ADA2B_AMBHO
ID ADA2B_AMBHO Reviewed; 386 AA.
AC O18935;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 25-MAY-2022, entry version 97.
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 Amblysomus hottentotus (Hottentot golden mole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Chrysochloridae; Amblysominae; Amblysomus.
OX NCBI_TaxID=9391;
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 121.
RA Madsen O.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; Y12526; CAA73126.2; -; Genomic_DNA.
DR AlphaFoldDB; O18935; -.
DR SMR; O18935; -.
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..>386
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069085"
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..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 351..374
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 375..383
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 384..>386
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT REGION 193..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Polar residues"
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 386
SQ SEQUENCE 386 AA; 42158 MW; ECE11E0B7192D95E CRC64;
AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
LLGYWYFRHM WCEVYLALDV LFCTSSIVHL CAISLDRYWA VSRALEYNSK RTPRRIKCII
LTVWLIAAAI SLPPLIYKGD QGPQPHGRPQ CKLNQEAWYI LSSSIGSFFA PCLIMILVYL
RIYLIAKRSN RRGPRAKGAT REGESKLPHP MAAGASASAK PPTLTSSLAV AGEANGHSKP
TGEEGETLED PVTSTLPPSW PALPNSDQGQ KEGVCETSPE EDDEEEECGP QAVPVSPASA
GSPPLQQPQG SRVLATLRGQ VLLGRGVGAA GGQWWRRRTQ LTREKRFTFV LAVVIGVFVL
CWFPFFFSYS LGAICPQHCK VPHGLF
