ADRB3_CAVPO
ID ADRB3_CAVPO Reviewed; 351 AA.
AC Q60483;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Beta-3 adrenergic receptor;
DE AltName: Full=Beta-3 adrenoreceptor;
DE Short=Beta-3 adrenoceptor;
DE Flags: Fragment;
GN Name=ADRB3;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8997376; DOI=10.1152/ajpregu.1996.271.6.r1729;
RA Atgie C., Tavernier G., D'Allaire F., Bengtsson T., Marti L., Carpene C.,
RA Lafontan M., Bukowiecki L.J., Langin D.;
RT "Beta 3-adrenoceptor in guinea pig brown and white adipocytes: low
RT expression and lack of function.";
RL Am. J. Physiol. 271:R1729-R1738(1996).
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, and digestive
CC tract.
CC -!- MISCELLANEOUS: The guinea pig differs from other rodents by an absence
CC of beta-3 adrenergic effects and by low expression in brown and white
CC adipose tissues. It is closer to human or primate than rodent beta-3.
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; U51098; AAA96315.1; -; mRNA.
DR AlphaFoldDB; Q60483; -.
DR SMR; Q60483; -.
DR InParanoid; Q60483; -.
DR Proteomes; UP000005447; 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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..>351
FT /note="Beta-3 adrenergic receptor"
FT /id="PRO_0000069141"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 61..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 131..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 153..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 176..200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 291..312
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 313..324
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 325..345
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 346..>351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 107..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 186..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 351
SQ SEQUENCE 351 AA; 37365 MW; B263C859EA5C04CD CRC64;
MAPWPHENSS AAPWPDTPTL APNTANTSGL PGVPWAAALA GALLALATVG GNLLVIVAIA
CTPRLQTMTN VFVTSLAAAD LVVGLLVVPP GATLALTGHW PLGATGCELW TSVDVLCVTA
SIETLCALAV DRYLAVTNPL RYRAVVTKRR ARAAVALVWA VAAAVSFAPI MSQWWRAGAD
AEAQLCHGNP RCCAFVSNVP YALLSSSVSF YLPLLVMLFV YARVFLVAQR QLRLLREEVG
RFPPQGSPRI RSRSASPAQG GGMRTAPAGE APCGPRPARL LPLRERRALR TLGLIVGTFA
LCWLPFFLAN VLRALGGPSL VPNSVLLPLN WLGYVNSAFN PLIYCRSPDF R
