AA2AR_HUMAN
ID AA2AR_HUMAN Reviewed; 412 AA.
AC P29274; B2R7E0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Adenosine receptor A2a;
GN Name=ADORA2A; Synonyms=ADORA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tiffany H.L., Murphy P.M.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Salvatore C.A., Luneau C.J., Johnson R.G., Jacobson M.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RX PubMed=1331670; DOI=10.1016/0169-328x(92)90152-2;
RA Furlong T.J., Pierce K.D., Selbie L.A., Shine J.;
RT "Molecular characterization of a human brain adenosine A2 receptor.";
RL Brain Res. Mol. Brain Res. 15:62-66(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8670304; DOI=10.1006/bbrc.1996.0916;
RA Le F., Townsend-Nicholson A., Baker E., Sutherland G.R., Schofield P.R.;
RT "Characterization and chromosomal localization of the human A2a adenosine
RT receptor gene: ADORA2A.";
RL Biochem. Biophys. Res. Commun. 223:461-467(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [11]
RP INTERACTION WITH NECAB2.
RX PubMed=17689978; DOI=10.1016/j.mcn.2007.05.007;
RA Canela L., Lujan R., Lluis C., Burgueno J., Mallol J., Canela E.I.,
RA Franco R., Ciruela F.;
RT "The neuronal Ca(2+) -binding protein 2 (NECAB2) interacts with the
RT adenosine A(2A) receptor and modulates the cell surface expression and
RT function of the receptor.";
RL Mol. Cell. Neurosci. 36:1-12(2007).
RN [12]
RP POSSIBLE INTERACTION WITH DRD4.
RX PubMed=20836733; DOI=10.3109/10799893.2010.513842;
RA Woods A.S.;
RT "The dopamine D(4) receptor, the ultimate disordered protein.";
RL J. Recept. Signal Transduct. 30:331-336(2010).
RN [13]
RP 3D-STRUCTURE MODELING OF TRANSMEMBRANE DOMAINS.
RX PubMed=7775460; DOI=10.1074/jbc.270.23.13987;
RA Kim J., Wess J., van Rhee A.M., Schoneberg T., Jacobson K.A.;
RT "Site-directed mutagenesis identifies residues involved in ligand
RT recognition in the human A2a adenosine receptor.";
RL J. Biol. Chem. 270:13987-13997(1995).
RN [14]
RP INTERACTION WITH USP4, UBIQUITINATION, AND DEUBIQUITINATION BY USP4.
RX PubMed=16339847; DOI=10.1124/mol.105.015818;
RA Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M.,
RA Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.;
RT "The ubiquitin-specific protease Usp4 regulates the cell surface level of
RT the A2A receptor.";
RL Mol. Pharmacol. 69:1083-1094(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-316 IN COMPLEX WITH ANTAGONIST,
RP TOPOLOGY, AND DISULFIDE BONDS.
RX PubMed=18832607; DOI=10.1126/science.1164772;
RA Jaakola V.-P., Griffith M.T., Hanson M.A., Cherezov V., Chien E.Y.T.,
RA Lane J.R., Ijzerman A.P., Stevens R.C.;
RT "The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound
RT to an antagonist.";
RL Science 322:1211-1217(2008).
RN [16] {ECO:0007744|PDB:2YDO, ECO:0007744|PDB:2YDV}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-317 IN COMPLEXES WITH
RP ENDOGENOUS AGONIST ADENOSINE AND SYNTHETIC AGONIST NECA.
RX PubMed=21593763; DOI=10.1038/nature10136;
RA Lebon G., Warne T., Edwards P.C., Bennett K., Langmead C.J., Leslie A.G.,
RA Tate C.G.;
RT "Agonist-bound adenosine A2A receptor structures reveal common features of
RT GPCR activation.";
RL Nature 474:521-525(2011).
