ADA2B_HORSE
ID ADA2B_HORSE Reviewed; 389 AA.
AC O77721;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 105.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
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).
RN [2]
RP SEQUENCE REVISION.
RA Madsen O.J.;
RL Submitted (NOV-1999) 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; Y15945; CAA75898.2; -; Genomic_DNA.
DR AlphaFoldDB; O77721; -.
DR SMR; O77721; -.
DR STRING; 9796.ENSECAP00000005015; -.
DR PaxDb; O77721; -.
DR PRIDE; O77721; -.
DR InParanoid; O77721; -.
DR Proteomes; UP000002281; 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..>389
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069093"
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..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 364..387
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 388..>389
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT REGION 194..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..302
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 389
SQ SEQUENCE 389 AA; 42258 MW; 992179431679B0FD CRC64;
AIAAVITFLI LFTIFGNALV ILAVLTSRSL RAPQNLFLVS LAAADILVAT LIIPFSLANE
LLGYWYFRRT WCEVYLALDV LFCTSSIVHL CAISLDRYWA VTRALEYNTK RTPRRIKCII
LTVWLIAAVI SLPPLIYKGD QGPQPRGRPQ CKLNQEAWYI LASSIGSFFA PCLIMILVYL
RIYLIAKRSH LRGPRAKGGP GGGGSKQPHP VPAGASASAK LPTVASCLAA AGEANGHSEP
TGEKEAETPE DSGTPALPSS WPALPSSGQD QKEGVCGASL EEEAEEEEEE EEEEEEGEEE
CEPQALPASP ASACSPPLQQ PQGSRVLATL RGQVLLGRGV ATAGAQWWRR RAQLTREKRF
TFVLAVVIGV FVLCWFPFFF SYSLGAICP
