ID   ADA2B_DUGDU             Reviewed;         390 AA.
AC   O77713;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   25-MAY-2022, entry version 89.
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   Dugong dugon (Dugong) (Trichechus dugon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Dugongidae; Dugong.
OX   NCBI_TaxID=29137;
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}.
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DR   EMBL; Y15947; CAA75900.2; -; Genomic_DNA.
DR   AlphaFoldDB; O77713; -.
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   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; Membrane;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..>390
FT                   /note="Alpha-2B adrenergic receptor"
FT                   /id="PRO_0000069089"
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..354
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        355..378
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        379..>390
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   REGION          191..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..311
FT                   /note="Disordered"
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         390
SQ   SEQUENCE   390 AA;  42563 MW;  779F849267F9F314 CRC64;
     AIATVITFLI LFTIFGNSLV ILAVLTSRSL RAPQNLFLVS LAAADIMVAT LIIPFSLANE
     LLGYWYFRRT WCEVYLALDV LFCTSSIVHL CAISLDRYWA VSRALEYNSK RTPRRIKCII
     LTVWLIAAAI SLPPLIYKGD QGPQPRGRPQ CKLNQEAWYI LSSSIGSFFA PCLIMILVYL
     RIYLIAKRSH RRGPGAKGGP RKGESKQPHS LDSGPSALAN LPTLASSLAV AGEANGHSMP
     PGEKERETSE DPGTPTLPPS WPVLPNSGQG QKGGVCGASL EEEADKEEEE ECGPPAVPAS
     PATACNPPLQ QPQGSQVLAT LRGQVFLGRG VGAAGGQWWR RWAQLTREKR FTFVLAVVIG
     VFVLCWFPFF FSYSLGAICP QHCKVPHGLF