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Adenosine receptor A2a

 AA2AR_HUMAN             Reviewed;         412 AA.
P29274; B2R7E0;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
10-OCT-2018, entry version 197.
RecName: Full=Adenosine receptor A2a;
Name=ADORA2A; Synonyms=ADORA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Tiffany H.L., Murphy P.M.;
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Salvatore C.A., Luneau C.J., Johnson R.G., Jacobson M.;
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hippocampus;
PubMed=1331670; DOI=10.1016/0169-328X(92)90152-2;
Furlong T.J., Pierce K.D., Selbie L.A., Shine J.;
"Molecular characterization of a human brain adenosine A2 receptor.";
Brain Res. Mol. Brain Res. 15:62-66(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8670304; DOI=10.1006/bbrc.1996.0916;
Le F., Townsend-Nicholson A., Baker E., Sutherland G.R.,
Schofield P.R.;
"Characterization and chromosomal localization of the human A2a
adenosine receptor gene: ADORA2A.";
Biochem. Biophys. Res. Commun. 223:461-467(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
INTERACTION WITH NECAB2.
PubMed=17689978; DOI=10.1016/j.mcn.2007.05.007;
Canela L., Lujan R., Lluis C., Burgueno J., Mallol J., Canela E.I.,
Franco R., Ciruela F.;
"The neuronal Ca(2+) -binding protein 2 (NECAB2) interacts with the
adenosine A(2A) receptor and modulates the cell surface expression and
function of the receptor.";
Mol. Cell. Neurosci. 36:1-12(2007).
[12]
POSSIBLE INTERACTION WITH DRD4.
PubMed=20836733; DOI=10.3109/10799893.2010.513842;
Woods A.S.;
"The dopamine D(4) receptor, the ultimate disordered protein.";
J. Recept. Signal Transduct. 30:331-336(2010).
[13]
3D-STRUCTURE MODELING OF TRANSMEMBRANE DOMAINS.
PubMed=7775460; DOI=10.1074/jbc.270.23.13987;
Kim J., Wess J., van Rhee A.M., Schoneberg T., Jacobson K.A.;
"Site-directed mutagenesis identifies residues involved in ligand
recognition in the human A2a adenosine receptor.";
J. Biol. Chem. 270:13987-13997(1995).
[14]
INTERACTION WITH USP4, UBIQUITINATION, AND DEUBIQUITINATION BY USP4.
PubMed=16339847; DOI=10.1124/mol.105.015818;
Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M.,
Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.;
"The ubiquitin-specific protease Usp4 regulates the cell surface level
of the A2A receptor.";
Mol. Pharmacol. 69:1083-1094(2006).
[15]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-316 IN COMPLEX WITH
ANTAGONIST, TOPOLOGY, AND DISULFIDE BONDS.
PubMed=18832607; DOI=10.1126/science.1164772;
Jaakola V.-P., Griffith M.T., Hanson M.A., Cherezov V., Chien E.Y.T.,
Lane J.R., Ijzerman A.P., Stevens R.C.;
"The 2.6 angstrom crystal structure of a human A2A adenosine receptor
bound to an antagonist.";
Science 322:1211-1217(2008).
[16]
VARIANT VAL-50.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[17]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
-!- FUNCTION: Receptor for adenosine. The activity of this receptor is
mediated by G proteins which activate adenylyl cyclase.
-!- SUBUNIT: Interacts (via cytoplasmic C-terminal domain) with USP4;
the interaction is direct. May interact with DRD4. Interacts with
NECAB2. {ECO:0000269|PubMed:16339847, ECO:0000269|PubMed:17689978,
ECO:0000269|PubMed:18832607}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-2902702, EBI-2902702;
P30542:ADORA1; NbExp=4; IntAct=EBI-2902702, EBI-2903663;
P62158:CALM3; NbExp=3; IntAct=EBI-2902702, EBI-397435;
Q99418:CYTH2; NbExp=6; IntAct=EBI-2902702, EBI-448974;
P14416:DRD2; NbExp=2; IntAct=EBI-2902702, EBI-2928178;
P31424-1:Grm5 (xeno); NbExp=3; IntAct=EBI-2902702, EBI-2902778;
Q7Z6G3:NECAB2; NbExp=6; IntAct=EBI-2902702, EBI-950070;
Q13107:USP4; NbExp=4; IntAct=EBI-2902702, EBI-723290;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- DOMAIN: The cytoplasmic C-terminal domain is necessary for
targeting the non-ubiquitinated form of this protein to the cell
surface.
