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ADA2B_MACPR
ID   ADA2B_MACPR             Reviewed;         387 AA.
AC   O19025;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   02-JUN-2021, entry version 90.
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   Macroscelides proboscideus (Short-eared elephant shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Macroscelidea; Macroscelididae; Macroscelides.
OX   NCBI_TaxID=29082;
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).
RN   [2]
RP   SEQUENCE REVISION TO 148 AND 255.
RA   Springer M.S., Cleven G.C., Madsen O.J., de Jong W.W., Waddell V.G.,
RA   Amrine H.M., Stanhope M.J.;
RL   Submitted (MAY-2000) 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; Y12524; CAA73124.2; -; 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; Lipoprotein;
KW   Membrane; Palmitate; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..>387
FT                   /note="Alpha-2B adrenergic receptor"
FT                   /id="PRO_0000069095"
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..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        352..375
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        376..384
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        385..>387
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   REGION          193..305
FT                   /note="Disordered"
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         387
SQ   SEQUENCE   387 AA;  42590 MW;  B74AD5F0EE23BD5A CRC64;
     AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
     LLGYWYFRHT WCXVYLALDV LFCTSSIVHL CAISLDRYWA VSRALEYNSK RTPRRIKCII
     LTVWLIAAAI SLPPLIYKGD QDPQPRGRPQ CKLNQEAWYI LSSSIGSFFV PCLIMILVYL
     RIYLIAKRSS SRRKPRAKGX PREGESKQPQ LRPVGTSVSA RPPALTSPLA VTGEANGHSK
     PTGERETPED LVSPASPPSW PAIPNSGQGR KEGVCGTSPE EEAEEEEECG PEAVPASPAL
     ACSPSLQPPQ GSRVLATLRG QVLLGRGVGT ARGQWWRRRA QLTREKRFTF VLAVVIGVFV
     LCWFPFFFSY SLGAICPQHC KVPHGLF
 
 
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