AA2DA_DANRE
ID AA2DA_DANRE Reviewed; 408 AA.
AC Q8JG70;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Alpha-2Da adrenergic receptor;
DE AltName: Full=Alpha-2Da adrenoceptor;
DE Short=Alpha(2Da)AR;
DE AltName: Full=Alpha-2Da adrenoreceptor;
GN Name=adra2da;
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 dexmedetomidine >
CC norepinephrine > epinephrine > oxymetazoline.
CC {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. ADRA2D sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY120895; AAM78031.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8JG70; -.
DR SMR; Q8JG70; -.
DR STRING; 7955.ENSDARP00000105653; -.
DR PaxDb; Q8JG70; -.
DR PRIDE; Q8JG70; -.
DR ZFIN; ZDB-GENE-021010-4; adra2da.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q8JG70; -.
DR PhylomeDB; Q8JG70; -.
DR PRO; PR:Q8JG70; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; 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 InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..408
FT /note="Alpha-2Da adrenergic receptor"
FT /id="PRO_0000069007"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 31..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 56..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 94..103
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 127..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 148..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 171..181
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 206..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..356
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 357..369
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 370..390
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 391..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 242..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 110
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 188
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT SITE 192
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 408 AA; 46199 MW; 5535ADE8177FB860 CRC64;
MSVTPTANST EEAANITASP RLWPYTEPAS AIIILVVSLI ILLTIVGNVL VIVAVLTSRA
LRAPQNLFLV SLACADILVA TLVIPFSLAN EIMGYWYFGS TWCAFYLALD VLFCTSSIVH
LCAISLDRYW SVTKAVRYNL KRTPRRIKCM IAVVWLISAV ISFPPLIMTK HDEKECLIND
ETWYILSSCA VSFFAPGLIM ITVYCKIYRV AKQRSSTVFV AKNGLERQPS QSETCFVRKD
KFEKESPSSN SSESAQRQEE LDDIDLEESA ASDSRARGSR FSKRRRVEGE RRGPQRSCRV
SWAAHQEPGS RQQQLASKSK VAQMREKRFT FVLAVVMGVF VLCWFPFFFT YSLQAVCGER
CGPPEALFKL FFWIGYCNSS VNPIIYTIFN RDFRKAFKKV VCWSAQRT
