ID   AA2BR_MOUSE             Reviewed;         332 AA.
AC   Q60614; Q8BXI2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Adenosine receptor A2b;
GN   Name=Adora2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Bone marrow;
RX   PubMed=8157966;
RA   Marquardt D.L., Walker L.L., Heinemann S.;
RT   "Cloning of two adenosine receptor subtypes from mouse bone marrow-derived
RT   mast cells.";
RL   J. Immunol. 152:4508-4515(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   -!- 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; U05673; AAA19001.1; -; mRNA.
DR   EMBL; AK047002; BAC32938.1; -; mRNA.
DR   EMBL; AL596110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC116415; AAI16416.1; -; mRNA.
DR   EMBL; BC116416; AAI16417.1; -; mRNA.
DR   CCDS; CCDS24822.1; -.
DR   PIR; I48933; I48933.
DR   RefSeq; NP_031439.2; NM_007413.4.
DR   AlphaFoldDB; Q60614; -.
DR   SMR; Q60614; -.
DR   STRING; 10090.ENSMUSP00000018644; -.
DR   BindingDB; Q60614; -.
DR   ChEMBL; CHEMBL2237; -.
DR   DrugCentral; Q60614; -.
DR   GuidetoPHARMACOLOGY; 20; -.
DR   GlyCosmos; Q60614; 2 sites, No reported glycans.
DR   GlyGen; Q60614; 2 sites.
DR   iPTMnet; Q60614; -.
DR   PhosphoSitePlus; Q60614; -.
DR   SwissPalm; Q60614; -.
DR   PaxDb; 10090-ENSMUSP00000018644; -.
DR   Antibodypedia; 25203; 393 antibodies from 37 providers.
DR   DNASU; 11541; -.
DR   Ensembl; ENSMUST00000018644.3; ENSMUSP00000018644.3; ENSMUSG00000018500.3.
DR   GeneID; 11541; -.
DR   KEGG; mmu:11541; -.
DR   UCSC; uc007jio.1; mouse.
DR   AGR; MGI:99403; -.
DR   CTD; 136; -.
DR   MGI; MGI:99403; Adora2b.
DR   VEuPathDB; HostDB:ENSMUSG00000018500; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234555; -.
DR   HOGENOM; CLU_009579_11_5_1; -.
DR   InParanoid; Q60614; -.
DR   OMA; CRREELY; -.
DR   OrthoDB; 2909020at2759; -.
DR   PhylomeDB; Q60614; -.
DR   TreeFam; TF325296; -.
DR   Reactome; R-MMU-417973; Adenosine P1 receptors.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-5683826; Surfactant metabolism.
DR   BioGRID-ORCS; 11541; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Adora2b; mouse.
DR   PRO; PR:Q60614; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q60614; Protein.
DR   Bgee; ENSMUSG00000018500; Expressed in gastrula and 125 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IMP:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI.
DR   GO; GO:0019934; P:cGMP-mediated signaling; IMP:MGI.
DR   GO; GO:0043303; P:mast cell degranulation; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR   GO; GO:0033605; P:positive regulation of catecholamine secretion; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IMP:MGI.
DR   GO; GO:0032722; P:positive regulation of chemokine production; IMP:MGI.
DR   GO; GO:0002882; P:positive regulation of chronic inflammatory response to non-antigenic stimulus; IMP:MGI.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:MGI.
DR   GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISO:MGI.
DR   GO; GO:0010893; P:positive regulation of steroid biosynthetic process; ISO:MGI.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:MGI.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; ISO:MGI.
DR   GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IMP:MGI.
DR   GO; GO:1990776; P:response to angiotensin; ISO:MGI.
DR   GO; GO:0042311; P:vasodilation; ISO:MGI.
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; Q60614; MM.
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_0000069004"
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   CONFLICT        169
FT                   /note="V -> L (in Ref. 1; AAA19001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="R -> S (in Ref. 1; AAA19001)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   332 AA;  36120 MW;  BABE2C782001564A CRC64;
     MQLETQDALY VALELVIAAL AVAGNVLVCA AVGASSALQT PTNYFLVSLA TADVAVGLFA
     IPFAITISLG FCTDFHGCLF LACFVLVLTQ SSIFSLLAVA VDRYLAIRVP LRYKGLVTGT
     RARGIIAVLW VLAFGIGLTP FLGWNSKDSA TSNCTELGDG IANKSCCPVT CLFENVVPMS
     YMVYFNFFGC VLPPLLIMLV IYIKIFMVAC KQLQRMELMD HSRTTLQREI HAAKSLAMIV
     GIFALCWLPV HAINCITLFH PALAKDKPKW VMNVAILLSH ANSVVNPIVY AYRNRDFRYS
     FHKIISRYVL CQAETKGGSG QAGAQSTLSL GL
//