ADA2C_CAVPO
ID ADA2C_CAVPO Reviewed; 455 AA.
AC Q60476;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 95.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hartley;
RX PubMed=8573196; DOI=10.1016/0006-2952(95)02179-5;
RA Svensson S.P., Bailey T.J., Porter A.C., Richman J.G., Regan J.W.;
RT "Heterologous expression of the cloned guinea pig alpha 2A, alpha 2B, and
RT alpha 2C adrenoceptor subtypes. Radioligand binding and functional coupling
RT to a cAMP-responsive reporter gene.";
RL Biochem. Pharmacol. 51:291-300(1996).
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; U25724; AAA67076.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60476; -.
DR SMR; Q60476; -.
DR InParanoid; Q60476; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IEA:InterPro.
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..455
FT /note="Alpha-2C adrenergic receptor"
FT /id="PRO_0000069103"
FT TOPO_DOM 1..47
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 73..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..120
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 121..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 144..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 165..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 188..203
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 204..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 228..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 377..400
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 401..413
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 414..434
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 435..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 241..340
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 127
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT SITE 214
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 455 AA; 49351 MW; 6B657D247FF8A3F4 CRC64;
MASPALAAAL LAAEGPNASG AGEGGGGVNA SGAVWGPPPS QYSAGAVAGL AAVVGFLIVF
TVVGNVLVVI AVLTSRALRA PQNLFLVSLA SADILVATLV MPFSLANELM AYWYFGQVWC
GVYLALDVLF CTSSIVHLCA ISLDRYWSVT QAVEYNLKRT PRRVKATIVA VWLISAIISF
PPLVSFYRQP DGAAYPRCGL NDETWYILSS CIGSFFAPCL IMGLVYARIY RVAKLRTRTL
SEKRGPAGPE GESPTTENGL GAAAAAAAGE NGHCAPPRAD VEPDESSAAE RRRRRGALRR
GARQREAGVE APGPGLGSAA ADPGALSVSR SPGPGGRLSR ASSRSVEFFL SRRRRARSSV
CRRKVAQARE KRFTFVLAVV MGVFVLCWFP FFFSYSLYGI CREACQLPTP LFKFFFWIGY
CNSSLNPVIY TIFNQDFRRS FKHILFRRRR RGFRQ
