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Q01338 (ADA2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-2A adrenergic receptor
Alternative name(s):
Alpha-2A adrenoreceptor
Short name=Alpha-2A adrenoceptor
Short name=Alpha-2AAR
Gene names
Name:Adra2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2A sub-subfamily.

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_processDNA replication

Inferred from electronic annotation. Source: Ensembl

activation of MAPK activity by adrenergic receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase B activity

Inferred from electronic annotation. Source: Ensembl

acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting adrenergic receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcium ion-dependent exocytosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipid catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of uterine smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating adrenergic receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

platelet activation

Inferred from electronic annotation. Source: InterPro

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of membrane protein ectodomain proteolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

positive regulation of wound healing

Inferred from electronic annotation. Source: Ensembl

regulation of vasoconstriction

Inferred from electronic annotation. Source: InterPro

thermoception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

receptor complex

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionalpha2-adrenergic receptor activity

Inferred from electronic annotation. Source: Ensembl

epinephrine binding

Inferred from electronic annotation. Source: Ensembl

norepinephrine binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 9235896. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF2B1Q142322EBI-491073,EBI-491065From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Alpha-2A adrenergic receptor
PRO_0000069081

Regions

Topological domain1 – 3333Extracellular By similarity
Transmembrane34 – 5926Helical; Name=1; By similarity
Topological domain60 – 7011Cytoplasmic By similarity
Transmembrane71 – 9626Helical; Name=2; By similarity
Topological domain97 – 10610Extracellular By similarity
Transmembrane107 – 12923Helical; Name=3; By similarity
Topological domain130 – 14920Cytoplasmic By similarity
Transmembrane150 – 17324Helical; Name=4; By similarity
Topological domain174 – 19219Extracellular By similarity
Transmembrane193 – 21725Helical; Name=5; By similarity
Topological domain218 – 374157Cytoplasmic By similarity
Transmembrane375 – 39925Helical; Name=6; By similarity
Topological domain400 – 40910Extracellular By similarity
Transmembrane410 – 43021Helical; Name=7; By similarity
Topological domain431 – 45020Cytoplasmic By similarity

Sites

Site1131Implicated in ligand binding By similarity
Site2001Implicated in catechol agonist binding By similarity
Site2041Implicated in catechol agonist binding By similarity

Amino acid modifications

Lipidation4421S-palmitoyl cysteine By similarity
Glycosylation101N-linked (GlcNAc...) Potential
Glycosylation141N-linked (GlcNAc...) Potential
Disulfide bond106 ↔ 188 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01338 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: F07E225393AFA93B

FASTA45048,865
        10         20         30         40         50         60 
MGSLQPDAGN SSWNGTEAPG GGTRATPYSL QVTLTLVCLA GLLMLFTVFG NVLVIIAVFT 

        70         80         90        100        110        120 
SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKVWCEIYL ALDVLFCTSS 

       130        140        150        160        170        180 
IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIVTVWVI SAVISFPPLI SIEKKGAGGG 

       190        200        210        220        230        240 
QQPAEPSCKI NDQKWYVISS SIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDACS 

       250        260        270        280        290        300 
APPGGADRRP NGLGPERGAG PTGAEAEPLP TQLNGAPGEP APAGPRDGDA LDLEESSSSE 

       310        320        330        340        350        360 
HAERPPGPRR PDRGPRAKGK TRASQVKPGD SLPRRGPGAA GPGASGSGHG EERGGGAKAS 

       370        380        390        400        410        420 
RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLIAVG CPVPSQLFNF FFWFGYCNSS 

       430        440        450 
LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV 

« Hide

References

[1]"Cloning of two mouse genes encoding alpha 2-adrenergic receptor subtypes and identification of a single amino acid in the mouse alpha 2-C10 homolog responsible for an interspecies variation in antagonist binding."
Link R.E., Daunt D.A., Barsh G., Chruscinski A.J., Kobilka B.K.
Mol. Pharmacol. 42:16-27(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M99377 Genomic DNA. Translation: AAA37213.1.
PIRI49481.
UniGeneMm.235195.
Mm.489007.

3D structure databases

ProteinModelPortalQ01338.
SMRQ01338. Positions 39-229, 368-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ01338. 1 interaction.

Chemistry

BindingDBQ01338.
ChEMBLCHEMBL2111338.
GuidetoPHARMACOLOGY25.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ01338.

Proteomic databases

PRIDEQ01338.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:87934. Adra2a.

Phylogenomic databases

eggNOGNOG249628.
HOVERGENHBG106962.
InParanoidQ01338.
PhylomeDBQ01338.

Gene expression databases

ArrayExpressQ01338.
BgeeQ01338.
CleanExMM_ADRA2A.
GenevestigatorQ01338.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR002233. ADR_fam.
IPR001946. ADRA2A_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24248:SF24. PTHR24248:SF24. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01103. ADRENERGICR.
PR00558. ADRENRGCA2AR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ01338.
SOURCESearch...

Entry information

Entry nameADA2A_MOUSE
AccessionPrimary (citable) accession number: Q01338
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 11, 2014
This is version 124 of the entry and version 1 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