ADA2B_BOVIN
ID ADA2B_BOVIN Reviewed; 392 AA.
AC O77700;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 129.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9667998; DOI=10.1006/mpev.1998.0517;
RA Stanhope M.J., Madsen O.J., Waddell V.G., Cleven G.C., de Jong W.W.,
RA Springer M.S.;
RT "Highly congruent molecular support for a diverse superordinal clade of
RT endemic African mammals.";
RL Mol. Phylogenet. Evol. 9:501-508(1998).
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; Y15944; CAA75897.2; -; Genomic_DNA.
DR AlphaFoldDB; O77700; -.
DR SMR; O77700; -.
DR STRING; 9913.ENSBTAP00000012514; -.
DR BindingDB; O77700; -.
DR PaxDb; O77700; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; O77700; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IBA:GO_Central.
DR GO; GO:0051379; F:epinephrine binding; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
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; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..>392
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069086"
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..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 357..380
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 381..>392
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT REGION 193..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
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 392
SQ SEQUENCE 392 AA; 42840 MW; 471596A7446475E0 CRC64;
AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
LLGYWYFWRT WCEVYLALDV LFCTSSIVHL CAISLDRYWA VSRALEYNSK RTPRRIKFII
LIVWLIAAVI SLPPLIYKGD QGPQPLARPQ CKLNQEAWYI LASSIGSFFA PCLIMILVYL
RIYLIAKRSH CRGPRAKGGP GERESKQPHP VPGEVSDSAK LPTLASQLAT PGEANGCSQP
RPGEKGDGET PEAPGTPALP PSWPAIPKSG QGQKEGVCGS SPEEEAEEEE EEGCEPQALP
ASPASACSPP LQQPQGSRVL ATLRGQVLLG RGTGTAGAQW WRRRTQLSRE KRFTFVLAVV
IGVFVLCWFP FFFSYSLGAI CPQHCKVPHG LF
