Q99P02 · Q99P02_RAT

  • Protein
    Beta-2 adrenergic receptor
  • Gene
    Adrb2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentearly endosome
Cellular ComponentGolgi apparatus
Cellular Componentplasma membrane
Molecular Functionbeta2-adrenergic receptor activity
Molecular Functionnorepinephrine binding
Biological Processadenylate cyclase-activating adrenergic receptor signaling pathway
Biological Processnegative regulation of smooth muscle contraction
Biological Processnorepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Beta-2 adrenergic receptor
  • Short names
    Beta-2 adrenoceptor
  • Alternative names
    • Beta-2 adrenoreceptor

Gene names

    • Name
      Adrb2

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q99P02

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Early endosome
Golgi apparatus
Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane17-43Helical
Transmembrane55-76Helical
Transmembrane97-116Helical
Transmembrane145-166Helical
Transmembrane222-242Helical

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Binds NHERF1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC (By similarity).
Interacts with USP20 and USP33 (By similarity).
Interacts with VHL; the interaction, which is increased on hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation. Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating VHL-E3 ligase-mediated ubiquitination. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. Interacts with CNIH4. Interacts with ARRDC3. Interacts with NEDD4 (By similarity).
Interacts with MARCHF2

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-273G-protein coupled receptors family 1 profile

Sequence similarities

Keywords

Family and domain databases

Protein family/group databases

Sequence

  • Sequence status
    Fragment
  • Length
    273
  • Mass (Da)
    31,169
  • Last updated
    2001-06-01 v1
  • Checksum
    3F0A9AA42E300B68
VITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGASHILMKMWNFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYVAITSPFKYQSLLTKNKARVVILMVWIVSGLTSFLPIQMHWYRATHKQAIDCYAKETCCDFFTNQAYAIASSIVSFYVPLVVMVFVYSRVFQVAKRQLQKIDKSEGRFHAQNLSQVEQDGRSGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIRANLIPKEVYILLNWLGYVNSAFNPLIY

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue273

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY011271
EMBL· GenBank· DDBJ
AAG35431.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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