-!- PTM: Ubiquitinated. Deubiquitinated by USP4; leading to
stabilization and expression at the cell surface.
{ECO:0000269|PubMed:16339847}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=AAA58356.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M97370; AAA58356.1; ALT_INIT; mRNA.
EMBL; X68486; CAA48504.1; -; mRNA.
EMBL; S46950; AAB23956.1; -; mRNA.
EMBL; U40771; AAA83270.1; -; Genomic_DNA.
EMBL; U40770; AAA83270.1; JOINED; Genomic_DNA.
EMBL; AY136747; AAN01273.1; -; mRNA.
EMBL; CR456367; CAG30253.1; -; mRNA.
EMBL; BT006999; AAP35645.1; -; mRNA.
EMBL; AK312946; BAG35787.1; -; mRNA.
EMBL; CH471095; EAW59658.1; -; Genomic_DNA.
EMBL; BC013780; AAH13780.1; -; mRNA.
CCDS; CCDS13826.1; -.
PIR; A48978; A48978.
RefSeq; NP_000666.2; NM_000675.5.
RefSeq; NP_001265426.1; NM_001278497.1.
RefSeq; NP_001265427.1; NM_001278498.1.
RefSeq; NP_001265428.1; NM_001278499.1.
RefSeq; NP_001265429.1; NM_001278500.1.
UniGene; Hs.197029; -.
PDB; 1MMH; Model; -; 1=6-36, 2=42-69, 3=78-102, 4=117-143, 5=175-203, 6=233-260, 7=264-296.
PDB; 1UPE; Model; -; A=1-304.
PDB; 2YDO; X-ray; 3.00 A; A=1-317.
PDB; 2YDV; X-ray; 2.60 A; A=1-317.
PDB; 3EML; X-ray; 2.60 A; A=2-208, A=222-316.
PDB; 3PWH; X-ray; 3.30 A; A=1-317.
PDB; 3QAK; X-ray; 2.71 A; A=2-208, A=222-316.
PDB; 3REY; X-ray; 3.31 A; A=1-317.
PDB; 3RFM; X-ray; 3.60 A; A=1-317.
PDB; 3UZA; X-ray; 3.27 A; A=1-317.
PDB; 3UZC; X-ray; 3.34 A; A=1-317.
PDB; 3VG9; X-ray; 2.70 A; A=1-316.
PDB; 3VGA; X-ray; 3.10 A; A=1-316.
PDB; 4EIY; X-ray; 1.80 A; A=2-208, A=219-316.
PDB; 4UG2; X-ray; 2.60 A; A/B=1-317.
PDB; 4UHR; X-ray; 2.60 A; A=1-317.
PDB; 5G53; X-ray; 3.40 A; A/B=1-308.
PDB; 5IU4; X-ray; 1.72 A; A=2-208, A=219-318.
PDB; 5IU7; X-ray; 1.90 A; A=2-208, A=219-315.
PDB; 5IU8; X-ray; 2.00 A; A=2-208, A=219-315.
PDB; 5IUA; X-ray; 2.20 A; A=2-208, A=219-315.
PDB; 5IUB; X-ray; 2.10 A; A=2-208, A=219-315.
PDB; 5JTB; X-ray; 2.80 A; A=2-212, A=219-316.
PDB; 5K2A; X-ray; 2.50 A; A=2-208, A=219-316.
