ADRB3_BOVIN
ID ADRB3_BOVIN Reviewed; 405 AA.
AC P46626; Q1LZC1; Q28045; Q9TS17;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
GN Name=ADRB3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brown adipose tissue;
RX PubMed=7601122; DOI=10.1111/j.1432-1033.1995.tb20570.x;
RA Pietri-Rouxel F., Lenzen G., Kapoor A., Drumare M.F., Archimbault P.,
RA Strosberg A.D., Manning B.S.J.;
RT "Molecular cloning and pharmacological characterization of the bovine beta
RT 3-adrenergic receptor.";
RL Eur. J. Biochem. 230:350-358(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Simmental;
RX PubMed=10834601; DOI=10.2527/2000.7851397x;
RA Forrest R.H., Hickford J.G.H.;
RT "Rapid communication: nucleotide sequences of the bovine, caprine, and
RT ovine beta3-adrenergic receptor genes.";
RL J. Anim. Sci. 78:1397-1398(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-106.
RC TISSUE=Muscle;
RA Stoffel B., Meyer H.H.D.;
RT "Bovine beta3-adrenergic receptor, partial genomic sequence.";
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE OF 156-298.
RC STRAIN=Friesian; TISSUE=Adipose tissue;
RX PubMed=7904157; DOI=10.1042/bj2970093;
RA Casteilla L., Muzzin P., Revelli J.-P., Ricquier D., Giacobino J.-P.;
RT "Expression of beta 1- and beta 3-adrenergic-receptor messages and
RT adenylate cyclase beta-adrenergic response in bovine perirenal adipose
RT tissue during its transformation from brown into white fat.";
RL Biochem. J. 297:93-97(1994).
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}.
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; X85961; CAA59937.1; -; mRNA.
DR EMBL; AF109930; AAD26149.1; -; Genomic_DNA.
DR EMBL; BC116092; AAI16093.1; -; mRNA.
DR EMBL; X67214; CAA47654.1; -; Genomic_DNA.
DR PIR; S65459; S65459.
DR RefSeq; NP_776657.1; NM_174232.2.
DR AlphaFoldDB; P46626; -.
DR SMR; P46626; -.
DR STRING; 9913.ENSBTAP00000023923; -.
DR PaxDb; P46626; -.
DR GeneID; 281606; -.
DR KEGG; bta:281606; -.
DR CTD; 155; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; P46626; -.
DR OrthoDB; 614199at2759; -.
DR TreeFam; TF316350; -.
DR Proteomes; UP000009136; 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..405
FT /note="Beta-3 adrenergic receptor"
FT /id="PRO_0000069138"
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..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 247..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..405
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"
FT CONFLICT 6..7
FT /note="PG -> HE (in Ref. 4; CAA47654)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> T (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 42903 MW; C93667DC1CC286F8 CRC64;
MAPWPPGNSS LTPWPDIPTL APNTANASGL PGVPWAVALA GALLALAVLA TVGGNLLVIV
AIARTPRLQT MTNVFVTSLA TADLVVGLLV VPPGATLALT GHWPLGVTGC ELWTSVDVLC
VTASIETLCA LAVDRYLAVT NPLRYGALVT KRRALAAVVL VWVVSAAVSF APIMSKWWRI
GADAEAQRCH SNPRCCTFAS NMPYALLSSS VSFYLPLLVM LFVYARVFVV ATRQLRLLRR
ELGRFPPEES PPAPSRSGSP GLAGPCASPA GVPSYGRRPA RLLPLREHRA LRTLGLIMGT
FTLCWLPFFV VNVVRALGGP SLVSGPTFLA LNWLGYANSA FNPLIYCRSP DFRSAFRRLL
CRCRPEEHLA AASPPRAPSG APTALTSPAG PMQPPELDGA SCGLS
