ADA2C_DANRE
ID ADA2C_DANRE Reviewed; 432 AA.
AC Q90WY6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alpha-2C adrenergic receptor;
DE AltName: Full=Alpha-2C adrenoreceptor;
DE Short=Alpha-2C adrenoceptor;
DE Short=Alpha-2CAR;
GN Name=adra2c;
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. {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. ADRA2C sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY048969; AAL07508.1; -; Genomic_DNA.
DR RefSeq; NP_997522.1; NM_207639.1.
DR AlphaFoldDB; Q90WY6; -.
DR SMR; Q90WY6; -.
DR STRING; 7955.ENSDARP00000101388; -.
DR PaxDb; Q90WY6; -.
DR PRIDE; Q90WY6; -.
DR Ensembl; ENSDART00000101562; ENSDARP00000101388; ENSDARG00000069669.
DR Ensembl; ENSDART00000188270; ENSDARP00000152698; ENSDARG00000109788.
DR GeneID; 266752; -.
DR KEGG; dre:266752; -.
DR CTD; 152; -.
DR ZFIN; ZDB-GENE-021010-3; adra2c.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161707; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; Q90WY6; -.
DR OMA; TQLAIWG; -.
DR OrthoDB; 737211at2759; -.
DR PhylomeDB; Q90WY6; -.
DR TreeFam; TF316350; -.
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:Q90WY6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000069669; Expressed in spleen and 4 other tissues.
DR ExpressionAtlas; Q90WY6; baseline.
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: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 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 PANTHER; PTHR24248:SF25; PTHR24248:SF25; 1.
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..432
FT /note="Alpha-2C adrenergic receptor"
FT /id="PRO_0000069108"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 61..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 99..108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 132..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 153..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 176..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..215
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 216..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 352..379
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 380..392
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 393..413
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 414..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 115
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT SITE 202
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 432 AA; 49137 MW; 1A52F0283C663DA7 CRC64;
MHNLSYASEE DTYTDTDFTP SGNSTNSTSY SPATIIGLAG LVSFLILFTI VGNVLVVIAV
LTSRALKPPQ NLFLVSLASA DILVATLIIP FSLANELMGY WFFGEVWCNI YLALDVLFCT
SSIVHLCAIS LDRYWSVTQA VEYNLKRTPR RVKGMIVVVW LISAVISFPP LISMDRNTVD
ERRPMCQLND HTWYILYSSI GSFFAPCVIM ILVYIRIYQV AKTRTRNMSE KRRDPDGGSG
TPRLENGLSR EDSRRENGHC SSSPGERKPA EDNPDADLED SSSSDEKAKR SQNETAPSKK
DRRSSRKNSS SSKHSSRKSR ASSKSLDLFS SRRKRRNTIS RKKISQAREK RFTFVLAVVM
GVFVVCWFPF FFSYSLYGIC REPCAIPDPL FKFFFWIGYC NSSLNPVIYT IFNQDFRRAF
QKILCKSWKR SF
