ID A0A455AZE5_PHYMC Unreviewed; 441 AA.
AC A0A455AZE5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
GN Name=ADRB2 {ECO:0000313|RefSeq:XP_028341902.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028341902.1};
RN [1] {ECO:0000313|RefSeq:XP_028341902.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028341902.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_028341902.1; XM_028486101.2.
DR AlphaFoldDB; A0A455AZE5; -.
DR Proteomes; UP000248484; Unplaced.
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; IPR002233; ADR_fam.
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; PR01103; ADRENERGICR.
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 Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
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,
KW ECO:0000313|RefSeq:XP_028341902.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
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 31..58
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368057"
FT TRANSMEM 70..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368057"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368057"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368057"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368057"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368057"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368057"
FT DOMAIN 50..326
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 49450 MW; 0ADD2CCC1994ADA9 CRC64;
MGQPGNRSVF LLAPNGSHAP DQDVTQERDE AWVVGMGIVM SLIVLAIVFG NVLVITAIAK
FERLQTVTNY FITSLACADL VMGLAVVPFG ATHILMKMWT FGNFWCEFWT SIDVLCVTAS
IETLCVIAVD RYLAITSPFK YQCLLTKNKA RVVVLMVWVV SGLTSFLPIQ MHWYRATHQE
AINCYAKETC CDFFTNQAYA IASSIVSFYL PLVVMVFVYS KVFQVAKRQL QKIDKSEGRF
HAHNISQVEQ DGRSGPGQRR ASKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD
NLIPKEVYIL LNWVGYVNSA FNPLIYCRSP DFRIAFQELL CRRKSSLKAS GNGYSSNSNG
RTDYPGEQSG YHLGEEKDSE MLCEDPPGTE DFVNRQGAHS PVLFHLPTPF HRPALPTGAQ
QTCSTVCLPC PVPQQPFKDL Q
//
