ID   Q9BYZ0_HUMAN            Unreviewed;       275 AA.
AC   Q9BYZ0;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Beta-2 adrenergic receptor {ECO:0000256|ARBA:ARBA00022188, ECO:0000256|RuleBase:RU368057};
DE            Short=Beta-2 adrenoceptor {ECO:0000256|RuleBase:RU368057};
DE   AltName: Full=Beta-2 adrenoreceptor {ECO:0000256|ARBA:ARBA00030379, ECO:0000256|RuleBase:RU368057};
DE   Flags: Fragment;
GN   Name=ADRB2 {ECO:0000313|EMBL:AAG35451.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAG35451.1};
RN   [1] {ECO:0000313|EMBL:AAG35451.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11214319; DOI=10.1038/35054550;
RA   Murphy W.J., Eizirik E., Johnson W.E., Zhang Y.P., Ryder O.A.,
RA   O'Brien S.J.;
RT   "Molecular phylogenetics and the origins of placental mammals.";
RL   Nature 409:614-618(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.
CC       {ECO:0000256|RuleBase:RU368057}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368057};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU368057}. Early
CC       endosome {ECO:0000256|RuleBase:RU368057}. Golgi apparatus
CC       {ECO:0000256|RuleBase:RU368057}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRB2 sub-subfamily.
CC       {ECO:0000256|RuleBase:RU368057}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU368057}.
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DR   EMBL; AY011291; AAG35451.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9BYZ0; -.
DR   PeptideAtlas; Q9BYZ0; -.
DR   ChiTaRS; ADRB2; human.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004941; F:beta2-adrenergic receptor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; IEA:InterPro.
DR   GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
DR   CDD; cd15957; 7tmA_Beta2_AR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000332; ADRB2_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF21; BETA-2 ADRENERGIC RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00562; ADRENRGCB2AR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU368057};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Endosome {ECO:0000256|RuleBase:RU368057};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU000688};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU368057};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368057};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Receptor {ECO:0000256|RuleBase:RU000688, ECO:0000313|EMBL:AAG35451.1};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368057};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   TRANSMEM        19..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368057"
FT   TRANSMEM        57..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368057"
FT   TRANSMEM        99..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368057"
FT   TRANSMEM        147..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368057"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368057"
FT   DOMAIN          1..275
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAG35451.1"
FT   NON_TER         275
FT                   /evidence="ECO:0000313|EMBL:AAG35451.1"
SQ   SEQUENCE   275 AA;  31547 MW;  5CBB37404B7ACBE7 CRC64;
     VLVITAIAKF ERLQTVTNYF ITSLACADLV MGLAVVPFGA AHILMKMWTF GNFWCEFWTS
     IDVLCVTASI ETLCVIAVDR YFAITSPFKY QSLLTKNKAR VIILMVWIVS GLTSFLPIQM
     HWYRATHQEA INCYANETCC DFFTNQAYAI ASSIVSFYVP LVIMVFVYSR VFQEAKRQLQ
     KIDKSEGRFH VQNLSQVEQD GRTGHGLRRS SKFCLKEHKA LKTLGIIMGT FTLCWLPFFI
     VNIVHVIQDN LIRKEVYILL NWIGYVNSGF NPLIY
//