ADA2C_MOUSE
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 03-AUG-2022, entry version 172.
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 GlyGen; Q01337; 2 sites.
DR iPTMnet; Q01337; -.
DR PhosphoSitePlus; Q01337; -.
DR PaxDb; Q01337; -.
DR PRIDE; Q01337; -.
DR ProteomicsDB; 285609; -.
DR ABCD; Q01337; 1 sequenced antibody.
DR Antibodypedia; 21167; 524 antibodies from 33 providers.
DR DNASU; 11553; -.
DR Ensembl; ENSMUST00000049545; ENSMUSP00000059705; ENSMUSG00000045318.
DR GeneID; 11553; -.
DR KEGG; mmu:11553; -.
DR UCSC; uc009vdd.1; mouse.
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; TQLAIWG; -.
DR OrthoDB; 737211at2759; -.
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; 7 hits in 72 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 tissues.
DR Genevisible; Q01337; MM.
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:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; 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:0032148; P:activation of protein kinase B 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 GO; GO:0035624; P:receptor transactivation; ISO:MGI.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
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..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
