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Protein

Beta-2 adrenergic receptor

Gene

ADRB2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei113 – 1131Agonist or antagonistBy similarity
Binding sitei118 – 1181Agonist or antagonistBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-BTA-390696. Adrenoceptors.
R-BTA-418555. G alpha (s) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-2 adrenergic receptor
Alternative name(s):
Beta-2 adrenoreceptor
Short name:
Beta-2 adrenoceptor
Gene namesi
Name:ADRB2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Early endosome By similarity

  • Note: Colocalizes with VHL on cell membranes. Activated receptors are internalized into endosomes prior to their degradation in lysosomes.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434ExtracellularBy similarityAdd
BLAST
Transmembranei35 – 5824Helical; Name=1By similarityAdd
BLAST
Topological domaini59 – 7113CytoplasmicBy similarityAdd
BLAST
Transmembranei72 – 9524Helical; Name=2By similarityAdd
BLAST
Topological domaini96 – 10611ExtracellularBy similarityAdd
BLAST
Transmembranei107 – 12923Helical; Name=3By similarityAdd
BLAST
Topological domaini130 – 15021CytoplasmicBy similarityAdd
BLAST
Transmembranei151 – 17424Helical; Name=4By similarityAdd
BLAST
Topological domaini175 – 19622ExtracellularBy similarityAdd
BLAST
Transmembranei197 – 22024Helical; Name=5By similarityAdd
BLAST
Topological domaini221 – 27454CytoplasmicBy similarityAdd
BLAST
Transmembranei275 – 29824Helical; Name=6By similarityAdd
BLAST
Topological domaini299 – 3057ExtracellularBy similarity
Transmembranei306 – 32924Helical; Name=7By similarityAdd
BLAST
Topological domaini330 – 41889CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3373.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Beta-2 adrenergic receptorPRO_0000069127Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi6 – 61N-linked (GlcNAc...)Sequence analysis
Glycosylationi15 – 151N-linked (GlcNAc...)Sequence analysis
Glycosylationi23 – 231N-linked (GlcNAc...)Sequence analysis
Disulfide bondi106 ↔ 191PROSITE-ProRule annotation
Modified residuei141 – 1411PhosphotyrosineBy similarity
Disulfide bondi184 ↔ 190PROSITE-ProRule annotation
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei261 – 2611Phosphothreonine; by PKASequence analysis
Modified residuei262 – 2621Phosphoserine; by PKASequence analysis
Lipidationi341 – 3411S-palmitoyl cysteineBy similarity
Modified residuei345 – 3451Phosphoserine; by PKABy similarity
Modified residuei346 – 3461Phosphoserine; by PKABy similarity
Modified residuei355 – 3551Phosphoserine; by BARKCurated
Modified residuei356 – 3561Phosphoserine; by BARKCurated
Modified residuei387 – 38714-hydroxyprolineBy similarity
Modified residuei400 – 40014-hydroxyprolineBy similarity

Post-translational modificationi

Palmitoylated (By similarity); 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).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).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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ28044.

Expressioni

Tissue specificityi

Expressed in oviduct epithelial cells with high levels during the luteal phase of the sexual cycle. Lower levels around ovulation. Also expressed in liver.1 Publication

Inductioni

50% increase with progesterone treatment in cultured oviduct epithelial cells.1 Publication

Interactioni

Subunit structurei

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. 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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002779.

Chemistry

BindingDBiQ28044.

Structurei

3D structure databases

ProteinModelPortaliQ28044.
SMRiQ28044. Positions 29-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 20715Agonist and antagonist bindingBy similarityAdd
BLAST
Regioni286 – 2938Agonist and antagonist bindingBy similarity
Regioni312 – 3165Agonist and antagonist bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi415 – 4184PDZ-binding

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118774.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiQ28044.
KOiK04142.
OMAiGRFHAQN.
OrthoDBiEOG7BS4BS.
TreeFamiTF316350.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR000332. ADRB2_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24248:SF21. PTHR24248:SF21. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q28044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQPGNRSVF LLAPNASHAP DQNVTLERDE AWVVGMGILM SLIVLAIVFG
60 70 80 90 100
NVLVITAIAK FERLQTVTNY FITSLACADL VMGLAVVPFG ACHILMKMWT
110 120 130 140 150
FGNFWCEFWT SIDVLCVTAS IETLCVIAVD RYLAITSPFK YQCLLTKNKA
160 170 180 190 200
RVVILMVWIV SGLTSFLPIQ MHWYRASHKE AINCYAKETC CDFFTNQPYA
210 220 230 240 250
IASSIVSFYL PLVVMVFVYS RVFQVAKRQL QKIDKSEGRF HAQNVSQVEQ
260 270 280 290 300
DGRSGLGQRR TSKFYLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIKD
310 320 330 340 350
NLIRKEIYIL LNWLGYINSA FNPLIYCRSP DFRIAFQELL CLRRSSLKAY
360 370 380 390 400
GNGCSSNSND RTDYTGEQSG YHLGEEKDSE LLCEDPPGTE NFVNQQGTVP
410
SDSIDSQGRN CSTNDSLL
Length:418
Mass (Da):47,136
Last modified:July 15, 1998 - v2
Checksum:iCAB2A18470A801B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti254 – 2541S → T in CAA47653 (Ref. 3) Curated
Sequence conflicti272 – 2721L → P in CAA47653 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z86037 mRNA. Translation: CAB06661.1.
BC114132 mRNA. Translation: AAI14133.1.
X67213 mRNA. Translation: CAA47653.1.
PIRiS31617.
RefSeqiNP_776656.1. NM_174231.1.
UniGeneiBt.100.

Genome annotation databases

EnsembliENSBTAT00000002779; ENSBTAP00000002779; ENSBTAG00000002144.
GeneIDi281605.
KEGGibta:281605.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z86037 mRNA. Translation: CAB06661.1.
BC114132 mRNA. Translation: AAI14133.1.
X67213 mRNA. Translation: CAA47653.1.
PIRiS31617.
RefSeqiNP_776656.1. NM_174231.1.
UniGeneiBt.100.

3D structure databases

ProteinModelPortaliQ28044.
SMRiQ28044. Positions 29-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002779.

Chemistry

BindingDBiQ28044.
ChEMBLiCHEMBL3373.

Protein family/group databases

GPCRDBiSearch...

Proteomic databases

PaxDbiQ28044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000002779; ENSBTAP00000002779; ENSBTAG00000002144.
GeneIDi281605.
KEGGibta:281605.

Organism-specific databases

CTDi154.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118774.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiQ28044.
KOiK04142.
OMAiGRFHAQN.
OrthoDBiEOG7BS4BS.
TreeFamiTF316350.

Enzyme and pathway databases

ReactomeiR-BTA-390696. Adrenoceptors.
R-BTA-418555. G alpha (s) signalling events.

Miscellaneous databases

NextBioi20805548.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR000332. ADRB2_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24248:SF21. PTHR24248:SF21. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and localization of beta2-adrenergic receptors in the bovine oviduct: indication for progesterone-mediated expression."
    Einspanier R., Gabler C., Kettler A., Kloas W.
    Endocrinology 140:2679-2684(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: Fleckvieh.
    Tissue: Oviduct.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.
  3. Stoffel B., Hagen-Mann K., Mann W., Meyer H.H.D.
    Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 253-377.

Entry informationi

Entry nameiADRB2_BOVIN
AccessioniPrimary (citable) accession number: Q28044
Secondary accession number(s): Q29RK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: May 11, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.