ADA2B_DANRE
ID ADA2B_DANRE Reviewed; 510 AA.
AC Q90WY5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Alpha-2B adrenergic receptor;
DE AltName: Full=Alpha-2B adrenoreceptor;
DE Short=Alpha-2B adrenoceptor;
DE Short=Alpha-2BAR;
GN Name=adra2b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12949138; DOI=10.1093/molbev/msg224;
RA Ruuskanen J.O., Xhaard H., Marjamaki A., Salaneck E., Salminen T.,
RA Yan Y.-L., Postlethwait J.H., Johnson M.S., Larhammar D., Scheinin M.;
RT "Identification of duplicated fourth alpha2-adrenergic receptor subtype by
RT cloning and mapping of five receptor genes in zebrafish.";
RL Mol. Biol. Evol. 21:14-28(2004).
RN [2]
RP FUNCTION, AND 3D-STRUCTURE MODELING.
RX PubMed=15655522; DOI=10.1038/sj.bjp.0706057;
RA Ruuskanen J.O., Laurila J., Xhaard H., Rantanen V.-V., Vuoriluoto K.,
RA Wurster S., Marjamaki A., Vainio M., Johnson M.S., Scheinin M.;
RT "Conserved structural, pharmacological and functional properties among the
RT three human and five zebrafish alpha2-adrenoceptors.";
RL Br. J. Pharmacol. 144:165-177(2005).
CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC induced inhibition of adenylate cyclase through the action of G
CC proteins. The order of potency for this receptor is norepinephrine >
CC epinephrine. {ECO:0000269|PubMed:15655522}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; AY048970; AAL07509.1; -; Genomic_DNA.
DR RefSeq; NP_997521.1; NM_207638.1.
DR AlphaFoldDB; Q90WY5; -.
DR SMR; Q90WY5; -.
DR STRING; 7955.ENSDARP00000110714; -.
DR PaxDb; Q90WY5; -.
DR GeneID; 266751; -.
DR KEGG; dre:266751; -.
DR CTD; 151; -.
DR ZFIN; ZDB-GENE-021010-2; adra2b.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q90WY5; -.
DR OrthoDB; 737211at2759; -.
DR PhylomeDB; Q90WY5; -.
DR Reactome; R-DRE-390696; Adrenoceptors.
DR Reactome; R-DRE-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR Reactome; R-DRE-418597; G alpha (z) signalling events.
DR PRO; PR:Q90WY5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:ZFIN.
DR GO; GO:0004936; F:alpha-adrenergic receptor activity; ISS:ZFIN.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IDA:UniProtKB.
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:0071881; P:adenylate cyclase-inhibiting adrenergic receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:ZFIN.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
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; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="Alpha-2B adrenergic receptor"
FT /id="PRO_0000069102"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 42..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 68..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 105..114
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 115..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 138..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 160..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 185..200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 225..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 433..456
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 457..465
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 466..489
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 490..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 234..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 121
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 207
FT /note="Implicated in catechol agonist binding"
FT /evidence="ECO:0000250"
FT SITE 211
FT /note="Implicated in catechol agonist binding"
FT /evidence="ECO:0000250"
FT LIPID 502
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 510 AA; 55971 MW; 1CB07C0AFC6DE3D3 CRC64;
MDSPCPVAVG LPGHTNGTGG TSSPTCNQSM IKLAPYSPEA TAAFATAITL MMLITIVGNI
LVIIAVLTSR SLRGPQNLFL VSLAAADILV ATLIIPFSLA NELMGYWYFR SVWCEIYLAL
DVLFCTSSIV HLCAISLDRY MSISRAVTYG PKRTPKRIKC AILVVWLISA VISFPPLLSM
NKNKGGGESG ALPQCQLNDE RWYILYSTIG SFFAPCLIMI LVYMRIYQIA KQRTRCPPGE
PRKEAPANAT TPQHKIQNGR GDETPGTLQK KARPPTLAVS QVESVQQAAN TPIANNLLQA
PSTTLTPTTP CPSPSPSNSS EVAPSKSKEG KKEKKKKKNN KNKNKKEPDN NNGESMSSDS
DTEQGGRGLE VPCTPTMTPS GIHSPATMQK YRDMIATAKG AKLVARKAKQ DGTPNSARRK
AMVNREKRFT FVLAVVIGVF VICWFPFFFS YSLQAVCPES CALPEPLFKF FFWIGYCNSC
LNPVIYTIFN KDFRRAFKKI LCKNTKGTFF
