ADA2B_ELEMA
ID ADA2B_ELEMA Reviewed; 384 AA.
AC O19014;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
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 Elephas maximus (Indian elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Elephas.
OX NCBI_TaxID=9783;
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).
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; Y12525; CAA73125.1; -; Genomic_DNA.
DR AlphaFoldDB; O19014; -.
DR SMR; O19014; -.
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; Lipoprotein;
KW Membrane; Palmitate; Receptor; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..>384
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069091"
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 192..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
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 384
SQ SEQUENCE 384 AA; 41912 MW; CF41B56CC355B94F CRC64;
AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
LLGYWYFRRT WCEVYLALDV LFCTSSIVHL CAISLDRYWA VSRALQYNSK RTPRRIKCVI
LTVWLIAAAI SLPPLIYKGD QGPQPRGRPQ CKLNQEAWYI LSSSIGSFFA PCLIMILVYL
RIYLIAKRSN RRGPRAKGAP REGEPKQPHP LPAGPSALAN SPTLASSLAV TGEANGHSEP
PGEKERETPE DPGTLTLPPS WPVLPNSGQG QKEGVCGASP EEEEECGSPA VPASPALACS
PPLQQPKGSR VLATLRGQVL LGRGVGTAGG QWWRRRAQLT REKRFTFVLA VVIGVFVLCW
FPFFFSYSLG AICPQHCKVP HGLF
