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Q60614 (AA2BR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosine receptor A2b
Gene names
Name:Adora2b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 16841096PubMed 18340377. Source: MGI

cellular response to extracellular stimulus

Inferred from direct assay Ref.1. Source: MGI

positive regulation of cAMP biosynthetic process

Inferred from mutant phenotype PubMed 16841096PubMed 18340377. Source: MGI

positive regulation of cGMP biosynthetic process

Inferred from mutant phenotype PubMed 18340377. Source: MGI

positive regulation of chemokine production

Inferred from mutant phenotype PubMed 18559975. Source: MGI

positive regulation of chronic inflammatory response to non-antigenic stimulus

Inferred from mutant phenotype PubMed 16841096. Source: MGI

positive regulation of guanylate cyclase activity

Inferred from mutant phenotype PubMed 18340377. Source: MGI

positive regulation of interleukin-6 production

Inferred from mutant phenotype PubMed 18559975. Source: MGI

positive regulation of mast cell degranulation

Inferred from mutant phenotype PubMed 11454903. Source: MGI

positive regulation vascular endothelial growth factor production

Inferred from mutant phenotype PubMed 18559975. Source: MGI

relaxation of vascular smooth muscle

Inferred from mutant phenotype PubMed 18340377. Source: MGI

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 12817016. Source: MGI

   Molecular_functionG-protein coupled adenosine receptor activity

Inferred from electronic annotation. Source: InterPro

G-protein coupled receptor activity

Inferred from mutant phenotype PubMed 16841096. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Adenosine receptor A2b
PRO_0000069004

Regions

Topological domain1 – 88Extracellular By similarity
Transmembrane9 – 3325Helical; Name=1; By similarity
Topological domain34 – 4310Cytoplasmic By similarity
Transmembrane44 – 6724Helical; Name=2; By similarity
Topological domain68 – 7811Extracellular By similarity
Transmembrane79 – 10123Helical; Name=3; By similarity
Topological domain102 – 12120Cytoplasmic By similarity
Transmembrane122 – 14423Helical; Name=4; By similarity
Topological domain145 – 17834Extracellular By similarity
Transmembrane179 – 20325Helical; Name=5; By similarity
Topological domain204 – 23532Cytoplasmic By similarity
Transmembrane236 – 25924Helical; Name=6; By similarity
Topological domain260 – 2678Extracellular By similarity
Transmembrane268 – 29124Helical; Name=7; By similarity
Topological domain292 – 33241Cytoplasmic By similarity
Region173 – 18210Agonist binding By similarity
Region247 – 2548Agonist binding By similarity
Region266 – 27611Agonist binding By similarity

Amino acid modifications

Lipidation3111S-palmitoyl cysteine Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Disulfide bond78 ↔ 171 By similarity

Experimental info

Sequence conflict1691V → L in AAA19001. Ref.1
Sequence conflict2151R → S in AAA19001. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60614 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BABE2C782001564A

FASTA33236,120
        10         20         30         40         50         60 
MQLETQDALY VALELVIAAL AVAGNVLVCA AVGASSALQT PTNYFLVSLA TADVAVGLFA 

        70         80         90        100        110        120 
IPFAITISLG FCTDFHGCLF LACFVLVLTQ SSIFSLLAVA VDRYLAIRVP LRYKGLVTGT 

       130        140        150        160        170        180 
RARGIIAVLW VLAFGIGLTP FLGWNSKDSA TSNCTELGDG IANKSCCPVT CLFENVVPMS 

       190        200        210        220        230        240 
YMVYFNFFGC VLPPLLIMLV IYIKIFMVAC KQLQRMELMD HSRTTLQREI HAAKSLAMIV 

       250        260        270        280        290        300 
GIFALCWLPV HAINCITLFH PALAKDKPKW VMNVAILLSH ANSVVNPIVY AYRNRDFRYS 

       310        320        330 
FHKIISRYVL CQAETKGGSG QAGAQSTLSL GL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of two adenosine receptor subtypes from mouse bone marrow-derived mast cells."
Marquardt D.L., Walker L.L., Heinemann S.
J. Immunol. 152:4508-4515(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Bone marrow.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05673 mRNA. Translation: AAA19001.1.
AK047002 mRNA. Translation: BAC32938.1.
AL596110 Genomic DNA. Translation: CAI35330.1.
BC116415 mRNA. Translation: AAI16416.1.
BC116416 mRNA. Translation: AAI16417.1.
CCDSCCDS24822.1.
PIRI48933.
RefSeqNP_031439.2. NM_007413.4.
UniGeneMm.40740.

3D structure databases

ProteinModelPortalQ60614.
SMRQ60614. Positions 8-314.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ60614.
ChEMBLCHEMBL2237.
GuidetoPHARMACOLOGY20.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ60614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018644; ENSMUSP00000018644; ENSMUSG00000018500.
GeneID11541.
KEGGmmu:11541.
UCSCuc007jio.1. mouse.

Organism-specific databases

CTD136.
MGIMGI:99403. Adora2b.

Phylogenomic databases

eggNOGNOG287824.
GeneTreeENSGT00550000074524.
HOGENOMHOG000015770.
HOVERGENHBG106962.
InParanoidQ8BXI2.
KOK04267.
OMAGWNSKDS.
OrthoDBEOG79SDXQ.
TreeFamTF325296.

Gene expression databases

BgeeQ60614.
CleanExMM_ADORA2B.
GenevestigatorQ60614.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR001435. Adeno_A2B_rcpt.
IPR001634. Adenosn_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00554. ADENOSINA2BR.
PR00424. ADENOSINER.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279004.
PROQ60614.
SOURCESearch...

Entry information

Entry nameAA2BR_MOUSE
AccessionPrimary (citable) accession number: Q60614
Secondary accession number(s): Q8BXI2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries