ID   AA2AR_MOUSE             Reviewed;         410 AA.
AC   Q60613; Q2NLC1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Adenosine receptor A2a;
GN   Name=Adora2a;
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 [GENOMIC DNA / MRNA].
RC   STRAIN=129/Sv;
RX   PubMed=9262401; DOI=10.1038/41771;
RA   Ledent C., Vaugeois J.M., Schiffmann S.N., Pedrazzini T., El-Yacoubi M.,
RA   Vanderhaeghen J.J., Costentin J., Heath J.K., Vassart G., Parmentier M.;
RT   "Aggressiveness, hypoalgesia and high blood pressure in mice lacking the
RT   adenosine A2a receptor.";
RL   Nature 388:674-678(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Jaw;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 53-213.
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   [5]
RP   INTERACTION WITH GAS2L2.
RX   PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA   Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT   "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT   of the A2A adenosine receptor.";
RL   Biochim. Biophys. Acta 1833:3145-3154(2013).
CC   -!- FUNCTION: Receptor for adenosine (By similarity). The activity of this
CC       receptor is mediated by G proteins which activate adenylyl cyclase (By
CC       similarity). {ECO:0000250|UniProtKB:P11617}.
CC   -!- SUBUNIT: Interacts (via cytoplasmic C-terminal domain) with USP4; the
CC       interaction is direct (By similarity). May interact with DRD4 (By
CC       similarity). Interacts with NECAB2 (By similarity). Interacts (via
CC       cytoplasmic C-terminal domain) with GAS2L2; interaction enhances
CC       receptor-mediated adenylyl cyclase activity (PubMed:23994616).
CC       {ECO:0000250|UniProtKB:P29274, ECO:0000269|PubMed:23994616}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30543};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P30543}.
CC       Note=Colocalizes with GAS2L2 at neuronal processes.
CC       {ECO:0000250|UniProtKB:P30543}.
CC   -!- DOMAIN: The cytoplasmic C-terminal domain is necessary for targeting
CC       the non-ubiquitinated form of this protein to the cell surface.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Deubiquitinated by USP4; leading to stabilization
CC       and expression at the cell surface (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; Y13344; CAA73787.1; -; Genomic_DNA.
DR   EMBL; Y13345; CAA73787.1; JOINED; Genomic_DNA.
DR   EMBL; Y13346; CAA73788.1; -; mRNA.
DR   EMBL; BC110692; AAI10693.1; -; mRNA.
DR   EMBL; CH466553; EDL31926.1; -; Genomic_DNA.
DR   EMBL; CH466553; EDL31927.1; -; Genomic_DNA.
DR   EMBL; U05672; AAA19000.1; -; mRNA.
DR   CCDS; CCDS23924.1; -.
DR   PIR; I48932; I48932.
DR   RefSeq; NP_001318024.1; NM_001331095.1.
DR   RefSeq; NP_001318025.1; NM_001331096.1.
DR   RefSeq; NP_033760.2; NM_009630.3.
DR   RefSeq; XP_006513156.1; XM_006513093.3.
DR   AlphaFoldDB; Q60613; -.
DR   SMR; Q60613; -.
DR   IntAct; Q60613; 3.
DR   STRING; 10090.ENSMUSP00000101060; -.
DR   BindingDB; Q60613; -.
DR   ChEMBL; CHEMBL2115; -.
DR   GuidetoPHARMACOLOGY; 19; -.
DR   GlyCosmos; Q60613; 2 sites, No reported glycans.
DR   GlyGen; Q60613; 2 sites.
DR   PhosphoSitePlus; Q60613; -.
DR   PaxDb; 10090-ENSMUSP00000101060; -.
DR   ProteomicsDB; 296427; -.
DR   Antibodypedia; 9718; 493 antibodies from 41 providers.
DR   DNASU; 11540; -.
DR   Ensembl; ENSMUST00000105420.3; ENSMUSP00000101060.2; ENSMUSG00000020178.7.
DR   GeneID; 11540; -.
DR   KEGG; mmu:11540; -.
DR   UCSC; uc007fqh.2; mouse.
DR   AGR; MGI:99402; -.
DR   CTD; 135; -.
DR   MGI; MGI:99402; Adora2a.
DR   VEuPathDB; HostDB:ENSMUSG00000020178; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234555; -.
DR   HOGENOM; CLU_009579_11_5_1; -.
DR   InParanoid; Q60613; -.
