ID   ADA2B_RABIT             Reviewed;         394 AA.
AC   O77830;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   25-MAY-2022, entry version 103.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Stanhope M.J., Madsen O.J., Waddell V.G., Cleven G.C., de Jong W.W.,
RA   Springer M.S., Madsen O.O.M.;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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. Interacts with
CC       GGA1, GGA2 and GGA3. {ECO:0000250|UniProtKB:P18089}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18089};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P18089}.
CC       Note=Interaction with RAB26, GGA1, GGA2 and GGA3 mediates transport
CC       from the Golgi to the cell membrane. {ECO:0000250|UniProtKB:P18089}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRA2B sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y16189; CAA76115.1; -; Genomic_DNA.
DR   EMBL; Y15946; CAA75899.2; -; Genomic_DNA.
DR   AlphaFoldDB; O77830; -.
DR   SMR; O77830; -.
DR   STRING; 9986.ENSOCUP00000019310; -.
DR   BindingDB; O77830; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; O77830; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
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; Membrane;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..>394
FT                   /note="Alpha-2B adrenergic receptor"
FT                   /id="PRO_0000069099"
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..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        359..382
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        383..391
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        392..>394
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   REGION          191..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..299
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        72..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
FT   NON_TER         394
SQ   SEQUENCE   394 AA;  42907 MW;  5D520975ACA6916A CRC64;
     AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
     LLGYWYFRRT WCEVYLALDV LFCTSSIVHL CAISLDRYWA VSRALEYNCK RTPRRIKCII
     LTVWLIAAAI SLPPLIYKGD QGPQPHGAPQ CKLNQEAWYI LSSSLGSFFV PCLIMILVYL
     RIYLIAKRSH RRGPRAKGGP GEGESRQACP VPGGPSASAK LPTLATPVAS ASEANGPSKP
     AGEKEEGETP EDPGTQALPP GWATLPNSGQ GQKEGVSGAS LEEEAEEEEE EEEEEDEPQA
     VPVSPASVGS PPLQQPQGSR VLATLRGQVL VGRGVGAMSG QWWRRRAQLS REKRFTFVLA
     VVIGVFVLCW FPFFFSYSLS AICPQQCRVP HGLF