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P54833 (ADRB2_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-2 adrenergic receptor
Alternative name(s):
Beta-2 adrenoreceptor
Short name=Beta-2 adrenoceptor
Gene names
Name:ADRB2
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC, USP20 and USP33. 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 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Note: Colocalizes with VHL on cell membranes By similarity.

Post-translational modification

Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation By similarity.

Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.

Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor By similarity.

Polyubiquitinated. Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation. Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and resensitization after prolonged agonist stimulation. USP20 and USP33 are constitutively associated and are dissociated immediately after agonist stimulation. Ubiquitination by the VHL-E3 ligase complex is oxygen-dependent By similarity.

Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2 By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Beta-2 adrenergic receptor
PRO_0000069128

Regions

Topological domain1 – 3434Extracellular By similarity
Transmembrane35 – 5824Helical; Name=1; By similarity
Topological domain59 – 7113Cytoplasmic By similarity
Transmembrane72 – 9524Helical; Name=2; By similarity
Topological domain96 – 10611Extracellular By similarity
Transmembrane107 – 12923Helical; Name=3; By similarity
Topological domain130 – 15021Cytoplasmic By similarity
Transmembrane151 – 17424Helical; Name=4; By similarity
Topological domain175 – 19622Extracellular By similarity
Transmembrane197 – 22024Helical; Name=5; By similarity
Topological domain221 – 27454Cytoplasmic By similarity
Transmembrane275 – 29824Helical; Name=6; By similarity
Topological domain299 – 3057Extracellular By similarity
Transmembrane306 – 32924Helical; Name=7; By similarity
Topological domain330 – 41586Cytoplasmic By similarity
Region193 – 20715Agonist and antagonist binding By similarity
Region286 – 2938Agonist and antagonist binding By similarity
Region312 – 3165Agonist and antagonist binding By similarity

Sites

Binding site1131Agonist or antagonist By similarity
Binding site1181Agonist or antagonist By similarity

Amino acid modifications

Modified residue1411Phosphotyrosine By similarity
Modified residue2461Phosphoserine By similarity
Modified residue2611Phosphoserine; by PKA Potential
Modified residue2621Phosphoserine; by PKA Potential
Modified residue3451Phosphoserine; by PKA By similarity
Modified residue3461Phosphoserine; by PKA By similarity
Modified residue3551Phosphoserine; by BARK Probable
Modified residue38714-hydroxyproline By similarity
Modified residue39714-hydroxyproline By similarity
Lipidation3411S-palmitoyl cysteine By similarity
Glycosylation61N-linked (GlcNAc...) Potential
Glycosylation151N-linked (GlcNAc...) Potential
Disulfide bond106 ↔ 191 By similarity
Disulfide bond184 ↔ 190 By similarity

Sequences

Sequence LengthMass (Da)Tools
P54833 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 392588623833445E

FASTA41546,589
        10         20         30         40         50         60 
MGQPANRSVF LLAPNGSHAP DQGDSQERSE AWVVGMGIVM SLIVLAIVFG NVLVITAIAR 

        70         80         90        100        110        120 
FERLQTVTNY FITSLACADL VMGLAVVPFG ASHILMKMWT FGNFWCEFWT SIDVLCVTAS 

       130        140        150        160        170        180 
IETLCVIAVD RYFAITSPFK YQSLLTKNKA RVVILMVWIV SGLTSFLPIQ MHWYRATHQE 

       190        200        210        220        230        240 
AINCYAKETC CDFFTNQAYA IASSIVSFYL PLVVMVFVYS RVFQVAQRQL QKIDRSEGRF 

       250        260        270        280        290        300 
HAQNLSQVEQ DGRSGHGHRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD 

       310        320        330        340        350        360 
NLIPKEVYIL LNWVGYVNSA FNPLIYCRSP DFRIAFQELL CLRRSSLKAY GNGYSNNSNS 

       370        380        390        400        410 
RSDYAGEHSG CHLGQEKDSE LLCEDPPGTE DRQGTVPSDS VDSQGRNCST NDSLL

« Hide

References

[1]"Rapid communication: cloning and sequencing of a canine beta 2-adrenergic receptor cDNA."
Emala C.W., Kuhl J., Hirshman C.A., Levine M.A.
J. Anim. Sci. 74:2285-2286(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart muscle.
[2]"Molecular cloning of the dog beta 1 and beta 2 adrenergic receptors."
Huang R.-R.C., Rapoport D., Schaeffer M.-T., Cascieri M.A., Fong T.M.
J. Recept. Signal Transduct. 17:599-607(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X94608 mRNA. Translation: CAA64316.1.
U73206 Genomic DNA. Translation: AAB93647.1.
RefSeqNP_001003234.1. NM_001003234.1.
UniGeneCfa.3770.

3D structure databases

ProteinModelPortalP54833.
SMRP54833. Positions 30-348.
ModBaseSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000027094.

Protein family/group databases

GPCRDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403910.
KEGGcfa:403910.

Organism-specific databases

CTD154.

Phylogenomic databases

eggNOGNOG262978.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP54833.
KOK04142.
OrthoDBEOG4WQ12W.

Family and domain databases

InterProIPR000332. Adrgc_rcpt_B2.
IPR002233. Adrnrgc_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP54833.
ChEMBLCHEMBL2289.
NextBio20817402.

Entry information

Entry nameADRB2_CANFA
AccessionPrimary (citable) accession number: P54833
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families

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