AA2BR_RAT
ID AA2BR_RAT Reviewed; 332 AA.
AC P29276;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Adenosine receptor A2b;
GN Name=Adora2b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1584214; DOI=10.1210/mend.6.3.1584214;
RA Stehle J.H., Rivkees S.A., Lee J.J., Weaver D.R., Deeds J.D., Reppert S.M.;
RT "Molecular cloning and expression of the cDNA for a novel A2-adenosine
RT receptor subtype.";
RL Mol. Endocrinol. 6:384-393(1992).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1333049; DOI=10.1210/mend.6.10.1333049;
RA Rivkees S.A., Reppert S.M.;
RT "RFL9 encodes an A2b-adenosine receptor.";
RL Mol. Endocrinol. 6:1598-1604(1992).
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M91466; AAA20981.1; -; mRNA.
DR PIR; A42171; A42171.
DR RefSeq; NP_058857.1; NM_017161.1.
DR AlphaFoldDB; P29276; -.
DR SMR; P29276; -.
DR IntAct; P29276; 1.
DR STRING; 10116.ENSRNOP00000003966; -.
DR BindingDB; P29276; -.
DR ChEMBL; CHEMBL2592; -.
DR DrugCentral; P29276; -.
DR GuidetoPHARMACOLOGY; 20; -.
DR GlyGen; P29276; 2 sites.
DR PhosphoSitePlus; P29276; -.
DR PaxDb; P29276; -.
DR GeneID; 29316; -.
DR KEGG; rno:29316; -.
DR UCSC; RGD:2050; rat.
DR CTD; 136; -.
DR RGD; 2050; Adora2b.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P29276; -.
DR OrthoDB; 550297at2759; -.
DR PhylomeDB; P29276; -.
DR Reactome; R-RNO-417973; Adenosine P1 receptors.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR PRO; PR:P29276; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IMP:RGD.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; ISO:RGD.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR GO; GO:0002882; P:positive regulation of chronic inflammatory response to non-antigenic stimulus; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:RGD.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:RGD.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; ISO:RGD.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; IMP:RGD.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; IMP:RGD.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IMP:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; ISO:RGD.
DR GO; GO:1990776; P:response to angiotensin; IMP:RGD.
DR GO; GO:0042311; P:vasodilation; IDA:RGD.
DR InterPro; IPR001435; Adeno_A2B_rcpt.
DR InterPro; IPR001634; Adenosn_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00554; ADENOSINA2BR.
DR PRINTS; PR00424; ADENOSINER.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..332
FT /note="Adenosine receptor A2b"
FT /id="PRO_0000069005"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 9..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 34..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 44..67
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 68..78
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..101
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 102..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 122..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 145..178
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 179..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 204..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 236..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 260..267
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 268..291
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 292..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 254
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 279
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 280
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT LIPID 311
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 332 AA; 36367 MW; F0ABAB5CCACA8858 CRC64;
MQLETQDALY VALELVIAAL AVAGNVLVCA AVGASSALQT PTNYFLVSLA TADVAVGLFA
IPFAITISLG FCTDFHSCLF LACFVLVLTQ SSIFSLLAVA VDRYLAIRVP LRYKGLVTGT
RARGIIAVLW VLAFGIGLTP FLGWNSKDRA TSNCTEPGDG ITNKSCCPVK CLFENVVPMS
YMVYFNFFGC VLPPLLIMMV IYIKIFMVAC KQLQHMELME HSRTTLQREI HAAKSLAMIV
GIFALCWLPV HAINCITLFH PALAKDKPKW VMNVAILLSH ANSVVNPIVY AYRNRDFRYS
FHRIISRYVL CQTDTKGGSG QAGGQSTFSL SL