PDB; 5K2B; X-ray; 2.50 A; A=2-208, A=219-316.
PDB; 5K2C; X-ray; 1.90 A; A=2-208, A=219-316.
PDB; 5K2D; X-ray; 1.90 A; A=2-208, A=219-316.
PDB; 5MZJ; X-ray; 2.00 A; A=2-208, A=219-318.
PDB; 5MZP; X-ray; 2.10 A; A=2-208, A=219-317.
PDB; 5N2R; X-ray; 2.80 A; A=2-208, A=219-318.
PDB; 5NLX; X-ray; 2.14 A; A=2-317.
PDB; 5NM2; X-ray; 1.95 A; A=2-317.
PDB; 5NM4; X-ray; 1.70 A; A=2-317.
PDB; 5OLG; X-ray; 1.87 A; A=2-208, A=219-317.
PDB; 5OLH; X-ray; 2.60 A; A=2-208, A=219-317.
PDB; 5OLO; X-ray; 3.10 A; A=2-208, A=219-318.
PDB; 5OLV; X-ray; 2.00 A; A=2-208, A=219-317.
PDB; 5OLZ; X-ray; 1.90 A; A=2-208, A=219-317.
PDB; 5OM1; X-ray; 2.10 A; A=2-208, A=219-317.
PDB; 5OM4; X-ray; 2.00 A; A=2-208, A=219-317.
PDB; 5UIG; X-ray; 3.50 A; A=1-191, A=219-316.
PDB; 5UVI; X-ray; 3.20 A; A=2-212, A=219-316.
PDB; 5VRA; X-ray; 2.35 A; A=2-208, A=219-316.
PDB; 5WF5; X-ray; 2.60 A; A=2-208, A=222-316.
PDB; 5WF6; X-ray; 2.90 A; A=2-208, A=222-316.
PDB; 6AQF; X-ray; 2.51 A; A=2-208, A=219-316.
PDB; 6GDG; EM; 4.11 A; A=8-316.
PDBsum; 1MMH; -.
PDBsum; 1UPE; -.
PDBsum; 2YDO; -.
PDBsum; 2YDV; -.
PDBsum; 3EML; -.
PDBsum; 3PWH; -.
PDBsum; 3QAK; -.
PDBsum; 3REY; -.
PDBsum; 3RFM; -.
PDBsum; 3UZA; -.
PDBsum; 3UZC; -.
PDBsum; 3VG9; -.
PDBsum; 3VGA; -.
PDBsum; 4EIY; -.
PDBsum; 4UG2; -.
PDBsum; 4UHR; -.
PDBsum; 5G53; -.
PDBsum; 5IU4; -.
PDBsum; 5IU7; -.
PDBsum; 5IU8; -.
PDBsum; 5IUA; -.
PDBsum; 5IUB; -.
PDBsum; 5JTB; -.
PDBsum; 5K2A; -.
PDBsum; 5K2B; -.
PDBsum; 5K2C; -.
PDBsum; 5K2D; -.
PDBsum; 5MZJ; -.
PDBsum; 5MZP; -.
PDBsum; 5N2R; -.
PDBsum; 5NLX; -.
PDBsum; 5NM2; -.
PDBsum; 5NM4; -.
PDBsum; 5OLG; -.
PDBsum; 5OLH; -.
PDBsum; 5OLO; -.
PDBsum; 5OLV; -.
PDBsum; 5OLZ; -.
PDBsum; 5OM1; -.
PDBsum; 5OM4; -.
PDBsum; 5UIG; -.
PDBsum; 5UVI; -.
PDBsum; 5VRA; -.
PDBsum; 5WF5; -.
PDBsum; 5WF6; -.
PDBsum; 6AQF; -.
PDBsum; 6GDG; -.
ProteinModelPortal; P29274; -.
SMR; P29274; -.
BioGrid; 106647; 9.
IntAct; P29274; 9.
MINT; P29274; -.
STRING; 9606.ENSP00000336630; -.
