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   27-MAR-2024, entry version 141.
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   GlyCosmos; Q90WY6; 3 sites, No reported glycans.
DR   PaxDb; 7955-ENSDARP00000101388; -.
DR   GeneID; 266752; -.
DR   KEGG; dre:266752; -.
DR   AGR; ZFIN:ZDB-GENE-021010-3; -.
DR   CTD; 152; -.
DR   ZFIN; ZDB-GENE-021010-3; adra2c.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; Q90WY6; -.
DR   OMA; RVKGMII; -.
DR   OrthoDB; 3087922at2759; -.
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; Alternate scaffold 1.
DR   Proteomes; UP000000437; Chromosome 1.
DR   Bgee; ENSDARG00000069669; Expressed in spleen and 4 other cell types or tissues.
DR   ExpressionAtlas; Q90WY6; baseline and differential.
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: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   CDD; cd15323; 7tmA_alpha2C_AR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000735; ADRA2C_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF25; ALPHA-2C ADRENERGIC RECEPTOR; 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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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
//