RN [17]
RP VARIANT VAL-50.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [18]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
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 (PubMed:16339847). May interact with DRD4
CC (PubMed:18832607). Interacts with NECAB2 (PubMed:17689978). Interacts
CC (via cytoplasmic C-terminal domain) with GAS2L2; interaction enhances
CC receptor-mediated adenylyl cyclase activity (By similarity).
CC {ECO:0000250|UniProtKB:P30543, ECO:0000269|PubMed:16339847,
CC ECO:0000269|PubMed:17689978, ECO:0000269|PubMed:18832607}.
CC -!- INTERACTION:
CC P29274; P30542: ADORA1; NbExp=4; IntAct=EBI-2902702, EBI-2903663;
CC P29274; P29274: ADORA2A; NbExp=8; IntAct=EBI-2902702, EBI-2902702;
CC P29274; P29275: ADORA2B; NbExp=5; IntAct=EBI-2902702, EBI-3904751;
CC P29274; O15155: BET1; NbExp=3; IntAct=EBI-2902702, EBI-749204;
CC P29274; P21554: CNR1; NbExp=8; IntAct=EBI-2902702, EBI-2909859;
CC P29274; Q99418: CYTH2; NbExp=6; IntAct=EBI-2902702, EBI-448974;
CC P29274; O15354: GPR37; NbExp=3; IntAct=EBI-2902702, EBI-15639515;
CC P29274; Q7Z6G3: NECAB2; NbExp=6; IntAct=EBI-2902702, EBI-950070;
CC P29274; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-2902702, EBI-12187159;
CC P29274; Q13107: USP4; NbExp=4; IntAct=EBI-2902702, EBI-723290;
CC P29274; Q5T9L3-1: WLS; NbExp=3; IntAct=EBI-2902702, EBI-22114623;
CC P29274; P31424-1: Grm5; Xeno; NbExp=3; IntAct=EBI-2902702, EBI-2902778;
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 -!- PTM: Ubiquitinated. Deubiquitinated by USP4; leading to stabilization
CC and expression at the cell surface. {ECO:0000269|PubMed:16339847}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58356.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M97370; AAA58356.1; ALT_INIT; mRNA.
DR EMBL; X68486; CAA48504.1; -; mRNA.
DR EMBL; S46950; AAB23956.1; -; mRNA.
DR EMBL; U40771; AAA83270.1; -; Genomic_DNA.
DR EMBL; U40770; AAA83270.1; JOINED; Genomic_DNA.
DR EMBL; AY136747; AAN01273.1; -; mRNA.
DR EMBL; CR456367; CAG30253.1; -; mRNA.
DR EMBL; BT006999; AAP35645.1; -; mRNA.
DR EMBL; AK312946; BAG35787.1; -; mRNA.
DR EMBL; CH471095; EAW59658.1; -; Genomic_DNA.
DR EMBL; BC013780; AAH13780.1; -; mRNA.
DR CCDS; CCDS13826.1; -.
DR PIR; A48978; A48978.
DR RefSeq; NP_000666.2; NM_000675.5.
DR RefSeq; NP_001265426.1; NM_001278497.1.
DR RefSeq; NP_001265427.1; NM_001278498.1.
DR RefSeq; NP_001265428.1; NM_001278499.1.
DR RefSeq; NP_001265429.1; NM_001278500.1.
DR PDB; 2YDO; X-ray; 3.00 A; A=1-317.
DR PDB; 2YDV; X-ray; 2.60 A; A=1-317.
DR PDB; 3EML; X-ray; 2.60 A; A=2-208, A=222-316.
DR PDB; 3PWH; X-ray; 3.30 A; A=1-317.
DR PDB; 3QAK; X-ray; 2.71 A; A=2-208, A=222-316.
DR PDB; 3REY; X-ray; 3.31 A; A=1-317.
DR PDB; 3RFM; X-ray; 3.60 A; A=1-317.
DR PDB; 3UZA; X-ray; 3.27 A; A=1-317.
DR PDB; 3UZC; X-ray; 3.34 A; A=1-317.
