelore M.R.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; U63592; AAB53939.1; -; Genomic_DNA.
DR EMBL; U63591; AAB53939.1; JOINED; Genomic_DNA.
DR EMBL; AF200596; AAF08306.1; -; mRNA.
DR PIR; G02953; G02953.
DR RefSeq; NP_001038195.1; NM_001044730.2.
DR AlphaFoldDB; Q28524; -.
DR SMR; Q28524; -.
DR STRING; 9544.ENSMMUP00000032146; -.
DR BindingDB; Q28524; -.
DR ChEMBL; CHEMBL3124732; -.
DR PRIDE; Q28524; -.
DR GeneID; 699129; -.
DR KEGG; mcc:699129; -.
DR CTD; 155; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q28524; -.
DR OMA; WPHENSS; -.
DR OrthoDB; 614199at2759; -.
DR TreeFam; TF316350; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISS:HGNC-UCL.
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; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0051380; F:norepinephrine binding; IBA:GO_Central.
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:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:HGNC-UCL.
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..418
FT /note="Beta-3 adrenergic receptor"
FT /id="PRO_0000069144"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 64..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 92..111
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 134..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 156..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..203
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 204..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 226..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 293..314
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 315..326
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 327..347
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 348..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 372..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 361
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 110..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 189..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 418 AA; 44657 MW; F076D520ADC3502D CRC64;
MAPWPHGNSS LVPWPDVPTL APNTANTSGL PGVPWAAALA GALLALAVLA TVGGNLLVIV
AITRTPRLQT MTNVFVTSLA AADLVMGLLV VPPAATLVLT GHWPLGATGC ELWTSVDVLC
VTASIETLCA LAVDRYLAVT NPLRYGALVT KRRARAAVVL VWVVSAAVSF APIMSQWWRV
GADAEAQRCH SNPRCCAFAS NMPYVLLSSS VSFYLPLLVM LFVYARVFVV ATRQLRLLRW
ELGRFPPEES SPALSRSLAP APAGTCAPPE GVPACCRRPA RLLPLREHRA LCTLGLIMGT
FTLCWLPFFL ANVLRALGGP SLVPDPAFLA LNWLGYANSA FNPLIYCRSP DFRSAFRRLL
CHCGGRLPRE PCAADRPASS PRAPLRPGPA PRSPGFASGS TGLLGEFLRP EGQEATLR