BindingDB; P29274; -.
ChEMBL; CHEMBL251; -.
DrugBank; DB00640; Adenosine.
DrugBank; DB05009; Apadenoson.
DrugBank; DB05191; Atl146e.
DrugBank; DB04853; Binodenoson.
DrugBank; DB00201; Caffeine.
DrugBank; DB04932; Defibrotide.
DrugBank; DB00651; Dyphylline.
DrugBank; DB00824; Enprofylline.
DrugBank; DB00358; Mefloquine.
DrugBank; DB01303; Oxtriphylline.
DrugBank; DB00806; Pentoxifylline.
DrugBank; DB06213; Regadenoson.
DrugBank; DB01412; Theobromine.
DrugBank; DB00277; Theophylline.
GuidetoPHARMACOLOGY; 19; -.
TCDB; 9.A.14.3.8; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P29274; -.
PhosphoSitePlus; P29274; -.
DMDM; 543740; -.
PaxDb; P29274; -.
PeptideAtlas; P29274; -.
PRIDE; P29274; -.
ProteomicsDB; 54531; -.
DNASU; 135; -.
Ensembl; ENST00000337539; ENSP00000336630; ENSG00000128271.
Ensembl; ENST00000610595; ENSP00000480012; ENSG00000128271.
Ensembl; ENST00000611543; ENSP00000483102; ENSG00000128271.
Ensembl; ENST00000618076; ENSP00000481552; ENSG00000128271.
GeneID; 135; -.
KEGG; hsa:135; -.
CTD; 135; -.
DisGeNET; 135; -.
EuPathDB; HostDB:ENSG00000128271.20; -.
EuPathDB; HostDB:ENSG00000258555.5; -.
GeneCards; ADORA2A; -.
HGNC; HGNC:263; ADORA2A.
HPA; CAB001943; -.
HPA; HPA065566; -.
HPA; HPA075997; -.
MalaCards; ADORA2A; -.
MIM; 102776; gene.
neXtProt; NX_P29274; -.
OpenTargets; ENSG00000128271; -.
Orphanet; 363549; Acute encephalopathy with biphasic seizures and late reduced diffusion.
PharmGKB; PA24584; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00550000074524; -.
HOGENOM; HOG000015770; -.
HOVERGEN; HBG106962; -.
InParanoid; P29274; -.
KO; K04266; -.
OMA; MESQPLP; -.
OrthoDB; EOG091G0I3U; -.
TreeFam; TF325296; -.
Reactome; R-HSA-187024; NGF-independant TRKA activation.
Reactome; R-HSA-417973; Adenosine P1 receptors.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-5683826; Surfactant metabolism.
EvolutionaryTrace; P29274; -.
GeneWiki; Adenosine_A2A_receptor; -.
GenomeRNAi; 135; -.
PRO; PR:P29274; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000128271; Expressed in 90 organ(s), highest expression level in cerebellum.
CleanEx; HS_ADORA2A; -.
ExpressionAtlas; P29274; baseline and differential.
Genevisible; P29274; HS.
GO; GO:0030673; C:axolemma; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0012505; C:endomembrane system; IEA:Ensembl.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0001609; F:G-protein coupled adenosine receptor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
GO; GO:0008015; P:blood circulation; TAS:ProtInc.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0006171; P:cAMP biosynthetic process; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
GO; GO:0042755; P:eating behavior; IEA:Ensembl.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0060080; P:inhibitory postsynaptic potential; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0046636; P:negative regulation of alpha-beta T cell activation; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0040013; P:negative regulation of locomotion; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
GO; GO:0006909; P:phagocytosis; TAS:ProtInc.
GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IEA:Ensembl.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl.
GO; GO:0014049; P:positive regulation of glutamate secretion; IEA:Ensembl.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl.
GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:0014061; P:regulation of norepinephrine secretion; IEA:Ensembl.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0007600; P:sensory perception; TAS:ProtInc.