DR PDB; 3VG9; X-ray; 2.70 A; A=1-316.
DR PDB; 3VGA; X-ray; 3.10 A; A=1-316.
DR PDB; 4EIY; X-ray; 1.80 A; A=2-208, A=219-316.
DR PDB; 4UG2; X-ray; 2.60 A; A/B=1-317.
DR PDB; 4UHR; X-ray; 2.60 A; A=1-317.
DR PDB; 5G53; X-ray; 3.40 A; A/B=1-308.
DR PDB; 5IU4; X-ray; 1.72 A; A=2-208, A=219-318.
DR PDB; 5IU7; X-ray; 1.90 A; A=2-208, A=219-315.
DR PDB; 5IU8; X-ray; 2.00 A; A=2-208, A=219-315.
DR PDB; 5IUA; X-ray; 2.20 A; A=2-208, A=219-315.
DR PDB; 5IUB; X-ray; 2.10 A; A=2-208, A=219-315.
DR PDB; 5JTB; X-ray; 2.80 A; A=2-212, A=219-316.
DR PDB; 5K2A; X-ray; 2.50 A; A=2-208, A=219-316.
DR PDB; 5K2B; X-ray; 2.50 A; A=2-208, A=219-316.
DR PDB; 5K2C; X-ray; 1.90 A; A=2-208, A=219-316.
DR PDB; 5K2D; X-ray; 1.90 A; A=2-208, A=219-316.
DR PDB; 5MZJ; X-ray; 2.00 A; A=2-208, A=219-318.
DR PDB; 5MZP; X-ray; 2.10 A; A=2-208, A=219-317.
DR PDB; 5N2R; X-ray; 2.80 A; A=2-208, A=219-318.
DR PDB; 5NLX; X-ray; 2.14 A; A=2-317.
DR PDB; 5NM2; X-ray; 1.95 A; A=2-317.
DR PDB; 5NM4; X-ray; 1.70 A; A=2-317.
DR PDB; 5OLG; X-ray; 1.87 A; A=2-208, A=219-317.
DR PDB; 5OLH; X-ray; 2.60 A; A=2-208, A=219-317.
DR PDB; 5OLO; X-ray; 3.10 A; A=2-208, A=219-318.
DR PDB; 5OLV; X-ray; 2.00 A; A=2-208, A=219-317.
DR PDB; 5OLZ; X-ray; 1.90 A; A=2-208, A=219-317.
DR PDB; 5OM1; X-ray; 2.10 A; A=2-208, A=219-317.
DR PDB; 5OM4; X-ray; 2.00 A; A=2-208, A=219-317.
DR PDB; 5UIG; X-ray; 3.50 A; A=1-191, A=219-316.
DR PDB; 5UVI; X-ray; 3.20 A; A=2-212, A=219-316.
DR PDB; 5VRA; X-ray; 2.35 A; A=2-208, A=219-316.
DR PDB; 5WF5; X-ray; 2.60 A; A=2-208, A=222-316.
DR PDB; 5WF6; X-ray; 2.90 A; A=2-208, A=222-316.
DR PDB; 6AQF; X-ray; 2.51 A; A=2-208, A=219-316.
DR PDB; 6GDG; EM; 4.11 A; A=8-316.
DR PDB; 6GT3; X-ray; 2.00 A; A=2-208, A=219-317.
DR PDB; 6JZH; X-ray; 2.25 A; A=2-208, A=219-316.
DR PDB; 6LPJ; X-ray; 1.80 A; A=2-208, A=219-316.
DR PDB; 6LPK; X-ray; 1.80 A; A=2-208, A=219-316.
DR PDB; 6LPL; X-ray; 2.00 A; A=2-208, A=219-316.
DR PDB; 6MH8; X-ray; 4.20 A; A=2-208, A=219-316.
DR PDB; 6PS7; X-ray; 1.85 A; A=2-208, A=219-316.
