ADA2A_DANRE
ID ADA2A_DANRE Reviewed; 388 AA.
AC Q90WY4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alpha-2A adrenergic receptor {ECO:0000250|UniProtKB:P08913};
DE AltName: Full=Alpha-2A adrenoreceptor;
DE Short=Alpha-2A adrenoceptor;
DE Short=Alpha-2AAR;
GN Name=adra2a {ECO:0000250|UniProtKB:P08913};
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 oxymetazoline = epinephrine > norepinephrine.
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. ADRA2A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY048971; AAL07510.1; -; Genomic_DNA.
DR AlphaFoldDB; Q90WY4; -.
DR SMR; Q90WY4; -.
DR STRING; 7955.ENSDARP00000059868; -.
DR PaxDb; Q90WY4; -.
DR PRIDE; Q90WY4; -.
DR ZFIN; ZDB-GENE-021010-1; adra2a.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q90WY4; -.
DR PhylomeDB; Q90WY4; -.
DR Reactome; R-DRE-390696; Adrenoceptors.
DR Reactome; R-DRE-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR Reactome; R-DRE-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR Reactome; R-DRE-418597; G alpha (z) signalling events.
DR PRO; PR:Q90WY4; -.
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:0007186; P:G protein-coupled receptor signaling pathway; ISS:ZFIN.
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 Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..388
FT /note="Alpha-2A adrenergic receptor"
FT /id="PRO_0000069084"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 23..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 49..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 86..95
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 163..173
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 174..198
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 199..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..337
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 338..344
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 345..368
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 369..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 208..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 102
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT SITE 185
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT LIPID 380
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 388 AA; 43997 MW; 431965A04E1986DD CRC64;
MICGANATNG TNATKEYTLL VALPLSIAVG LLILLIIFGN VLVIIAVFTS RALRAPQNLF
LVSLASADIL VATLVMPFSL ANELMGMWTF GGVWCEIYLA LDVLFCTASI THLCAISLDR
YWSITQAIEY NLKRTPQRIK RIIFIVWIIA AVISCPPLIT MKKSEGDICD INKEKWYIVS
SCIGSFFLPC IIMVLVYIRI YQIAKKRTRA PPGDHRKNEV GKKENDPHEK LNGIQNAEPD
DKDEINGVDM EESSSSDHKV SNPCSLKKKS SKGKTKLSQI KPGDGDKTEA CQTTKASRWK
GRQNREKRFT FVLAVVIGVF VICWFPFFFT YTFTAFCDCC VPETLFKFFF WFGYCNSSLN
PIIYTIFNND FRRSFKKILC RRDKRRVV
