ID ADA2B_ERIEU Reviewed; 391 AA.
AC O19012;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 24-JAN-2024, entry version 102.
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 Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365;
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; Y12521; CAA73121.1; -; Genomic_DNA.
DR AlphaFoldDB; O19012; -.
DR SMR; O19012; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; O19012; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
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 CDD; cd15321; 7tmA_alpha2B_AR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000207; ADRA2B_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24248:SF130; ALPHA-2B ADRENERGIC RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00559; ADRENRGCA2BR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..>391
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069092"
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..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 356..379
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 380..388
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 389..>391
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT REGION 194..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Acidic 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 391
SQ SEQUENCE 391 AA; 42920 MW; F21FA2757B1EE1DA CRC64;
AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
LLGYWYFRRT WCEVYLALDV LFCTSSIVHL CAISLDRYWA VSRALEYNSK RTPRRIKCII
LTVWLIAAVI SLPPLIYKGD QGPQPRGRPQ CKLNQEAWYI LASSIGSFFA PCLIMILVYL
RIYLIAKRSH CRGPRAKGAP GKGESKQTGQ ASLGAPSSAK LPNLVSRLVA AREANRHSKS
TGEKVEGETP EGPGTPGVPP SWPPLPSSGR GQEEDIYRAS PEEEAGDDEE EECEPQAVPV
SPASACSPPL QQPQGSRVLA TLRGQVLLSR GVGTASGQWW RRRAQLTREK RFTFVLAVVI
GVFVLCWFPF FFSYSLGAIC PQHCKVPHGL F
//
