ID   ADA2B_DIDVI             Reviewed;         382 AA.
AC   O77715;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
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   Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS   virginiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX   NCBI_TaxID=9267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9667998; DOI=10.1006/mpev.1998.0517;
RA   Stanhope M.J., Madsen O.J., Waddell V.G., Cleven G.C., de Jong W.W.,
RA   Springer M.S.;
RT   "Highly congruent molecular support for a diverse superordinal clade of
RT   endemic African mammals.";
RL   Mol. Phylogenet. Evol. 9:501-508(1998).
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; Y15943; CAA75896.1; -; Genomic_DNA.
DR   AlphaFoldDB; O77715; -.
DR   SMR; O77715; -.
DR   BindingDB; O77715; -.
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..>382
FT                   /note="Alpha-2B adrenergic receptor"
FT                   /id="PRO_0000069088"
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..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        347..370
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        371..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        380..>382
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   REGION          192..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..285
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..305
FT                   /note="Polar 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         382
SQ   SEQUENCE   382 AA;  41870 MW;  EAFF12DD44B2AA19 CRC64;
     AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
     LLGYWYFRHT WCEVYLALDV LFCTSSIVHL CAISLDRYWS VSRALEYNSK RTPRRIKGII
     LTVWLIAAFI SLPPLIYKGD KGKKPGGRPQ CKLNEEAWYI LSSSIGSFFA PCLIMILVYL
     RIYLIAKRRN RQGPHGKQAP GDGDTGPSAL GGTSTISKLP PSILPAVGEA NGHSKPPGER
     EGGEQMGDPT SPSTPPNQSS VGPEDGSQKQ EEEEEEEEEE EEECGPPAPP TSSSLQGTPN
     FQPSQGSQVL ATLRGQVLLA RGPASLGLQP WRRRTQMNRE KRFTFVLAVV IGVFVLCWFP
     FFFSYSLGAI CPQHCKVPHG LF