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}.
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; 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