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UniProtKB/Swiss-Prot entry P29274


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AA2AR_HUMAN
Primary accession number P29274
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Adenosine receptor A2a
Synonyms None
Gene name
Name: ADORA2A
Synonyms: ADORA2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[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;
DOI=10.1016/0169-328X(92)90152-2; PubMed=1331670 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1006/bbrc.1996.0916; PubMed=8670304 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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:RESEARCH84.1-RESEARCH84.11(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=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
3D-STRUCTURE MODELING OF TRANSMEMBRANE DOMAINS.
DOI=10.1074/jbc.270.23.13879; PubMed=7775460 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-316 IN COMPLEX WITH ANTAGONIST, TOPOLOGY, AND DISULFIDE BONDS.
DOI=10.1126/science.1164772; PubMed=18832607 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
VARIANT VAL-50.
DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M97370; AAA58356.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68486; CAA48504.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S46950; AAB23956.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U40771; AAA83270.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U40770; AAA83270.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136747; AAN01273.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456367; CAG30253.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006999; AAP35645.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013780; AAH13780.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00020974; -.
PIR A48978; A48978.
RefSeq NP_000666.2; -.
UniGene Hs.197029
3D structure databases
PDB
1MMH; Model; -; 1=6-36, 2=42-69, 3=78-102, 4=117-143, 5=175-203, 6=233-260, 7=264-296.[ExPASy / RCSB / EBI]
1UPE; Model; -; A=1-304.[ExPASy / RCSB / EBI]
3EML; X-ray; 2.60 A; A=2-316.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MMH; -.
1UPE; -.
3EML; -.
ModBase P29274.
Protein family/group databases
GPCRDB P29274; AA2AR_HUMAN.
PTM databases
PhosphoSite P29274; -.
Enzyme and pathway databases
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC22P022997; -.
HGNC HGNC:263; ADORA2A.
GenAtlas ADORA2A.
MIM 102776; gene. [NCBI / EBI]
PharmGKB PA24584; -.
Gene expression databases
ArrayExpress P29274; -.
Bgee P29274; -.
CleanEx HS_ADORA2A; -.
GermOnline ENSG00000128271; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0001609; Molecular function: adenosine receptor activity, G-protein coupled (inferred from electronic annotation from InterPro).
GO:0007190; Biological process: activation of adenylate cyclase activity (inferred from experiment from Reactome).
GO:0006915; Biological process: apoptosis (traceable author statement from ProtInc).
GO:0008015; Biological process: blood circulation (traceable author statement from ProtInc).
GO:0007596; Biological process: blood coagulation (traceable author statement from ProtInc).
GO:0006171; Biological process: cAMP biosynthetic process (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0006968; Biological process: cellular defense response (traceable author statement from ProtInc).
GO:0007417; Biological process: central nervous system development (traceable author statement from ProtInc).
GO:0007188; Biological process: G-protein signaling, coupled to cAMP nucleotide second messenger (traceable author statement from ProtInc).
GO:0006954; Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0006909; Biological process: phagocytosis (traceable author statement from ProtInc).
GO:0007600; Biological process: sensory perception (traceable author statement from ProtInc).
GO:0007169; Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR000276; 7TM_GPCR_Rhodpsn.
IPR001513; Adeno_A2A_rcpt.
IPR001634; Adenosn_rcpt.
IPR017452; GPCR_Rhodpsn_supfam.
Graphical view of domain structure.
Pfam PF00001; 7tm_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00553; ADENOSINA2AR.
PR00424; ADENOSINER.
PR00237; GPCRRHODOPSN.
PROSITE PS00237; G_PROTEIN_RECEP_F1_1; 1.
PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P29274; -.
Genome annotation databases
Ensembl ENSG00000128271; Homo sapiens. [Contig view]
GeneID 135; -.
KEGG hsa:135; -.
Phylogenomic databases
HOGENOM P29274; -.
HOVERGEN P29274; -.
OMA P29274; CSHAPLW.
Other
DrugBank DB00201; Caffeine.
DB04932; Defibrotide.
DB00061; Pegademase bovine.
DB00277; Theophylline.
NextBio 543; -.
SOURCE ADORA2A; Homo sapiens.
GPCRDB-Snakes P29274.
ProtoNet P29274.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; Receptor; Transducer; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   412  412     Adenosine receptor A2a. PRO_0000068999
TOPO_DOM   1     7  7     Extracellular. 
TRANSMEM   8    32  25     1. 
TOPO_DOM   33    42  10     Cytoplasmic. 
TRANSMEM   43    66  24     2. 
TOPO_DOM   67    77  11     Extracellular. 
TRANSMEM   78   100  23     3. 
TOPO_DOM   101   120  20     Cytoplasmic. 
TRANSMEM   121   143  23     4. 
TOPO_DOM   144   173  30     Extracellular. 
TRANSMEM   174   198  25     5. 
TOPO_DOM   199   234  36     Cytoplasmic. 
TRANSMEM   235   258  24     6. 
TOPO_DOM   259   266  8     Extracellular. 
TRANSMEM   267   290  24     7. 
TOPO_DOM   291   412  122     Cytoplasmic. 
REGION   168   177  10     Agonist binding. 
REGION   246   253  8     Agonist binding. 
REGION   264   274  11     Agonist binding. 
CARBOHYD   154   154        N-linked (GlcNAc...) (Potential). 
DISULFID   71   159         
DISULFID   74   146         
DISULFID   77   166         
DISULFID   259   262         
VARIANT   50    50  1     A -> V (in dbSNP:rs4530 [NCBI]). VAR_011835 
VARIANT   300   300  1     R -> H (in dbSNP:rs4990 [NCBI]). VAR_011836 
VARIANT   392   392  1     G -> R. VAR_003451 
Sequence information
Length: 412 AA [This is the length of the unprocessed precursor] Molecular weight: 44707 Da [This is the MW of the unprocessed precursor] CRC64: 9438E9D64A6BE61B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPIMGSSVYI TVELAIAVLA ILGNVLVCWA VWLNSNLQNV TNYFVVSLAA ADIAVGVLAI 

        70         80         90        100        110        120 
PFAITISTGF CAACHGCLFI ACFVLVLTQS SIFSLLAIAI DRYIAIRIPL RYNGLVTGTR 

       130        140        150        160        170        180 
AKGIIAICWV LSFAIGLTPM LGWNNCGQPK EGKNHSQGCG EGQVACLFED VVPMNYMVYF 

       190        200        210        220        230        240 
NFFACVLVPL LLMLGVYLRI FLAARRQLKQ MESQPLPGER ARSTLQKEVH AAKSLAIIVG 

       250        260        270        280        290        300 
LFALCWLPLH IINCFTFFCP DCSHAPLWLM YLAIVLSHTN SVVNPFIYAY RIREFRQTFR 

       310        320        330        340        350        360 
KIIRSHVLRQ QEPFKAAGTS ARVLAAHGSD GEQVSLRLNG HPPGVWANGS APHPERRPNG 

       370        380        390        400        410 
YALGLVSGGS AQESQGNTGL PDVELLSHEL KGVCPEPPGL DDPLAQDGAG VS 

P29274 in FASTA format

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