AA2DB_DANRE
ID AA2DB_DANRE Reviewed; 415 AA.
AC Q8JG69;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alpha-2Db adrenergic receptor;
DE AltName: Full=Alpha-2Db adrenoceptor;
DE Short=Alpha(2Db)AR;
DE AltName: Full=Alpha-2Db adrenoreceptor;
GN Name=adra2db;
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; AY120896; AAM78032.1; -; Genomic_DNA.
DR RefSeq; NP_919346.1; NM_194365.1.
DR AlphaFoldDB; Q8JG69; -.
DR SMR; Q8JG69; -.
DR PaxDb; Q8JG69; -.
DR PRIDE; Q8JG69; -.
DR GeneID; 266755; -.
DR KEGG; dre:266755; -.
DR CTD; 266755; -.
DR ZFIN; ZDB-GENE-021010-5; adra2db.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q8JG69; -.
DR OrthoDB; 737211at2759; -.
DR PhylomeDB; Q8JG69; -.
DR PRO; PR:Q8JG69; -.
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 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; IPR000735; ADRA2C_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00560; ADRENRGCA2CR.
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..415
FT /note="Alpha-2Db adrenergic receptor"
FT /id="PRO_0000069008"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 59..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 97..106
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 107..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 130..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 151..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..184
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 209..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 340..363
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 364..376
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 377..397
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 398..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 234..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 113
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 415 AA; 46863 MW; C1550DC08B4764B2 CRC64;
MDLSTITFLL PNSSEDTNGT SAPRLPPHSQ CASVLIVLVV TVIILVTIVG NVLVVVAVFT
SRALRAPQNL FLVSLAAADI LVATLVIPFS LANEVMGYWY LGSTWCAFYL ALDVLFCTSS
IVHLCAISLD RYWSVTKAVS YNLKRTPRRI KIMITVVWVI SAVISFPPLL MTKHDELECL
LNNETWYILS SCIVSFFAPG LIMILVYCRI YRVAKQRAST VFVAKNGMER QPSQSETCFV
RKGKSEVESP SSHSSGSRER KGELDDIDLE ESSVSNRHRN SRFAKSRKVE GAQSCPKPNG
RLSWACSRAS ELEQEPRARQ LSLSKSKLAQ MREKRFTFVL AVVMGVFVLC WFPFFFTYSL
HAICRKSCTI PDSLFNLFFW IGYCNSSVNP IIYTIFNRDF RKAFKKIMCR HSTRT
