AA2BR_MOUSE
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 03-AUG-2022, entry version 160.
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 GlyGen; Q60614; 2 sites.
DR iPTMnet; Q60614; -.
DR PhosphoSitePlus; Q60614; -.
DR SwissPalm; Q60614; -.
DR PaxDb; Q60614; -.
DR PRIDE; Q60614; -.
DR ProteomicsDB; 296428; -.
DR Antibodypedia; 25203; 315 antibodies from 37 providers.
DR DNASU; 11541; -.
DR Ensembl; ENSMUST00000018644; ENSMUSP00000018644; ENSMUSG00000018500.
DR GeneID; 11541; -.
DR KEGG; mmu:11541; -.
DR UCSC; uc007jio.1; mouse.
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; PVKCLFE; -.
DR OrthoDB; 550297at2759; -.
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 74 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 121 other tissues.
DR Genevisible; Q60614; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP: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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:0031284; P:positive regulation of guanylate cyclase activity; IMP: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:0010906; P:regulation of glucose metabolic process; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
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 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_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
