ID   ADA2C_MOUSE             Reviewed;         458 AA.
AC   Q01337;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Alpha-2C adrenergic receptor;
DE   AltName: Full=Alpha-2 adrenergic receptor subtype C4;
DE   AltName: Full=Alpha-2C adrenoreceptor;
DE            Short=Alpha-2C adrenoceptor;
DE            Short=Alpha-2CAR;
GN   Name=Adra2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1353249;
RA   Link R.E., Daunt D.A., Barsh G., Chruscinski A.J., Kobilka B.K.;
RT   "Cloning of two mouse genes encoding alpha 2-adrenergic receptor subtypes
RT   and identification of a single amino acid in the mouse alpha 2-C10 homolog
RT   responsible for an interspecies variation in antagonist binding.";
RL   Mol. Pharmacol. 42:16-27(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2J;
RX   PubMed=8387367;
RA   Chang Y.-H., Chang A.C., Chen W.-M., Chang N.-C.A.;
RT   "Molecular characterization of a murine homologue of alpha 2C4 adrenoceptor
RT   subtype gene.";
RL   Biochem. Mol. Biol. Int. 29:467-474(1993).
CC   -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC       induced inhibition of adenylate cyclase through the action of G
CC       proteins.
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; M99376; AAA37212.1; -; Genomic_DNA.
DR   EMBL; M97516; AAA37183.1; -; Genomic_DNA.
DR   CCDS; CCDS19226.1; -.
DR   PIR; A48392; A48392.
DR   PIR; I49480; I49480.
DR   RefSeq; NP_031444.2; NM_007418.3.
DR   AlphaFoldDB; Q01337; -.
DR   SMR; Q01337; -.
DR   IntAct; Q01337; 1.
DR   STRING; 10090.ENSMUSP00000059705; -.
DR   ChEMBL; CHEMBL4826; -.
DR   DrugCentral; Q01337; -.
DR   GlyCosmos; Q01337; 2 sites, No reported glycans.
DR   GlyGen; Q01337; 2 sites.
DR   iPTMnet; Q01337; -.
DR   PhosphoSitePlus; Q01337; -.
DR   PaxDb; 10090-ENSMUSP00000059705; -.
DR   ProteomicsDB; 285609; -.
DR   ABCD; Q01337; 1 sequenced antibody.
DR   Antibodypedia; 21167; 573 antibodies from 33 providers.
DR   DNASU; 11553; -.
DR   Ensembl; ENSMUST00000049545.7; ENSMUSP00000059705.6; ENSMUSG00000045318.7.
DR   GeneID; 11553; -.
DR   KEGG; mmu:11553; -.
DR   UCSC; uc009vdd.1; mouse.
DR   AGR; MGI:87936; -.
DR   CTD; 152; -.
DR   MGI; MGI:87936; Adra2c.
DR   VEuPathDB; HostDB:ENSMUSG00000045318; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000161707; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; Q01337; -.
DR   OMA; KGHKPQL; -.
DR   OrthoDB; 3087922at2759; -.
DR   PhylomeDB; Q01337; -.
DR   TreeFam; TF316350; -.
DR   Reactome; R-MMU-390696; Adrenoceptors.
DR   Reactome; R-MMU-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR   Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-418597; G alpha (z) signalling events.
DR   Reactome; R-MMU-5683826; Surfactant metabolism.
DR   BioGRID-ORCS; 11553; 8 hits in 77 CRISPR screens.
DR   PRO; PR:Q01337; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q01337; Protein.
DR   Bgee; ENSMUSG00000045318; Expressed in lumbar dorsal root ganglion and 60 other cell types or tissues.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0031694; F:alpha-2A adrenergic receptor binding; ISO:MGI.
DR   GO; GO:0004938; F:alpha2-adrenergic receptor activity; ISO:MGI.
DR   GO; GO:0051379; F:epinephrine binding; ISO:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0071875; P:adrenergic receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007565; P:female pregnancy; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0070473; P:negative regulation of uterine smooth muscle contraction; ISO:MGI.
DR   GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR   CDD; cd15323; 7tmA_alpha2C_AR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
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.
DR   Genevisible; Q01337; MM.
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..458
FT                   /note="Alpha-2C adrenergic receptor"
FT                   /id="PRO_0000069106"
FT   TOPO_DOM        1..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        52..76
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        77..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        89..114
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        115..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        125..147
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        148..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        169..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        192..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        208..231
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        232..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        380..403
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        404..416
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        417..437
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        438..458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          245..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            131
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            214
FT                   /note="Implicated in catechol agonist binding and receptor
FT                   activation"
FT                   /evidence="ECO:0000250"
FT   SITE            218
FT                   /note="Implicated in catechol agonist binding and receptor
FT                   activation"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        124..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        196
FT                   /note="G -> V (in Ref. 2; AAA37183)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="G -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="L -> V (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   458 AA;  49906 MW;  C0A8BDF0302BF1FB CRC64;
     MASPALAAAL AAAAAEGPNG SDAGEWGSGG GANASGTDWV PPPGQYSAGA VAGLAAVVGF
     LIVFTVVGNV LVVIAVLTSR ALRAPQNLFL VSLASADILV ATLVMPFSLA NELMAYWYFG
     QVWCGVYLAL DVLFCTSSIV HLCAISLDRY WSVTQAVEYN LKRTPRRVKA TIVAVWLISA
     VISFPPLVSF YRRPDGAAYP QCGLNDETWY ILSSCIGSFF APCLIMGLVY ARIYRVAKLR
     TRTLSEKRGP AGPDGASPTT ENGLGKAAGE NGHCAPPRTE VEPDESSAAE RRRRRGALRR
     GGRRREGAEG DTGSADGPGP GLAAEQGART ASRSPGPGGR LSRASSRSVE FFLSRRRRAR
     SSVCRRKVAQ AREKRFTFVL AVVMGVFVLC WFPFFFSYSL YGICREACQL PEPLFKFFFW
     IGYCNSSLNP VIYTVFNQDF RRSFKHILFR RRRRGFRQ
//