ADRB2_MERUN
ID ADRB2_MERUN Reviewed; 251 AA.
AC O70431;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Beta-2 adrenergic receptor;
DE AltName: Full=Beta-2 adrenoreceptor;
DE Short=Beta-2 adrenoceptor;
DE Flags: Fragment;
GN Name=ADRB2;
OS Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Meriones.
OX NCBI_TaxID=10047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adipose tissue, Brain, and Stria vascularis;
RX PubMed=10398761; DOI=10.1007/s002329900538;
RA Wangemann P., Liu J., Shimozono M., Scofield M.A.;
RT "Beta1-adrenergic receptors but not beta2-adrenergic or vasopressin
RT receptors regulate K+ secretion in vestibular dark cells of the inner
RT ear.";
RL J. Membr. Biol. 170:67-77(1999).
CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced
CC activation of adenylate cyclase through the action of G proteins. The
CC beta-2-adrenergic receptor binds epinephrine with an approximately 30-
CC fold greater affinity than it does norepinephrine (By similarity).
CC {ECO:0000250|UniProtKB:P07550}.
CC -!- SUBUNIT: Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and ARRB2.
CC Interacts with SRC (By similarity). Interacts with USP20 and USP33 (By
CC similarity). Interacts with VHL; the interaction, which is increased on
CC hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation.
CC Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating
CC VHL-E3 ligase-mediated ubiquitination. Interacts (via PDZ-binding
CC motif) with SNX27 (via PDZ domain); the interaction is required when
CC endocytosed to prevent degradation in lysosomes and promote recycling
CC to the plasma membrane. Interacts with CNIH4. Interacts with ARRDC3.
CC Interacts with NEDD4 (By similarity). Interacts with MARCHF2 (By
CC similarity). {ECO:0000250|UniProtKB:P07550}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07550};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}. Early
CC endosome {ECO:0000250|UniProtKB:P07550}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P07550}. Note=Colocalizes with VHL at the cell
CC membrane. Activated receptors are internalized into endosomes prior to
CC their degradation in lysosomes. Activated receptors are also detected
CC within the Golgi apparatus. {ECO:0000250|UniProtKB:P07550}.
CC -!- PTM: Phosphorylated by PKA and BARK upon agonist stimulation, which
CC mediates homologous desensitization of the receptor. PKA-mediated
CC phosphorylation seems to facilitate phosphorylation by BARK.
CC -!- PTM: Phosphorylation of Tyr-67 is induced by insulin and leads to
CC supersensitization of the receptor. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Agonist-induced ubiquitination leads to sort
CC internalized receptors to the lysosomes for degradation.
CC Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and
CC resensitization after prolonged agonist stimulation. USP20 and USP33
CC are constitutively associated and are dissociated immediately after
CC agonist stimulation (By similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P07550}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRB2 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF055350; AAC12768.1; -; mRNA.
DR AlphaFoldDB; O70431; -.
DR SMR; O70431; -.
DR PRIDE; O70431; -.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004941; F:beta2-adrenergic receptor activity; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:InterPro.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; ISS:GO_Central.
DR GO; GO:1904504; P:positive regulation of lipophagy; ISS:GO_Central.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
DR InterPro; IPR000332; ADRB2_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248:SF21; PTHR24248:SF21; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00562; ADRENRGCB2AR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Receptor; Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN <1..>251
FT /note="Beta-2 adrenergic receptor"
FT /id="PRO_0000069132"
FT TRANSMEM <1..21
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 22..32
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..55
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 56..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 77..100
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 101..122
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..146
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 147..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..224
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 225..231
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 232..>251
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07550"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07550"
FT MOD_RES 187
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 188
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 191
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P07550"
FT DISULFID 32..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 110..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 251
SQ SEQUENCE 251 AA; 28502 MW; 6B9A873BB804608B CRC64;
LACAGLVMGL AVVPFGASHI LMNMWNFGNF WCEFWTSIDV LCVTASIETL CVIAVDRYIA
ITAPFKYQSL LTKNKARVVI LMVWIVSGLT SFLPIQMHWY RATNKEAITC YTNETCCDFF
TNQAYAIASS IVSFYVPLVV MVFVYSRVFQ VAKRQLQKID KSEGRFHAQN LSQVEQDGRS
GHGLRRSSKF CLKEHKALKT LGIIMGTFTL CWLPFFIVNV VHAIKENLIP KEVYILLNWL
GYVNSAFNPL I
