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Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (Beta-2 adrenoceptor)

 ADRB2_CANLF             Reviewed;         415 AA.
P54833;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 127.
RecName: Full=Beta-2 adrenergic receptor;
AltName: Full=Beta-2 adrenoreceptor;
Short=Beta-2 adrenoceptor;
Name=ADRB2;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart muscle;
PubMed=8880434; DOI=10.2527/1996.7492285x;
Emala C.W., Kuhl J., Hirshman C.A., Levine M.A.;
"Rapid communication: cloning and sequencing of a canine beta 2-
adrenergic receptor cDNA.";
J. Anim. Sci. 74:2285-2286(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9220370; DOI=10.3109/10799899709039152;
Huang R.-R.C., Rapoport D., Schaeffer M.-T., Cascieri M.A., Fong T.M.;
"Molecular cloning of the dog beta 1 and beta 2 adrenergic
receptors.";
J. Recept. Signal Transduct. 17:599-607(1997).
-!- 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. {ECO:0000269|PubMed:9220370}.
-!- SUBUNIT: 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. {ECO:0000250|UniProtKB:P07550}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9220370};
Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}. Early
endosome {ECO:0000250|UniProtKB:P07550}. Note=Colocalizes with VHL
on cell membranes. Activated receptors are internalized into
endosomes prior to their degradation in lysosomes.
{ECO:0000250|UniProtKB:P07550}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: Phosphorylated by PKA and BARK upon agonist stimulation,
which mediates homologous desensitization of the receptor. PKA-
mediated phosphorylation seems to facilitate phosphorylation by
BARK.
-!- PTM: Phosphorylation of Tyr-141 is induced by insulin and leads to
supersensitization of the receptor. {ECO:0000250}.
-!- PTM: 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).
{ECO:0000250}.
-!- PTM: Hydroxylation by EGLN3 occurs only under normoxia and
increases the interaction with VHL and the subsequent
ubiquitination and degradation of ADRB2. {ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Adrenergic receptor subfamily. ADRB2 sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; X94608; CAA64316.1; -; mRNA.
EMBL; U73206; AAB93647.1; -; Genomic_DNA.
RefSeq; NP_001003234.1; NM_001003234.1.
UniGene; Cfa.3770; -.
ProteinModelPortal; P54833; -.
SMR; P54833; -.
STRING; 9615.ENSCAFP00000027094; -.
BindingDB; P54833; -.
ChEMBL; CHEMBL2289; -.
PaxDb; P54833; -.
GeneID; 403910; -.
KEGG; cfa:403910; -.
CTD; 154; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
HOGENOM; HOG000239242; -.
HOVERGEN; HBG106962; -.
InParanoid; P54833; -.
KO; K04142; -.
PRO; PR:P54833; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043235; C:receptor complex; ISS:HGNC.
GO; GO:0004941; F:beta2-adrenergic receptor activity; ISS:HGNC.
GO; GO:0051379; F:epinephrine binding; IBA:GO_Central.
GO; GO:0051380; F:norepinephrine binding; ISS:HGNC.
GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:HGNC.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0002032; P:desensitization of G-protein coupled receptor protein signaling pathway by arrestin; ISS:HGNC.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IBA:GO_Central.
GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IBA:GO_Central.
GO; GO:1901098; P:positive regulation of autophagosome maturation; ISS:GO_Central.
GO; GO:1904504; P:positive regulation of lipophagy; ISS:GO_Central.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:HGNC.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:HGNC.
CDD; cd15957; 7tmA_Beta2_AR; 1.
InterPro; IPR002233; ADR_fam.
InterPro; IPR000332; ADRB2_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24248:SF21; PTHR24248:SF21; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01103; ADRENERGICR.
PRINTS; PR00562; ADRENRGCB2AR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Hydroxylation; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 415 Beta-2 adrenergic receptor.
/FTId=PRO_0000069128.
TOPO_DOM 1 34 Extracellular. {ECO:0000250}.
TRANSMEM 35 58 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 59 71 Cytoplasmic. {ECO:0000250}.
TRANSMEM 72 95 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 96 106 Extracellular. {ECO:0000250}.
TRANSMEM 107 129 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 130 150 Cytoplasmic. {ECO:0000250}.
TRANSMEM 151 174 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 175 196 Extracellular. {ECO:0000250}.
TRANSMEM 197 220 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 221 274 Cytoplasmic. {ECO:0000250}.
TRANSMEM 275 298 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 299 305 Extracellular. {ECO:0000250}.
TRANSMEM 306 329 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 330 415 Cytoplasmic. {ECO:0000250}.
REGION 193 207 Agonist and antagonist binding.
{ECO:0000250}.
REGION 286 293 Agonist and antagonist binding.
{ECO:0000250}.
REGION 312 316 Agonist and antagonist binding.
{ECO:0000250}.
MOTIF 412 415 PDZ-binding.
BINDING 113 113 Agonist or antagonist. {ECO:0000250}.
BINDING 118 118 Agonist or antagonist. {ECO:0000250}.
MOD_RES 141 141 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07550}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000250|UniProtKB:P07550}.
MOD_RES 261 261 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 262 262 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 345 345 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P07550}.
MOD_RES 346 346 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P07550}.
MOD_RES 355 355 Phosphoserine; by BARK. {ECO:0000305}.
MOD_RES 387 387 4-hydroxyproline. {ECO:0000250}.
MOD_RES 397 397 4-hydroxyproline. {ECO:0000250}.
LIPID 341 341 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 15 15 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 106 191 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 184 190 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 415 AA; 46589 MW; 392588623833445E CRC64;
MGQPANRSVF LLAPNGSHAP DQGDSQERSE AWVVGMGIVM SLIVLAIVFG NVLVITAIAR
FERLQTVTNY FITSLACADL VMGLAVVPFG ASHILMKMWT FGNFWCEFWT SIDVLCVTAS
IETLCVIAVD RYFAITSPFK YQSLLTKNKA RVVILMVWIV SGLTSFLPIQ MHWYRATHQE
AINCYAKETC CDFFTNQAYA IASSIVSFYL PLVVMVFVYS RVFQVAQRQL QKIDRSEGRF
HAQNLSQVEQ DGRSGHGHRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD
NLIPKEVYIL LNWVGYVNSA FNPLIYCRSP DFRIAFQELL CLRRSSLKAY GNGYSNNSNS
RSDYAGEHSG CHLGQEKDSE LLCEDPPGTE DRQGTVPSDS VDSQGRNCST NDSLL


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