ID   AA2BR_HUMAN             Reviewed;         332 AA.
AC   P29275;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   24-JAN-2024, entry version 199.
DE   RecName: Full=Adenosine receptor A2b;
GN   Name=ADORA2B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1325798; DOI=10.1016/s0006-291x(05)81462-7;
RA   Pierce K.D., Furlong T.J., Selbie L.A., Shine J.;
RT   "Molecular cloning and expression of an adenosine A2b receptor from human
RT   brain.";
RL   Biochem. Biophys. Res. Commun. 187:86-93(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7558011; DOI=10.1006/geno.1995.1061;
RA   Jacobson M.A., Johnson R.G., Luneau C.J., Salvatore C.A.;
RT   "Cloning and chromosomal localization of the human A2b adenosine receptor
RT   gene (ADORA2B) and its pseudogene.";
RL   Genomics 27:374-376(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC       mediated by G proteins which activate adenylyl cyclase.
CC   -!- INTERACTION:
CC       P29275; P29274: ADORA2A; NbExp=5; IntAct=EBI-3904751, EBI-2902702;
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; M97759; AAA51598.1; -; mRNA.
DR   EMBL; X68487; CAA48505.1; -; mRNA.
DR   EMBL; AY136748; AAN01274.1; -; mRNA.
DR   EMBL; BC025722; AAH25722.1; -; mRNA.
DR   CCDS; CCDS11173.1; -.
DR   PIR; JC1229; JC1229.
DR   RefSeq; NP_000667.1; NM_000676.2.
DR   PDB; 7XY6; EM; 2.99 A; R=2-332.
DR   PDB; 7XY7; EM; 3.26 A; R=2-332.
DR   PDB; 8HDO; EM; 2.87 A; R=1-332.
DR   PDB; 8HDP; EM; 3.20 A; R=1-332.
DR   PDBsum; 7XY6; -.
DR   PDBsum; 7XY7; -.
DR   PDBsum; 8HDO; -.
DR   PDBsum; 8HDP; -.
DR   AlphaFoldDB; P29275; -.
DR   EMDB; EMD-34676; -.
DR   EMDB; EMD-34677; -.
DR   SMR; P29275; -.
DR   BioGRID; 106648; 46.
DR   IntAct; P29275; 3.
DR   STRING; 9606.ENSP00000304501; -.
DR   BindingDB; P29275; -.
DR   ChEMBL; CHEMBL255; -.
DR   DrugBank; DB00640; Adenosine.
DR   DrugBank; DB00201; Caffeine.
DR   DrugBank; DB05936; CVT-6883.
DR   DrugBank; DB04932; Defibrotide.
DR   DrugBank; DB00824; Enprofylline.
DR   DrugBank; DB00277; Theophylline.
DR   DrugCentral; P29275; -.
DR   GuidetoPHARMACOLOGY; 20; -.
DR   GlyCosmos; P29275; 2 sites, No reported glycans.
DR   GlyGen; P29275; 2 sites.
DR   iPTMnet; P29275; -.
DR   PhosphoSitePlus; P29275; -.
DR   BioMuta; ADORA2B; -.
DR   DMDM; 112938; -.
DR   MassIVE; P29275; -.
DR   PaxDb; 9606-ENSP00000304501; -.
DR   PeptideAtlas; P29275; -.
DR   Antibodypedia; 25203; 393 antibodies from 37 providers.
DR   DNASU; 136; -.
DR   Ensembl; ENST00000304222.3; ENSP00000304501.2; ENSG00000170425.4.
DR   GeneID; 136; -.
DR   KEGG; hsa:136; -.
DR   MANE-Select; ENST00000304222.3; ENSP00000304501.2; NM_000676.4; NP_000667.1.
DR   UCSC; uc002gpd.2; human.
DR   AGR; HGNC:264; -.
DR   CTD; 136; -.
DR   DisGeNET; 136; -.
DR   GeneCards; ADORA2B; -.
DR   HGNC; HGNC:264; ADORA2B.
DR   HPA; ENSG00000170425; Tissue enhanced (urinary).
DR   MIM; 600446; gene.
DR   neXtProt; NX_P29275; -.
DR   OpenTargets; ENSG00000170425; -.
DR   PharmGKB; PA24585; -.
DR   VEuPathDB; HostDB:ENSG00000170425; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234555; -.
DR   HOGENOM; CLU_009579_11_5_1; -.
DR   InParanoid; P29275; -.
DR   OMA; CRREELY; -.
DR   OrthoDB; 2909020at2759; -.
DR   PhylomeDB; P29275; -.
DR   TreeFam; TF325296; -.
DR   PathwayCommons; P29275; -.
DR   Reactome; R-HSA-417973; Adenosine P1 receptors.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-5683826; Surfactant metabolism.
DR   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   SignaLink; P29275; -.
DR   SIGNOR; P29275; -.
DR   BioGRID-ORCS; 136; 6 hits in 1160 CRISPR screens.
DR   ChiTaRS; ADORA2B; human.
DR   GeneWiki; Adenosine_A2B_receptor; -.
DR   GenomeRNAi; 136; -.
DR   Pharos; P29275; Tclin.
DR   PRO; PR:P29275; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P29275; Protein.
DR   Bgee; ENSG00000170425; Expressed in mucosa of transverse colon and 132 other cell types or tissues.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
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:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
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: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:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
DR   GO; GO:0042311; P:vasodilation; IBA:GO_Central.
DR   CDD; cd15069; 7tmA_Adenosine_R_A2B; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001435; Adeno_A2B_rcpt.
DR   InterPro; IPR001634; Adenosn_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24246:SF18; ADENOSINE RECEPTOR A2B; 1.
DR   PANTHER; PTHR24246; OLFACTORY RECEPTOR AND ADENOSINE RECEPTOR; 1.
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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P29275; HS.
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..332
FT                   /note="Adenosine receptor A2b"
FT                   /id="PRO_0000069003"
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"
FT   HELIX           5..33
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           41..69
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           75..108
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           119..137
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           173..175
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           179..184
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           192..217
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           224..259
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           262..265
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           270..290
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   TURN            291..293
FT                   /evidence="ECO:0007829|PDB:7XY6"
FT   HELIX           295..307
FT                   /evidence="ECO:0007829|PDB:7XY6"
SQ   SEQUENCE   332 AA;  36333 MW;  38AD088E2439C7FA CRC64;
     MLLETQDALY VALELVIAAL SVAGNVLVCA AVGTANTLQT PTNYFLVSLA AADVAVGLFA
     IPFAITISLG FCTDFYGCLF LACFVLVLTQ SSIFSLLAVA VDRYLAICVP LRYKSLVTGT
     RARGVIAVLW VLAFGIGLTP FLGWNSKDSA TNNCTEPWDG TTNESCCLVK CLFENVVPMS
     YMVYFNFFGC VLPPLLIMLV IYIKIFLVAC RQLQRTELMD HSRTTLQREI HAAKSLAMIV
     GIFALCWLPV HAVNCVTLFQ PAQGKNKPKW AMNMAILLSH ANSVVNPIVY AYRNRDFRYT
     FHKIISRYLL CQADVKSGNG QAGVQPALGV GL
//