DR   OMA; VVISHCP; -.
DR   OrthoDB; 2909020at2759; -.
DR   PhylomeDB; Q60613; -.
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; 11540; 1 hit in 80 CRISPR screens.
DR   PRO; PR:Q60613; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q60613; Protein.
DR   Bgee; ENSMUSG00000020178; Expressed in caudate-putamen and 135 other cell types or tissues.
DR   ExpressionAtlas; Q60613; baseline and differential.
DR   GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR   GO; GO:0030673; C:axolemma; ISO:MGI.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR   GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR   GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008289; F:lipid binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; ISO:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0048143; P:astrocyte activation; ISO:MGI.
DR   GO; GO:0042755; P:eating behavior; IGI:MGI.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; ISO:MGI.
DR   GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0140928; P:inhibition of non-skeletal tissue mineralization; ISO:MGI.
DR   GO; GO:0060080; P:inhibitory postsynaptic potential; IGI:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IGI:MGI.
DR   GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR   GO; GO:0046636; P:negative regulation of alpha-beta T cell activation; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IGI:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR   GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; ISO:MGI.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; ISO:MGI.
DR   GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR   GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:MGI.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR   GO; GO:0035810; P:positive regulation of urine volume; ISO:MGI.
DR   GO; GO:0060134; P:prepulse inhibition; ISO:MGI.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
DR   GO; GO:0014061; P:regulation of norepinephrine secretion; ISO:MGI.
DR   GO; GO:0043279; P:response to alkaloid; ISO:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0031000; P:response to caffeine; ISO:MGI.
DR   GO; GO:0010035; P:response to inorganic substance; IMP:MGI.
DR   GO; GO:0014074; P:response to purine-containing compound; IMP:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:MGI.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IGI:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:MGI.
DR   GO; GO:0042311; P:vasodilation; ISO:MGI.
DR   CDD; cd15068; 7tmA_Adenosine_R_A2A; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001513; Adeno_A2A_rcpt.
DR   InterPro; IPR001634; Adenosn_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24246:SF47; ADENOSINE RECEPTOR A2A; 1.
DR   PANTHER; PTHR24246; OLFACTORY RECEPTOR AND ADENOSINE RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00553; ADENOSINA2AR.
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; Q60613; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..410
FT                   /note="Adenosine receptor A2a"
FT                   /id="PRO_0000069000"
FT   TOPO_DOM        1..4
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        5..29
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        30..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        40..63
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        64..74
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        75..97
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        98..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        118..140
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        141..168
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        169..193
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        194..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        230..253
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        254..261
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        262..285
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        286..410
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          322..410
FT                   /note="Interaction with GAS2L2"
FT                   /evidence="ECO:0000250|UniProtKB:P30543"
FT   REGION          342..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P29274"
FT   BINDING         248
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P29274"
FT   BINDING         272
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P29274"
FT   BINDING         273
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P29274"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        71..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        74..161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        254..257
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        77
FT                   /note="F -> I (in Ref. 1; CAA73787/CAA73788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="R -> K (in Ref. 1; CAA73787/CAA73788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137..138
FT                   /note="ML -> TA (in Ref. 4; AAA19000)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="K -> T (in Ref. 1; CAA73787/CAA73788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="K -> P (in Ref. 4; AAA19000)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  44971 MW;  E5670F442D243E71 CRC64;
     MGSSVYIMVE LAIAVLAILG NVLVCWAVWI NSNLQNVTNF FVVSLAAADI AVGVLAIPFA
     ITISTGFCAA CHGCLFFACF VLVLTQSSIF SLLAIAIDRY IAIRIPLRYN GLVTGMRAKG
     IIAICWVLSF AIGLTPMLGW NNCSQKDENS TKTCGEGRVT CLFEDVVPMN YMVYYNFFAF
     VLLPLLLMLA IYLRIFLAAR RQLKQMESQP LPGERTRSTL QKEVHAAKSL AIIVGLFALC
     WLPLHIINCF TFFCSTCQHA PPWLMYLAII LSHSNSVVNP FIYAYRIREF RQTFRKIIRT
     HVLRRQEPFR AGGSSAWALA AHSTEGEQVS LRLNGHPLGV WANGSAPHSG RRPNGYTLGP
     GGGGSTQGSP GDVELLTQEH QEGQEHPGLG DHLAQGRVGT ASWSSEFAPS
//