ADA2C_RAT
ID ADA2C_RAT Reviewed; 458 AA.
AC P22086;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 164.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1704126; DOI=10.1073/pnas.88.3.1019;
RA Flordellis C.S., Handy D.E., Bresnahan M.R., Zannis V.I., Gavras H.;
RT "Cloning and expression of a rat brain alpha 2B-adrenergic receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1019-1023(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1704314; DOI=10.1016/0014-5793(91)80080-m;
RA Voigt M.M., McCune S.K., Kanterman R.Y., Felder C.C.;
RT "The rat alpha 2-C4 adrenergic receptor gene encodes a novel
RT pharmacological subtype.";
RL FEBS Lett. 278:45-50(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1645350; DOI=10.1016/s0021-9258(18)99248-3;
RA Lanier S.M., Downing S., Duzic E., Homcy C.J.;
RT "Isolation of rat genomic clones encoding subtypes of the alpha 2-
RT adrenergic receptor. Identification of a unique receptor subtype.";
RL J. Biol. Chem. 266:10470-10478(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Saitoh M., Imai A., Shimomura H.;
RT "Cloning of rat alpha-2-B-adrenergic receptor gene and expression in rat
RT submandibular gland.";
RL Shigaku 80:317-326(1992).
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; M58316; AAA40634.1; -; mRNA.
DR EMBL; X57659; CAA40861.1; -; Genomic_DNA.
DR EMBL; M62371; AAA42033.1; -; Genomic_DNA.
DR EMBL; D00819; BAA00700.1; -; Genomic_DNA.
DR PIR; A37869; A37869.
DR PIR; A40392; A40392.
DR RefSeq; NP_612515.1; NM_138506.1.
DR AlphaFoldDB; P22086; -.
DR SMR; P22086; -.
DR STRING; 10116.ENSRNOP00000012322; -.
DR BindingDB; P22086; -.
DR ChEMBL; CHEMBL314; -.
DR DrugCentral; P22086; -.
DR GlyGen; P22086; 2 sites.
DR PhosphoSitePlus; P22086; -.
DR PaxDb; P22086; -.
DR Ensembl; ENSRNOT00000012322; ENSRNOP00000012322; ENSRNOG00000009299.
DR GeneID; 24175; -.
DR KEGG; rno:24175; -.
DR CTD; 152; -.
DR RGD; 2058; Adra2c.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161707; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P22086; -.
DR OMA; TQLAIWG; -.
DR OrthoDB; 737211at2759; -.
DR PhylomeDB; P22086; -.
DR TreeFam; TF316350; -.
DR Reactome; R-RNO-390696; Adrenoceptors.
DR Reactome; R-RNO-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-418597; G alpha (z) signalling events.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR PRO; PR:P22086; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000009299; Expressed in frontal cortex and 1 other tissue.
DR Genevisible; P22086; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0031694; F:alpha-2A adrenergic receptor binding; ISO:RGD.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; ISO:RGD.
DR GO; GO:0051379; F:epinephrine binding; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:RGD.
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:RGD.
DR GO; GO:0007565; P:female pregnancy; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0070473; P:negative regulation of uterine smooth muscle contraction; IMP:RGD.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0035624; P:receptor transactivation; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
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 2: Evidence at transcript level;
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_0000069107"
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 24
FT /note="G -> R (in Ref. 4; BAA00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="G -> A (in Ref. 1; AAA40634)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="N -> T (in Ref. 1; AAA40634)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Q -> E (in Ref. 2; CAA40861)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="S -> T (in Ref. 1; AAA40634)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="G -> R (in Ref. 3; AAA42033)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="A -> R (in Ref. 4; BAA00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="L -> V (in Ref. 3; AAA42033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 49864 MW; 6846C2AF963B33BF CRC64;
MASPALAAAL AAAAAEGPNG SDAGEWGSGG GANASGTDWG 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
