ADRB3_CANLF
ID ADRB3_CANLF Reviewed; 405 AA.
AC O02662; Q9TTT2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
GN Name=ADRB3; Synonyms=B3AR;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9881593; DOI=10.1016/s0014-2999(98)00809-7;
RA Lenzen G., Pietri-Rouxel F., Drumare M.F., Amiard A., Guillot S.,
RA Archimbault P., Strosberg A.D.;
RT "Genomic cloning and species-specific properties of the recombinant canine
RT beta3-adrenoceptor.";
RL Eur. J. Pharmacol. 363:217-227(1998).
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; U92468; AAB51068.1; -; Genomic_DNA.
DR EMBL; AF200597; AAF08307.1; -; mRNA.
DR RefSeq; NP_001003377.1; NM_001003377.1.
DR PDB; 7DH5; EM; 3.16 A; R=2-379.
DR PDBsum; 7DH5; -.
DR AlphaFoldDB; O02662; -.
DR SMR; O02662; -.
DR STRING; 9615.ENSCAFP00000009245; -.
DR BindingDB; O02662; -.
DR ChEMBL; CHEMBL4400; -.
DR PaxDb; O02662; -.
DR Ensembl; ENSCAFT00030028389; ENSCAFP00030024764; ENSCAFG00030015392.
DR GeneID; 442979; -.
DR KEGG; cfa:442979; -.
DR CTD; 155; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; O02662; -.
DR OrthoDB; 614199at2759; -.
DR PRO; PR:O02662; -.
DR Proteomes; UP000002254; Unplaced.
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:0031699; F:beta-3 adrenergic receptor binding; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR GO; GO:0031649; P:heat generation; IEA:Ensembl.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..405
FT /note="Beta-3 adrenergic receptor"
FT /id="PRO_0000069139"
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 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..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 395
FT /note="Q -> P (in Ref. 2; AAF08307)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="A -> V (in Ref. 2; AAF08307)"
FT /evidence="ECO:0000305"
FT HELIX 40..63
FT /evidence="ECO:0007829|PDB:7DH5"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:7DH5"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 107..140
FT /evidence="ECO:0007829|PDB:7DH5"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 151..169
FT /evidence="ECO:0007829|PDB:7DH5"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 214..240
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 290..317
FT /evidence="ECO:0007829|PDB:7DH5"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 325..345
FT /evidence="ECO:0007829|PDB:7DH5"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:7DH5"
SQ SEQUENCE 405 AA; 43051 MW; 1A4E3EBA8C9D047F CRC64;
MAPWPHGNGS VASWPAAPTP TPDAANTSGL PGAPWAVALA GALLALEVLA TVGGNLLVIV
AIARTPRLQT MTNVFVTSLA TADLVVGLLV VPPGATLALT GRWPLGATGC ELWTSVDVLC
VTASIETLCA LAVDRYLAVT NPLRYGALVT KRRARAAVVL VWVVSAAVSF APIMSKWWRV
GADAEAQRCH SNPHCCAFAS NIPYALLSSS VSFYLPLLVM LFVYARVFLV ATRQLRLLRR
ELGRFPPAES PPAASRSRSP GPARRCASPA AVPSDRLRPA RLLPLREHRA LRTLGLIVGT
FTLCWLPFFV ANVMRALGGP SLVPSPALLA LNWLGYANSA FNPLIYCRSP DFRSAFRRLL
CRCRREEHRA AASPPGDPSA APAALTSPAE SSRCQALDGA SWGIS
