ADA2C_DIDVI
ID ADA2C_DIDVI Reviewed; 469 AA.
AC P35405;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 98.
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 Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=7509437;
RA Blaxall H.S., Cerutis D., Hass N.A., Iversen L.J., Bylund D.B.;
RT "Cloning and expression of the alpha 2C-adrenergic receptor from the OK
RT cell line.";
RL Mol. Pharmacol. 45:176-181(1994).
RN [2]
RP SEQUENCE REVISION TO 60; 75; 110; 143; 326-332; 365 AND 432.
RA Bylund D.B.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U04310; AAA17566.2; -; mRNA.
DR AlphaFoldDB; P35405; -.
DR SMR; P35405; -.
DR BindingDB; P35405; -.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..469
FT /note="Alpha-2C adrenergic receptor"
FT /id="PRO_0000069104"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 63..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 74..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 100..109
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 176..194
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 217..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 387..407
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 408..427
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 428..448
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 449..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 116
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 199
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT SITE 203
FT /note="Implicated in catechol agonist binding and receptor
FT activation"
FT /evidence="ECO:0000250"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 469 AA; 53223 MW; 6F97D3718CC15C18 CRC64;
MDLQLTTNST DSGDRGGSSN ESLQRQPPSQ YSPAEVAGLA AVVSFLIVFT IVGNVLVVIA
VLTSRALKAP QNLFQVSLAS ADILVATLVM PFSLANELMN YWYFGKVWCV IYLALDVLFC
TSSIVHLCAI SLDRYWSVTQ AVEYNLKRTP RRIKGIIVTV WLISAVISFP PLISLYRDPE
DDLYPQCELN DETWYILSSC IGSFFAPCII MVLVYVRIYR VAKLRTRTLS EKRTVPEGSS
QTENGLSRPP VGAGPSTAAA AAASLRLQAG ENGHYHLHHH HHHLHHHHHH HHHQLRKSAE
LEDIELEESS TSENRRRRRS REEAAARKGS RGFSFSFSST KGGQSAGAGS RLSRASNRSL
EFFSTHRRRK RSSLCRRKVT QAREKRFTFV LAVVMGVFVV CWFPFFFTYS LYGICREACQ
VPETLFKFFF WIGYCNSSLN PVIYTIFNQD FRRSFKHILF KKKKKTSLQ
