ADRB2_ONCMY
ID ADRB2_ONCMY Reviewed; 409 AA.
AC Q8UUY8;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Beta-2 adrenergic receptor;
DE AltName: Full=Beta-2 adrenoreceptor;
DE Short=Beta-2 adrenoceptor;
GN Name=adrb2;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000312|EMBL:AAK94672.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11737201; DOI=10.1046/j.0014-2956.2001.02600.x;
RA Nickerson J.G., Dugan S.G., Drouin G., Moon T.W.;
RT "A putative beta2-adrenoceptor from the rainbow trout (Oncorhynuchus
RT mykiss). Molecular characterization and pharmacology.";
RL Eur. J. Biochem. 268:6465-6472(2001).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07550};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and red and white
CC muscle, with lower levels of expression in the gills, heart, kidney and
CC spleen. {ECO:0000269|PubMed:11737201}.
CC -!- PTM: Lacks the regulatory protein kinase A phosphorylation sites within
CC the G-protein binding domain that mediate desensitization and are
CC present in mammalian homologs. {ECO:0000269|PubMed:11737201}.
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; AY044093; AAK94672.1; -; mRNA.
DR RefSeq; NP_001117912.1; NM_001124440.1.
DR AlphaFoldDB; Q8UUY8; -.
DR SMR; Q8UUY8; -.
DR GeneID; 100136153; -.
DR KEGG; omy:100136153; -.
DR OrthoDB; 614199at2759; -.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004941; F:beta2-adrenergic receptor activity; NAS:UniProtKB.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; NAS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; IMP:AgBase.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:InterPro.
DR GO; GO:0032811; P:negative regulation of epinephrine secretion; IMP:AgBase.
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 GO; GO:0043434; P:response to peptide hormone; IMP:AgBase.
DR InterPro; IPR002233; ADR_fam.
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; PR01103; ADRENERGICR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..409
FT /note="Beta-2 adrenergic receptor"
FT /id="PRO_0000069137"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 62..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 99..109
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 154..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 178..199
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 200..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 224..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 283..306
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 307..318
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 319..337
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 338..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 349
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 187..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 409 AA; 45098 MW; AEFFA8BC71574BD2 CRC64;
MENVSTPAVF NLSDLSVEMN SSSRQWSYSE YSEAVAVLLG ILMALLVMCI VFGNVLVITA
IVRFQRLQTV TNMFITSLAC ADLVMGLLVV PFGACYILLN TWHFGSFLCE FWTAADVLCV
TASIETLCVI ALDRYLAITS PLRYPSLLTK RKACVVVVTV WGVAALISFL PIHMKWWVSD
EPEALSCLED AHCCDFNTNA AYAVASSVVS FYIPLAVMAF VYGRVFQEAR KQLEKIRGSE
GRFHAQMIDN NQGQDGGDGS GGGGGNGKRP KFCLKEHKAL KTLGIIMGTF TLCWLPFFVL
NVVVTIWKVD NIKMPFRILN WIGYANSAFN PLIYCRSPEF RYAFQEILCL RGAAFPTNGY
IYRGHSLRLS PKDKPGSLSN NVGTVELGSL SSVTNINGYC NNPPLASIV
