Adenosine receptor A2a - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
Adenosine receptor A2a

Gene names

Name:	ADORA2A
Synonyms:	ADORA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

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Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	apoptosis Traceable author statement. Source: ProtInc blood coagulation Traceable author statement. Source: ProtInc cAMP biosynthetic process Traceable author statement. Source: ProtInc cellular defense response Traceable author statement. Source: ProtInc inflammatory response Traceable author statement. Source: ProtInc phagocytosis Traceable author statement. Source: ProtInc sensory perception Traceable author statement. Source: ProtInc transmembrane receptor protein tyrosine kinase signaling pathway Inferred from Experiment. Source: Reactome
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc membrane fraction Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 412

412

Adenosine receptor A2a

PRO_0000068999

Regions

Topological domain

1 – 7

7

Extracellular Ref.12

Transmembrane

8 – 32

25

1

Topological domain

33 – 42

10

Cytoplasmic Ref.12

Transmembrane

43 – 66

24

2

Topological domain

67 – 77

11

Extracellular Ref.12

Transmembrane

78 – 100

23

3

Topological domain

101 – 120

20

Cytoplasmic Ref.12

Transmembrane

121 – 143

23

4

Topological domain

144 – 173

30

Extracellular Ref.12

Transmembrane

174 – 198

25

5

Topological domain

199 – 234

36

Cytoplasmic Ref.12

Transmembrane

235 – 258

24

6

Topological domain

259 – 266

8

Extracellular Ref.12

Transmembrane

267 – 290

24

7

Topological domain

291 – 412

122

Cytoplasmic Ref.12

Region

168 – 177

10

Agonist binding

Region

246 – 253

8

Agonist binding

Region

264 – 274

11

Agonist binding

Amino acid modifications

Glycosylation

154

1

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

50

1

A → V: dbSNP rs4530. Ref.13

VAR_011835

Natural variant

300

1

R → H: dbSNP rs4990.

VAR_011836

Natural variant

392

1

G → R

VAR_003451

Secondary structure

1

.

412

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P29274-1 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 9438E9D64A6BE61B
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FASTA

412

44,707

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Tiffany H.L., Murphy P.M. Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Salvatore C.A., Luneau C.J., Johnson R.G., Jacobson M. Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Molecular characterization of a human brain adenosine A2 receptor." Furlong T.J., Pierce K.D., Selbie L.A., Shine J. Brain Res. Mol. Brain Res. 15:62-66(1992) [PubMed: 1331670] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Hippocampus.
[4]	"Characterization and chromosomal localization of the human A2a adenosine receptor gene: ADORA2A." Le F., Townsend-Nicholson A., Baker E., Sutherland G.R., Schofield P.R. Biochem. Biophys. Res. Commun. 223:461-467(1996) [PubMed: 8670304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"A genome annotation-driven approach to cloning the human ORFeome." 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. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[9]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[11]	"Site-directed mutagenesis identifies residues involved in ligand recognition in the human A2a adenosine receptor." Kim J., Wess J., van Rhee A.M., Schoneberg T., Jacobson K.A. J. Biol. Chem. 270:13987-13997(1995) [PubMed: 7775460] [Abstract] Cited for: 3D-STRUCTURE MODELING OF TRANSMEMBRANE DOMAINS.
[12]	"The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist." Jaakola V.-P., Griffith M.T., Hanson M.A., Cherezov V., Chien E.Y.T., Lane J.R., Ijzerman A.P., Stevens R.C. Science 322:1211-1217(2008) [PubMed: 18832607] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-316 IN COMPLEX WITH ANTAGONIST, TOPOLOGY, DISULFIDE BONDS.
[13]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." 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. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANT VAL-50.
[14]	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)
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M97370 mRNA. Translation: AAA58356.1. Different initiation.
X68486 mRNA. Translation: CAA48504.1.
S46950 mRNA. Translation: AAB23956.1.
U40771, U40770 Genomic DNA. Translation: AAA83270.1.
AY136747 mRNA. Translation: AAN01273.1.
CR456367 mRNA. Translation: CAG30253.1.
BT006999 mRNA. Translation: AAP35645.1.
AK312946 mRNA. Translation: BAG35787.1.
CH471095 Genomic DNA. Translation: EAW59658.1.
BC013780 mRNA. Translation: AAH13780.1.

IPI

IPI00020974.

PIR

A48978.

RefSeq

NP_000666.2.

UniGene

Hs.197029

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MMH	model	-	1	6-36	[»]
			2	42-69	[»]
			3	78-102	[»]
			4	117-143	[»]
			5	175-203	[»]
			6	233-260	[»]
			7	264-296	[»]
1UPE	model	-	A	1-304	[»]
3EML	X-ray	2.60	A	2-316	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P29274.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P29274.

Proteomic databases

PRIDE

P29274.

Genome annotation databases

Ensembl

ENST00000337539; ENSP00000336630; ENSG00000128271; Homo sapiens. [Genome view]
ENST00000417596; ENSP00000394368; ENSG00000128271; Homo sapiens. [Genome view]

GeneID

135.

KEGG

hsa:135.

UCSC

uc002zzx.1. human.

Organism-specific databases

CTD

135.

GeneCards

GC22P022997.

HGNC

HGNC:263. ADORA2A.

MIM

102776. gene.

PharmGKB

PA24584.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10218.

HOGENOM

HBG445348.

HOVERGEN

HBG106962.

InParanoid

P29274.

OMA

CSHAPLW.

PhylomeDB

P29274.

Enzyme and pathway databases

Reactome

REACT_11061. Signalling by NGF.
REACT_14797. Signaling by GPCR.

Gene expression databases

Bgee

P29274.

CleanEx

HS_ADORA2A.

Genevestigator

P29274.

GermOnline

ENSG00000128271. Homo sapiens.

Family and domain databases

InterPro

IPR000276. 7TM_GPCR_Rhodpsn.
IPR001513. Adeno_A2A_rcpt.
IPR001634. Adenosn_rcpt.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00553. ADENOSINA2AR.
PR00424. ADENOSINER.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00201. Caffeine.
DB04932. Defibrotide.
DB00061. Pegademase bovine.
DB00277. Theophylline.

NextBio

543.

SOURCE

Search...

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Entry information

Entry name

AA2AR_HUMAN

Accession

Primary (citable) accession number: P29274
Secondary accession number(s): B2R7E0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	June 1, 1994
Last modified:	March 2, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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