AA2AR_CANLF
ID AA2AR_CANLF Reviewed; 412 AA.
AC P11617;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Adenosine receptor A2a;
GN Name=ADORA2A; Synonyms=RDC8;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2541503; DOI=10.1126/science.2541503;
RA Libert F., Parmentier M., Lefort A., Dinsart C., van Sande J., Maenhaut C.,
RA Simons M.-J., Dumont J.E., Vassart G.;
RT "Selective amplification and cloning of four new members of the G protein-
RT coupled receptor family.";
RL Science 244:569-572(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2159628; DOI=10.1093/nar/18.7.1914;
RA Libert F., Parmentier M., Lefort A., Dumont J.E., Vassart G.;
RT "Complete nucleotide sequence of a putative G protein coupled receptor:
RT RDC8.";
RL Nucleic Acids Res. 18:1914-1914(1990).
RN [3]
RP FUNCTION.
RX PubMed=2125216; DOI=10.1016/s0006-291x(05)80909-x;
RA Maenhaut C., van Sande J., Libert F., Abramowicz M., Parmentier M.,
RA Vanderhaegen J.-J., Dumont J.E., Vassart G., Schiffmann S.;
RT "RDC8 codes for an adenosine A2 receptor with physiological constitutive
RT activity.";
RL Biochem. Biophys. Res. Commun. 173:1169-1178(1990).
CC -!- FUNCTION: Receptor for adenosine (PubMed:2125216). The activity of this
CC receptor is mediated by G proteins which activate adenylyl cyclase
CC (PubMed:2125216). {ECO:0000269|PubMed:2125216}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P29274, ECO:0000250|UniProtKB:P30543}.
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; X14052; CAA32210.1; -; mRNA.
DR PIR; D30341; D30341.
DR RefSeq; NP_001003278.1; NM_001003278.1.
DR AlphaFoldDB; P11617; -.
DR SMR; P11617; -.
DR STRING; 9615.ENSCAFP00000020374; -.
DR iPTMnet; P11617; -.
DR PaxDb; P11617; -.
DR Ensembl; ENSCAFT00030040239; ENSCAFP00030035115; ENSCAFG00030021927.
DR Ensembl; ENSCAFT00040033703; ENSCAFP00040029336; ENSCAFG00040018245.
DR Ensembl; ENSCAFT00845039604; ENSCAFP00845031026; ENSCAFG00845022393.
DR GeneID; 403960; -.
DR KEGG; cfa:403960; -.
DR CTD; 135; -.
DR VEuPathDB; HostDB:ENSCAFG00845022393; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; P11617; -.
DR OMA; GQQEPFK; -.
DR OrthoDB; 550297at2759; -.
DR TreeFam; TF325296; -.
DR Reactome; R-CFA-417973; Adenosine P1 receptors.
DR Reactome; R-CFA-418555; G alpha (s) signalling events.
DR Reactome; R-CFA-5683826; Surfactant metabolism.
DR Proteomes; UP000002254; Chromosome 26.
DR Bgee; ENSCAFG00000013828; Expressed in granulocyte and 46 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0110148; P:biomineralization; IEA:Ensembl.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0046636; P:negative regulation of alpha-beta T cell activation; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR GO; GO:0014074; P:response to purine-containing compound; IEA:Ensembl.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl.
DR InterPro; IPR001513; Adeno_A2A_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; PR00553; ADENOSINA2AR.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..412
FT /note="Adenosine receptor A2a"
FT /id="PRO_0000068996"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 8..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 33..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 43..66
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 67..77
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 78..100
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 101..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 121..143
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 144..173
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 174..198
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 199..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 235..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 259..266
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 267..290
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 291..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 392..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 253
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 277
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 278
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 74..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 77..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 259..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 412 AA; 45061 MW; EB1B094AD581C6A7 CRC64;
MSTMGSWVYI TVELAIAVLA ILGNVLVCWA VWLNSNLQNV TNYFVVSLAA ADIAVGVLAI
PFAITISTGF CAACHNCLFF ACFVLVLTQS SIFSLLAIAI DRYIAIRIPL RYNGLVTGTR
AKGIIAVCWV LSFAIGLTPM LGWNNCSQPK EGRNYSQGCG EGQVACLFED VVPMNYMVYY
NFFAFVLVPL LLMLGVYLRI FLAARRQLKQ MESQPLPGER ARSTLQKEVH AAKSLAIIVG
LFALCWLPLH IINCFTFFCP ECSHAPLWLM YLTIVLSHTN SVVNPFIYAY RIREFRQTFR
KIIRSHVLRR REPFKAGGTS ARALAAHGSD GEQISLRLNG HPPGVWANGS APHPERRPNG
YTLGLVSGGI APESHGDMGL PDVELLSHEL KGACPESPGL EGPLAQDGAG VS