GO; GO:0007271; P:synaptic transmission, cholinergic; IEA:Ensembl.
GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
CDD; cd15068; 7tmA_Adenosine_R_A2A; 1.
InterPro; IPR001513; Adeno_A2A_rcpt.
InterPro; IPR001634; Adenosn_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00553; ADENOSINA2AR.
PRINTS; PR00424; ADENOSINER.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 412 Adenosine receptor A2a.
/FTId=PRO_0000068999.
TOPO_DOM 1 7 Extracellular.
{ECO:0000269|PubMed:18832607}.
TRANSMEM 8 32 Helical; Name=1.
TOPO_DOM 33 42 Cytoplasmic.
{ECO:0000269|PubMed:18832607}.
TRANSMEM 43 66 Helical; Name=2.
TOPO_DOM 67 77 Extracellular.
{ECO:0000269|PubMed:18832607}.
TRANSMEM 78 100 Helical; Name=3.
TOPO_DOM 101 120 Cytoplasmic.
{ECO:0000269|PubMed:18832607}.
TRANSMEM 121 143 Helical; Name=4.
TOPO_DOM 144 173 Extracellular.
{ECO:0000269|PubMed:18832607}.
TRANSMEM 174 198 Helical; Name=5.
TOPO_DOM 199 234 Cytoplasmic.
{ECO:0000269|PubMed:18832607}.
TRANSMEM 235 258 Helical; Name=6.
TOPO_DOM 259 266 Extracellular.
{ECO:0000269|PubMed:18832607}.
TRANSMEM 267 290 Helical; Name=7.
TOPO_DOM 291 412 Cytoplasmic.
{ECO:0000269|PubMed:18832607}.
REGION 168 177 Agonist binding.
REGION 246 253 Agonist binding.
REGION 264 274 Agonist binding.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 71 159 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:18832607}.
DISULFID 74 146 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:18832607}.
DISULFID 77 166 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:18832607}.
DISULFID 259 262 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:18832607}.
VARIANT 50 50 A -> V (in dbSNP:rs4530).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_011835.
VARIANT 300 300 R -> H (in dbSNP:rs4990).
/FTId=VAR_011836.
VARIANT 392 392 G -> R.
/FTId=VAR_003451.
HELIX 2 33 {ECO:0000244|PDB:5NM4}.
HELIX 35 37 {ECO:0000244|PDB:5NM4}.
HELIX 40 57 {ECO:0000244|PDB:5NM4}.
HELIX 59 67 {ECO:0000244|PDB:5NM4}.
STRAND 71 73 {ECO:0000244|PDB:5NM4}.
HELIX 74 107 {ECO:0000244|PDB:5NM4}.
HELIX 109 115 {ECO:0000244|PDB:5NM4}.
HELIX 118 136 {ECO:0000244|PDB:5NM4}.
HELIX 138 141 {ECO:0000244|PDB:5NM4}.
STRAND 144 148 {ECO:0000244|PDB:5JTB}.
HELIX 151 157 {ECO:0000244|PDB:5NM4}.
STRAND 163 165 {ECO:0000244|PDB:5NM4}.
HELIX 168 171 {ECO:0000244|PDB:5NM4}.
HELIX 174 179 {ECO:0000244|PDB:5NM4}.
HELIX 182 185 {ECO:0000244|PDB:5NM4}.
HELIX 187 208 {ECO:0000244|PDB:5NM4}.
STRAND 213 216 {ECO:0000244|PDB:3VGA}.
HELIX 219 258 {ECO:0000244|PDB:5NM4}.
STRAND 260 262 {ECO:0000244|PDB:2YDV}.
HELIX 267 291 {ECO:0000244|PDB:5NM4}.
HELIX 293 303 {ECO:0000244|PDB:5NM4}.
TURN 304 307 {ECO:0000244|PDB:3QAK}.
TURN 308 310 {ECO:0000244|PDB:2YDV}.
HELIX 312 317 {ECO:0000244|PDB:2YDV}.
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


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