ADA2B_CAVPO
ID ADA2B_CAVPO Reviewed; 448 AA.
AC Q60475;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Alpha-2B adrenergic receptor;
DE AltName: Full=Alpha-2B adrenoreceptor;
DE Short=Alpha-2B adrenoceptor;
DE Short=Alpha-2BAR;
GN Name=ADRA2B;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hartley;
RX PubMed=8573196; DOI=10.1016/0006-2952(95)02179-5;
RA Svensson S.P., Bailey T.J., Porter A.C., Richman J.G., Regan J.W.;
RT "Heterologous expression of the cloned guinea pig alpha 2A, alpha 2B, and
RT alpha 2C adrenoceptor subtypes. Radioligand binding and functional coupling
RT to a cAMP-responsive reporter gene.";
RL Biochem. Pharmacol. 51:291-300(1996).
CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC induced inhibition of adenylate cyclase through the action of G
CC proteins.
CC -!- SUBUNIT: Interacts with RAB26. Interacts with PPP1R9B.
CC {ECO:0000250|UniProtKB:P18089}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA2B sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U25723; AAA67075.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60475; -.
DR SMR; Q60475; -.
DR STRING; 10141.ENSCPOP00000015298; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q60475; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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:0004938; F:alpha2-adrenergic receptor activity; IEA:InterPro.
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 InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000207; ADRA2B_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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 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; Disulfide bond; G-protein coupled receptor; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..448
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069087"
FT TOPO_DOM 1..12
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 13..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 39..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 76..85
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 86..108
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 109..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 131..153
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 154..168
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 169..192
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 193..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 371..394
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 395..403
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 404..427
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 428..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 203..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 92
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 175
FT /note="Implicated in catechol agonist binding"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Implicated in catechol agonist binding"
FT /evidence="ECO:0000250"
FT LIPID 440
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT DISULFID 85..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 448 AA; 49597 MW; 8384F8757E404777 CRC64;
MDHQEPYSVQ ATAAIAAVIT FLILFTIFGN ALVILAVLTS RSLPAPQNLF LVSLAAADIL
VATLIIPFSL ANELLGYWYF WRTWCEVYLA LDVLFCTSSI VHLCAISLDR YWAVSRALEY
NSKRTPRRIK CIILTVWLIA AVISLPPLIY KGDQGPSPRG PQCKINQEAW YILASSIGSF
FAPCLIMILV YLRIYLIAKR SHRRGPRAKG GPGEGESKES RPSPGGAPAS AKVPPLASPL
SSTGEANGHP KPTGEKEEGE TSEDPGARTL PPSWAALPTS GQGQKKAVVL APAEEEAEEE
EEEEGDECEP QAAPGLPASM CSPSLQQPQG SRVLATLRGQ VLLGRGVGAV DGQWWRRRTQ
MTREKRFTFV LAVVIGVFVL CWFPFFFTYS LGAICPQHCK VPHGLFQFFF WIGYCNSSLN
PVIYTIFNQD FRRAFRRILC RQWTQTAW