DR PDB; 6S0L; X-ray; 2.65 A; A=2-317.
DR PDB; 6S0Q; X-ray; 2.65 A; A=2-208, A=219-317.
DR PDB; 6WQA; X-ray; 2.00 A; A=2-208, A=219-316.
DR PDB; 6ZDR; X-ray; 1.92 A; A=2-208, A=219-317.
DR PDB; 6ZDV; X-ray; 2.13 A; A=2-208, A=219-317.
DR PDB; 7ARO; X-ray; 3.12 A; A=2-208, A=219-317.
DR PDB; 7EZC; X-ray; 3.80 A; A/B=2-208, A/B=219-308.
DR PDB; 7PX4; X-ray; 2.25 A; A=2-208, A=219-316.
DR PDB; 7PYR; X-ray; 2.60 A; A=2-208, A=219-316.
DR PDB; 7RM5; EM; 2.79 A; A=2-208, A=219-316.
DR PDBsum; 2YDO; -.
DR PDBsum; 2YDV; -.
DR PDBsum; 3EML; -.
DR PDBsum; 3PWH; -.
DR PDBsum; 3QAK; -.
DR PDBsum; 3REY; -.
DR PDBsum; 3RFM; -.
DR PDBsum; 3UZA; -.
DR PDBsum; 3UZC; -.
DR PDBsum; 3VG9; -.
DR PDBsum; 3VGA; -.
DR PDBsum; 4EIY; -.
DR PDBsum; 4UG2; -.
DR PDBsum; 4UHR; -.
DR PDBsum; 5G53; -.
DR PDBsum; 5IU4; -.
DR PDBsum; 5IU7; -.
DR PDBsum; 5IU8; -.
DR PDBsum; 5IUA; -.
DR PDBsum; 5IUB; -.
DR PDBsum; 5JTB; -.
DR PDBsum; 5K2A; -.
DR PDBsum; 5K2B; -.
DR PDBsum; 5K2C; -.
DR PDBsum; 5K2D; -.
DR PDBsum; 5MZJ; -.
DR PDBsum; 5MZP; -.
DR PDBsum; 5N2R; -.
DR PDBsum; 5NLX; -.
DR PDBsum; 5NM2; -.
DR PDBsum; 5NM4; -.
DR PDBsum; 5OLG; -.
DR PDBsum; 5OLH; -.
DR PDBsum; 5OLO; -.
DR PDBsum; 5OLV; -.
DR PDBsum; 5OLZ; -.
DR PDBsum; 5OM1; -.
DR PDBsum; 5OM4; -.
DR PDBsum; 5UIG; -.
DR PDBsum; 5UVI; -.
DR PDBsum; 5VRA; -.
DR PDBsum; 5WF5; -.
DR PDBsum; 5WF6; -.
DR PDBsum; 6AQF; -.
DR PDBsum; 6GDG; -.
DR PDBsum; 6GT3; -.
DR PDBsum; 6JZH; -.
DR PDBsum; 6LPJ; -.
DR PDBsum; 6LPK; -.
DR PDBsum; 6LPL; -.
DR PDBsum; 6MH8; -.
DR PDBsum; 6PS7; -.
DR PDBsum; 6S0L; -.
DR PDBsum; 6S0Q; -.
DR PDBsum; 6WQA; -.
DR PDBsum; 6ZDR; -.
DR PDBsum; 6ZDV; -.
DR PDBsum; 7ARO; -.
DR PDBsum; 7EZC; -.
DR PDBsum; 7PX4; -.
DR PDBsum; 7PYR; -.
DR PDBsum; 7RM5; -.
DR AlphaFoldDB; P29274; -.
DR SMR; P29274; -.
DR BioGRID; 106647; 26.
DR IntAct; P29274; 23.
DR MINT; P29274; -.
DR STRING; 9606.ENSP00000480012; -.
DR BindingDB; P29274; -.
