ID   ADA2B_ECHTE             Reviewed;         384 AA.
AC   O77723;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   02-JUN-2021, entry version 84.
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   Echinops telfairi (Lesser hedgehog tenrec).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Tenrecidae; Tenrecinae; Echinops.
OX   NCBI_TaxID=9371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9707584; DOI=10.1073/pnas.95.17.9967;
RA   Stanhope M.J., Waddell V.G., Madsen O.J., de Jong W.W., Hedges S.B.,
RA   Cleven G.C., Kao D., Springer M.S.;
RT   "Molecular evidence for multiple origins of Insectivora and for a new order
RT   of endemic African insectivore mammals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:9967-9972(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}.
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; Y17692; CAA76816.1; -; Genomic_DNA.
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; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..>384
FT                   /note="Alpha-2B adrenergic receptor"
FT                   /id="PRO_0000069090"
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..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        349..372
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        373..381
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        382..>384
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   REGION          193..308
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         384
SQ   SEQUENCE   384 AA;  41692 MW;  331EBD31475AE384 CRC64;
     AIAAVTTFLI LFTVFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIXPFSLANE
     LLGYWYFWHT WCEVYLALXV LXCTSSIVHL CAISLDRYWA VSRALEYNSK RTPRRIXGII
     LTVWLIAAAI SLPPLIYKGD QGPQPHGRPQ CRLNQEAWYI LSSSIGSFFA PCLIMILVYL
     RIYLIAKRRN RRGPRAQGAS KGGASKQPHP LAGGASTKPP TLTSSLAVAG EVNGHSKPTG
     QEGKTPEDLG VVTLPPNWPA LPNSGQGQKE GVCGISPEXA EEEEEGGPEA LPASPASXGS
     PQLQQPQGTR VLVTLRGQVV LSRGLGAASG QWWRRRTQLT REKRFTFVLA VVIGVXVLCW
     FPFFXSYSLG AICPQHCTVX HGLF