AA2AR_CAVPO
ID AA2AR_CAVPO Reviewed; 409 AA.
AC P46616;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Adenosine receptor A2a;
GN Name=ADORA2A;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Leukocyte;
RX PubMed=8645236; DOI=10.1042/bj3160081;
RA Hirano D., Ogasawara H., Kodama H., Waga I., Sakanaka C., Shimizu T.,
RA Nakamura M.;
RT "Functional coupling of adenosine A2a receptor to inhibition of the
RT mitogen-activated protein kinase cascade in Chinese hamster ovary cells.";
RL Biochem. J. 316:81-86(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Brain;
RX PubMed=8065518; DOI=10.1007/bf00971338;
RA Meng F., Xie G.X., Chalmers D., Morgan C., Watson S.J., Akil H.;
RT "Cloning and expression of the A2a adenosine receptor from guinea pig
RT brain.";
RL Neurochem. Res. 19:613-621(1994).
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 (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; D63674; BAA09825.1; -; mRNA.
DR EMBL; U04201; AAA18421.1; -; mRNA.
DR PIR; I48095; I48095.
DR PIR; S68247; S68247.
DR RefSeq; NP_001166204.1; NM_001172733.1.
DR AlphaFoldDB; P46616; -.
DR SMR; P46616; -.
DR STRING; 10141.ENSCPOP00000018786; -.
DR BindingDB; P46616; -.
DR ChEMBL; CHEMBL2605; -.
DR DrugCentral; P46616; -.
DR GeneID; 100135473; -.
DR KEGG; cpoc:100135473; -.
DR CTD; 135; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P46616; -.
DR OrthoDB; 550297at2759; -.
DR PRO; PR:P46616; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IEA:InterPro.
DR GO; GO:0010646; P:regulation of cell communication; IEA:UniProt.
DR GO; GO:0023051; P:regulation of signaling; IEA:UniProt.
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..409
FT /note="Adenosine receptor A2a"
FT /id="PRO_0000068997"
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..170
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 171..195
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 196..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 232..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 256..263
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 264..287
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 288..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 250
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 274
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P29274"
FT BINDING 275
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 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 71..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 74..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 256..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 94
FT /note="T -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="T -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="P -> A (in Ref. 2; AAA18421)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="C -> W (in Ref. 2; AAA18421)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="N -> H (in Ref. 2; AAA18421)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> G (in Ref. 2; AAA18421)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="YL -> SM (in Ref. 2; AAA18421)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="L -> P (in Ref. 2; AAA18421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44943 MW; C4263E63B9000633 CRC64;
MSSSVYITVE LVIAVLAILG NVLVCWAVWI NSNLQNVTNY FVVSLAAADI AVGVLAIPFA
ITISTGFCAA CHGCLFFACF VLVLTQSSIF SLLTITIDRY IAIRIPLRYN GLVTCTRAKG
IIAICWVLSF AIGLTPMLGW NNCSQPKGDK NHSESCDEGQ VTCLFEDVVP MNYMVYYNFF
AFVLVPLLLM LGIYLRIFLA ARRQLKQMES QPLPGERTRS TLQKEVHPAK SLAIIVGLFA
LCCLPLNIIN CFTFFCPECD HAPPWLMYLT IILSHGNSVV NPLIYAYRIR EFRQTFRKII
RSHILRRREL FKAGGTSARA SAAHSPEGEQ VSLRLNGHPP GVWANGSALR PEQRPNGYVL
GLVSGRSAQR SHGDASLSDV ELLSHEHKGT CPESPSLEDP PAHGGAGVS
