ID G5CVL3_CEBAL Unreviewed; 400 AA.
AC G5CVL3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Alpha-2B adrenergic receptor {ECO:0000256|ARBA:ARBA00019305, ECO:0000256|RuleBase:RU368059};
DE AltName: Full=Alpha-2B adrenoreceptor {ECO:0000256|ARBA:ARBA00031735, ECO:0000256|RuleBase:RU368059};
DE Flags: Fragment;
GN Name=adra2b {ECO:0000313|EMBL:AEP17853.1};
OS Cebus albifrons (White-fronted capuchin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Cebus.
OX NCBI_TaxID=9514 {ECO:0000313|EMBL:AEP17853.1};
RN [1] {ECO:0000313|EMBL:AEP17853.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21940861; DOI=10.1126/science.1211028;
RA Meredith R.W., Janecka J.E., Gatesy J., Ryder O.A., Fisher C.A.,
RA Teeling E.C., Goodbla A., Eizirik E., Simao T.L., Stadler T., Rabosky D.L.,
RA Honeycutt R.L., Flynn J.J., Ingram C.M., Steiner C., Williams T.L.,
RA Robinson T.J., Burk-Herrick A., Westerman M., Ayoub N.A., Springer M.S.,
RA Murphy W.J.;
RT "Impacts of the Cretaceous Terrestrial Revolution and KPg extinction on
RT mammal diversification.";
RL Science 334:521-524(2011).
CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC induced inhibition of adenylate cyclase through the action of G
CC proteins. {ECO:0000256|RuleBase:RU368059}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU368059}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368059}.
CC Membrane {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. ADRA2B sub-subfamily.
CC {ECO:0000256|RuleBase:RU368059}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU368059}.
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DR EMBL; JN413817; AEP17853.1; -; Genomic_DNA.
DR AlphaFoldDB; G5CVL3; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR CDD; cd15321; 7tmA_alpha2B_AR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000207; ADRA2B_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:SF130; ALPHA-2B ADRENERGIC RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00559; ADRENRGCA2BR.
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:RU368059};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368059};
KW Receptor {ECO:0000256|RuleBase:RU000688, ECO:0000313|EMBL:AEP17853.1};
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:RU368059}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368059"
FT TRANSMEM 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368059"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368059"
FT TRANSMEM 109..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368059"
FT TRANSMEM 150..175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368059"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368059"
FT DOMAIN 9..400
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 184..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEP17853.1"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:AEP17853.1"
SQ SEQUENCE 400 AA; 44345 MW; FAF3F2F2187F42F6 CRC64;
FLILFTIFGN ALVILAVLTS RSLRAPQNLF LVSLAAADIL VATLIIPFSL ANELLGYWYF
RRTWCEVYLA LDVLFCTSSI VHLCAISLDR YWAVSRALEY NSKRTPRRIK CIILTVWLIA
AIISLPPLIY KGDQGPQPRG RPQCKLNQEA WYILASSIGS FFAPCLIMIL VYLRIYLIAK
RSNRRGPRAK QGPGQGESKQ PRRDRGGALA SAKLPALASL AEAREAKVQS KSTGEQEEGE
TPEDTGNQAL PPSWAALPKS GQGQKEGVCG PSPEDEAEEE EEEEEEEEEE ECGPQAVSAS
PASACSPPLQ QPQGSQVLAT LRGQVLLGRG VGGMGGQWWR RRAQLTREKR FTFVLAVVIG
VFVLCWFPFF FSYSLGAICP KHCKVPHGLF QFFFWIGYCN
//