DR ChEMBL; CHEMBL251; -.
DR DrugBank; DB08770; 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol.
DR DrugBank; DB14132; 8-chlorotheophylline.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB05009; Apadenoson.
DR DrugBank; DB05191; Atl146e.
DR DrugBank; DB04853; Binodenoson.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB04932; Defibrotide.
DR DrugBank; DB09273; Doxofylline.
DR DrugBank; DB00651; Dyphylline.
DR DrugBank; DB00824; Enprofylline.
DR DrugBank; DB11757; Istradefylline.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB00358; Mefloquine.
DR DrugBank; DB01303; Oxtriphylline.
DR DrugBank; DB00806; Pentoxifylline.
DR DrugBank; DB06213; Regadenoson.
DR DrugBank; DB01412; Theobromine.
DR DrugBank; DB00277; Theophylline.
DR DrugCentral; P29274; -.
DR GuidetoPHARMACOLOGY; 19; -.
DR TCDB; 9.A.14.3.8; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P29274; 1 site.
DR iPTMnet; P29274; -.
DR PhosphoSitePlus; P29274; -.
DR BioMuta; ADORA2A; -.
DR DMDM; 543740; -.
DR MassIVE; P29274; -.
DR PaxDb; P29274; -.
DR PeptideAtlas; P29274; -.
DR PRIDE; P29274; -.
DR ProteomicsDB; 54531; -.
DR ABCD; P29274; 3 sequenced antibodies.
DR Antibodypedia; 9718; 447 antibodies from 41 providers.
DR DNASU; 135; -.
DR Ensembl; ENST00000337539.12; ENSP00000336630.6; ENSG00000128271.22.
DR Ensembl; ENST00000610595.4; ENSP00000480012.1; ENSG00000128271.22.
DR Ensembl; ENST00000611543.4; ENSP00000483102.1; ENSG00000128271.22.
DR Ensembl; ENST00000618076.3; ENSP00000481552.1; ENSG00000128271.22.
DR GeneID; 135; -.
DR KEGG; hsa:135; -.
DR MANE-Select; ENST00000337539.12; ENSP00000336630.6; NM_000675.6; NP_000666.2.
DR CTD; 135; -.
DR DisGeNET; 135; -.
DR GeneCards; ADORA2A; -.
DR HGNC; HGNC:263; ADORA2A.
DR HPA; ENSG00000128271; Tissue enhanced (bone marrow, brain, lymphoid tissue).
DR MalaCards; ADORA2A; -.
DR MIM; 102776; gene.
DR neXtProt; NX_P29274; -.
DR OpenTargets; ENSG00000128271; -.
DR Orphanet; 363549; Acute encephalopathy with biphasic seizures and late reduced diffusion.
DR PharmGKB; PA24584; -.
DR VEuPathDB; HostDB:ENSG00000128271; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR InParanoid; P29274; -.
DR OMA; GQQEPFK; -.
DR OrthoDB; 550297at2759; -.
DR PhylomeDB; P29274; -.
DR TreeFam; TF325296; -.
DR PathwayCommons; P29274; -.
DR Reactome; R-HSA-187024; NGF-independant TRKA activation.
DR Reactome; R-HSA-417973; Adenosine P1 receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P29274; -.
DR SIGNOR; P29274; -.
DR BioGRID-ORCS; 135; 11 hits in 1071 CRISPR screens.
DR EvolutionaryTrace; P29274; -.
DR GeneWiki; Adenosine_A2A_receptor; -.
DR GenomeRNAi; 135; -.
DR Pharos; P29274; Tclin.
DR PRO; PR:P29274; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P29274; protein.
DR Bgee; ENSG00000128271; Expressed in putamen and 93 other tissues.
DR ExpressionAtlas; P29274; baseline and differential.
DR Genevisible; P29274; HS.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0012505; C:endomembrane system; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR GO; GO:0110148; P:biomineralization; IDA:MGI.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; 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:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
DR GO; GO:0046636; P:negative regulation of alpha-beta T cell activation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0040013; P:negative regulation of locomotion; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; TAS:ProtInc.
