AA2BR_RABIT
ID AA2BR_RABIT Reviewed; 332 AA.
AC Q32ZE2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Adenosine receptor A2b;
GN Name=ADORA2B;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Auchampach J.A., Wan T.C., Kreckler L.M.;
RT "Analysis of recombinant A2B adenosine receptors from multiple species:
RT identification of a potential non-functional splice variant.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase (By similarity).
CC {ECO:0000250}.
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; AY630339; AAV31919.1; -; mRNA.
DR RefSeq; NP_001075644.1; NM_001082175.2.
DR AlphaFoldDB; Q32ZE2; -.
DR SMR; Q32ZE2; -.
DR STRING; 9986.ENSOCUP00000023252; -.
DR PRIDE; Q32ZE2; -.
DR GeneID; 100008951; -.
DR KEGG; ocu:100008951; -.
DR CTD; 136; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; Q32ZE2; -.
DR OMA; PVKCLFE; -.
DR OrthoDB; 550297at2759; -.
DR TreeFam; TF325296; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
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:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0043303; P:mast cell degranulation; IEA:Ensembl.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0002882; P:positive regulation of chronic inflammatory response to non-antigenic stimulus; IEA:Ensembl.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
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 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..332
FT /note="Adenosine receptor A2b"
FT /id="PRO_0000269715"
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; 36251 MW; EBE31450932589B3 CRC64;
MQLETQDALY VALELAIAAL SVAGNVLVCA AVGTSSALQT PTNYFLVSLA AADVAVGLFA
IPFAITISLG FCTDFHSCLF LACFVLVLTQ SSIFSLLAVA VDRYLAILVP LRYKSLVTGT
RARGVIAVLW VLAFGIGLTP FLGWNSKDSA TANCTEPRDG TTNESCCLVK CLFENVVPMS
YMVYFNFFGC VLPPLLIMLA IYIKIFLVAC RQLQRTELMD HSRTTLQREI HAAKSLAMIV
GIFALCWLPV HAINCVTLFQ PAQAKDKPKW AMNTAILLSH ANSVVNPIVY AYRNRDFRET
FHKIISRYVL CQTDVKSGNG QSGAQPVLSM GL
