ID   ADA2B_TALEU             Reviewed;         397 AA.
AC   O19091;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Alpha-2B adrenergic receptor;
DE   AltName: Full=Alpha-2B adrenoreceptor;
DE            Short=Alpha-2B adrenoceptor;
DE            Short=Alpha-2BAR;
DE   Flags: Fragment;
GN   Name=ADRA2B;
OS   Talpa europaea (European mole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Talpidae; Talpa.
OX   NCBI_TaxID=9375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9214502; DOI=10.1038/40386;
RA   Springer M.S., Cleven G.C., Madsen O.J., de Jong W.W., Waddell V.G.,
RA   Amrine H.M., Stanhope M.J.;
RT   "Endemic African mammals shake the phylogenetic tree.";
RL   Nature 388:61-64(1997).
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; Y12520; CAA73120.1; -; Genomic_DNA.
DR   AlphaFoldDB; O19091; -.
DR   SMR; O19091; -.
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   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; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..>397
FT                   /note="Alpha-2B adrenergic receptor"
FT                   /id="PRO_0000069101"
FT   TRANSMEM        <1..25
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        26..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        37..62
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        63..72
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        73..95
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        96..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        118..140
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        141..156
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        157..180
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        181..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        362..385
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        386..394
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        395..>397
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   REGION          193..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..299
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            79
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            163
FT                   /note="Implicated in catechol agonist binding"
FT                   /evidence="ECO:0000250"
FT   SITE            167
FT                   /note="Implicated in catechol agonist binding"
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
FT   NON_TER         397
SQ   SEQUENCE   397 AA;  43621 MW;  9C3812515ADC3EB4 CRC64;
     AIAAIIIFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
     LLGYWYFRRM WCKVYLALDV LFCTSSIVHL CAISLDRYWA VSRALEYNSK RTPRRIKCII
     LMVWLIAAVI SLPSLVYKGD QGPQPSGAPQ CNLNQETWYI LASSIGSFFA PCLIMILVYL
     RIYLIAKRSH CRGPRAKGAP GKSKFKQSRQ VPGGTLASAK VPNLAAHLVA AGETNGRSKP
     TGEKEMGETP EDSGTSTLPP SWPALPNSGQ DQKEGICEAS LEEEAEEEEE GEEEREEECE
     PQALPASPAS ACSPPLQQPQ GSQVLATLRG QVLLGRAAGA ASGQWWRRRT QLSREKRFTF
     VLAVVIGVFV LCWFPFFFSY SLGAICPQQC KVPHDLF