ADRB3_PIG
ID ADRB3_PIG Reviewed; 407 AA.
AC Q95252; Q9MZ00;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
GN Name=ADRB3; Synonyms=BAR3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith T.R., Bidwell C.A., Mills S.E.;
RT "Sus scrofa beta-3-adrenergic receptor (BAR3) gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-105, AND TISSUE SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=7592080; DOI=10.2527/1995.7371962x;
RA McNeel R.L., Mersmann H.J.;
RT "Beta-adrenergic receptor subtype transcripts in porcine adipose tissue.";
RL J. Anim. Sci. 73:1962-1971(1995).
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 -!- TISSUE SPECIFICITY: White and brown adipose tissues.
CC {ECO:0000269|PubMed:7592080}.
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; AF274007; AAF82301.1; -; Genomic_DNA.
DR EMBL; U55858; AAB07688.1; -; mRNA.
DR AlphaFoldDB; Q95252; -.
DR SMR; Q95252; -.
DR STRING; 9823.ENSSSCP00000016767; -.
DR PaxDb; Q95252; -.
DR PRIDE; Q95252; -.
DR Ensembl; ENSSSCT00025038960; ENSSSCP00025016482; ENSSSCG00025028700.
DR Ensembl; ENSSSCT00055012382; ENSSSCP00055009757; ENSSSCG00055006394.
DR Ensembl; ENSSSCT00065040660; ENSSSCP00065017201; ENSSSCG00065030134.
DR Ensembl; ENSSSCT00070054010; ENSSSCP00070045782; ENSSSCG00070026931.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q95252; -.
DR TreeFam; TF316350; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 15.
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..407
FT /note="Beta-3 adrenergic receptor"
FT /id="PRO_0000069147"
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..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..269
FT /note="Pro residues"
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..24
FT /note="QGNSSLPPRPDVSTLAPNN -> HRNGSLALWSDAPTLDPSA (in Ref.
FT 2; AAB07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="V -> A (in Ref. 2; AAB07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..48
FT /note="Missing (in Ref. 2; AAB07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> I (in Ref. 2; AAB07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="M -> I (in Ref. 2; AAB07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="T -> A (in Ref. 2; AAB07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="V -> M (in Ref. 2; AAB07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="T -> A (in Ref. 2; AAB07688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 43611 MW; C6598382A9B38DD9 CRC64;
MAPWPQGNSS LPPRPDVSTL APNNANTSGL PGVPWAVALA GALLAPAVLA TVGGNLLVIV
AIARTPRLQT MTNVFVTSLA TADLVVGLLV VPPGTTLALT GHWPLGATCC ELWTSVDVLC
VTASIETLCA LAVDRYLAVT NPLRYGALVT KRRARAAVVL VWVVSAAVSF APIMSKWWRV
GADAEAQRCH SNPSCCTFAS NMPYALLSSS VSFYLPLLVM LFVYARVFVV ATSQLRLLRW
ELSRFPPEES PPAPSRSQSP APGRPWPSPA GVPSHGRRPA RLLPLREHRA LCTLGLIMGT
FTLCWLPFFV VNVVRALGGP SLVPVPAFLA LNWLGYANSA FNPLIYCHSP DFRSAFRRLL
CRCGPEEHLA AASPPRAPSG APETLTHPAE SRQSPPLNEA SWGLFRP
