ADRB3_CAPHI
ID ADRB3_CAPHI Reviewed; 405 AA.
AC Q9XT57;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
GN Name=ADRB3; Synonyms=B3AR;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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; AF109929; AAD26148.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XT57; -.
DR SMR; Q9XT57; -.
DR STRING; 9925.ENSCHIP00000011884; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:HGNC-UCL.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
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 3: Inferred from homology;
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_0000069140"
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 369..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"
SQ SEQUENCE 405 AA; 43126 MW; 776B81756BF5556F CRC64;
MAPWPPRNSS LTPWPDIPTL APNTANASGL PGVPWAVALA GALLALAVLA IVGGNLLVIV
AIARTPRLQT MTNVFVTSLA TADLVVGLLV VPPGATLALT GHWPLGVTGC ELWTSVDVLC
VTASIETLCA LAVDRYLAVT NPLRYGALVT KRRARAAVVL VWVVSAAVSF APIMSKWWRV
GADAEAQRCH SNPRCCTFAS NMPYALLSSS VSFYLPLLVM LFVYARVFVV ATRQLRLLRR
ELGRFPPEES PPAPSRSGSP GPAGPYASPA GVPSYGRRPA RLLPLREHRA LRTLGLIMGT
FTLCWLPFFV VNVVRALGGP SLVSGPTFLA LNWLGYANSA FNPLIYCRSP DFQSAFRRLL
CRCRPEEHLA AASPPRAPSG APRVLTSPAG PRQPSPLDGA SCGLS