DR GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IEA:Ensembl.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl.
DR GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0014061; P:regulation of norepinephrine secretion; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR GO; GO:0014074; P:response to purine-containing compound; IDA:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007600; P:sensory perception; TAS:ProtInc.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IEA:Ensembl.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR DisProt; DP01547; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..412
FT /note="Adenosine receptor A2a"
FT /id="PRO_0000068999"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18832607"
FT TRANSMEM 8..32
FT /note="Helical; Name=1"
FT TOPO_DOM 33..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18832607"
FT TRANSMEM 43..66
FT /note="Helical; Name=2"
FT TOPO_DOM 67..77
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18832607"
FT TRANSMEM 78..100
FT /note="Helical; Name=3"
FT TOPO_DOM 101..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18832607"
FT TRANSMEM 121..143
FT /note="Helical; Name=4"
FT TOPO_DOM 144..173
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18832607"
FT TRANSMEM 174..198
FT /note="Helical; Name=5"
FT TOPO_DOM 199..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18832607"
FT TRANSMEM 235..258
FT /note="Helical; Name=6"
FT TOPO_DOM 259..266
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18832607"
FT TRANSMEM 267..290
FT /note="Helical; Name=7"
FT TOPO_DOM 291..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18832607"
FT REGION 391..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:0000269|PubMed:21593763,
FT ECO:0007744|PDB:2YDO"
FT BINDING 253
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:21593763,
FT ECO:0007744|PDB:2YDO"
FT BINDING 277
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:21593763,
FT ECO:0007744|PDB:2YDO"
FT BINDING 278
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:21593763,
FT ECO:0007744|PDB:2YDO"
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 ECO:0000269|PubMed:18832607"
FT DISULFID 74..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:18832607"
FT DISULFID 77..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:18832607"
FT DISULFID 259..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:18832607"
FT VARIANT 50
FT /note="A -> V (in dbSNP:rs4530)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011835"
FT VARIANT 300
FT /note="R -> H (in dbSNP:rs4990)"
FT /id="VAR_011836"
FT VARIANT 392
FT /note="G -> R (in dbSNP:rs1277013918)"
FT /id="VAR_003451"
FT HELIX 2..33
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 40..57
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:5NM4"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 74..107
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:5NM4"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:7RM5"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:5NM4"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 187..208
FT /evidence="ECO:0007829|PDB:5NM4"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3VGA"
FT HELIX 219..258
FT /evidence="ECO:0007829|PDB:5NM4"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2YDV"
FT HELIX 267..291
FT /evidence="ECO:0007829|PDB:5NM4"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:5NM4"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:3QAK"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:2YDV"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:2YDV"
SQ SEQUENCE 412 AA; 44707 MW; 9438E9D64A6BE61B CRC64;
MPIMGSSVYI TVELAIAVLA ILGNVLVCWA VWLNSNLQNV TNYFVVSLAA ADIAVGVLAI
PFAITISTGF CAACHGCLFI ACFVLVLTQS SIFSLLAIAI DRYIAIRIPL RYNGLVTGTR
AKGIIAICWV LSFAIGLTPM LGWNNCGQPK EGKNHSQGCG EGQVACLFED VVPMNYMVYF
NFFACVLVPL LLMLGVYLRI FLAARRQLKQ MESQPLPGER ARSTLQKEVH AAKSLAIIVG
LFALCWLPLH IINCFTFFCP DCSHAPLWLM YLAIVLSHTN SVVNPFIYAY RIREFRQTFR
KIIRSHVLRQ QEPFKAAGTS ARVLAAHGSD GEQVSLRLNG HPPGVWANGS APHPERRPNG
YALGLVSGGS AQESQGNTGL PDVELLSHEL KGVCPEPPGL DDPLAQDGAG VS
