ID ADA2A_PIG Reviewed; 450 AA.
AC P18871;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-APR-2013, entry version 102.
DE RecName: Full=Alpha-2A adrenergic receptor;
DE AltName: Full=Alpha-2A adrenoreceptor;
DE Short=Alpha-2A adrenoceptor;
DE Short=Alpha-2AAR;
GN Name=ADRA2A; Synonyms=A2AR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 212-232.
RC TISSUE=Liver;
RX PubMed=2170371;
RA Guyer C.A., Horstman D.A., Wilson A.L., Clark J.D., Kragoe E.J. Jr.,
RA Limbird L.E.;
RT "Cloning, sequencing, and expression of the gene encoding the porcine
RT alpha 2-adrenergic receptor. Allosteric modulation by Na+, H+, and
RT amiloride analogs.";
RL J. Biol. Chem. 265:17307-17317(1990).
RN [2]
RP MUTAGENESIS OF CYS-442.
RX PubMed=8385131;
RA Kennedy M.E., Limbird L.E.;
RT "Mutations of the alpha 2A-adrenergic receptor that eliminate
RT detectable palmitoylation do not perturb receptor-G-protein
RT coupling.";
RL J. Biol. Chem. 268:8003-8011(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 -!- MISCELLANEOUS: Alpha2-adrenergic receptor shows an allosteric
CC modulation by Na(+), H(+) and amiloride analogs.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA2A sub-subfamily.
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DR EMBL; J05652; AAA30984.1; -; Genomic_DNA.
DR PIR; A38316; A38316.
DR RefSeq; NP_999565.1; NM_214400.1.
DR UniGene; Ssc.27594; -.
DR ProteinModelPortal; P18871; -.
DR SMR; P18871; 118-149.
DR Ensembl; ENSSSCT00000011625; ENSSSCP00000011323; ENSSSCG00000010629.
DR GeneID; 399501; -.
DR KEGG; ssc:399501; -.
DR CTD; 150; -.
DR eggNOG; NOG249628; -.
DR GeneTree; ENSGT00700000104198; -.
DR HOGENOM; HOG000239242; -.
DR HOVERGEN; HBG106962; -.
DR KO; K04138; -.
DR OMA; NNEQVTS; -.
DR OrthoDB; EOG4R502W; -.
DR SABIO-RK; P18871; -.
DR BindingDB; P18871; -.
DR ChEMBL; CHEMBL2350; -.
DR ArrayExpress; P18871; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Compara.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; IEA:Compara.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IDA:BHF-UCL.
DR GO; GO:0051379; F:epinephrine binding; IDA:BHF-UCL.
DR GO; GO:0051380; F:norepinephrine binding; IEA:Compara.
DR GO; GO:0071883; P:activation of MAPK activity by adrenergic receptor signaling pathway; IEA:Compara.
DR GO; GO:0032148; P:activation of protein kinase B activity; IEA:Compara.
DR GO; GO:0071881; P:adenylate cyclase-inhibiting adrenergic receptor signaling pathway; IEA:Compara.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Compara.
DR GO; GO:0035625; P:epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway; IEA:Compara.
DR GO; GO:0042596; P:fear response; IEA:Compara.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Compara.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:BHF-UCL.
DR GO; GO:0071878; P:negative regulation of adrenergic receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:BHF-UCL.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Compara.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Compara.
DR GO; GO:0071882; P:phospholipase C-activating adrenergic receptor signaling pathway; IEA:Compara.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Compara.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Compara.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Compara.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Compara.
DR InterPro; IPR001946; Adren_rcpt_A2A.
DR InterPro; IPR002233; Adrnrgc_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00558; ADRENRGCA2AR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Direct protein sequencing;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 450 Alpha-2A adrenergic receptor.
FT /FTId=PRO_0000069082.
FT TOPO_DOM 1 33 Extracellular (By similarity).
FT TRANSMEM 34 59 Helical; Name=1; (By similarity).
FT TOPO_DOM 60 70 Cytoplasmic (By similarity).
FT TRANSMEM 71 96 Helical; Name=2; (By similarity).
FT TOPO_DOM 97 106 Extracellular (By similarity).
FT TRANSMEM 107 129 Helical; Name=3; (By similarity).
FT TOPO_DOM 130 149 Cytoplasmic (By similarity).
FT TRANSMEM 150 173 Helical; Name=4; (By similarity).
FT TOPO_DOM 174 192 Extracellular (By similarity).
FT TRANSMEM 193 217 Helical; Name=5; (By similarity).
FT TOPO_DOM 218 374 Cytoplasmic (By similarity).
FT TRANSMEM 375 399 Helical; Name=6; (By similarity).
FT TOPO_DOM 400 409 Extracellular (By similarity).
FT TRANSMEM 410 430 Helical; Name=7; (By similarity).
FT TOPO_DOM 431 450 Cytoplasmic (By similarity).
FT SITE 113 113 Implicated in ligand binding (By
FT similarity).
FT SITE 200 200 Implicated in catechol agonist binding
FT (By similarity).
FT SITE 204 204 Implicated in catechol agonist binding
FT (By similarity).
FT LIPID 442 442 S-palmitoyl cysteine.
FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential).
FT DISULFID 106 188 By similarity.
FT MUTAGEN 442 442 C->A,S: Loss of palmitoylation.
SQ SEQUENCE 450 AA; 48976 MW; 79D7D5B47372074E CRC64;
MGSLQPEAGN ASWNGTEAPG GGARATPYSL QVTLTLVCLA GLLMLFTVFG NVLVIIAVFT
SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKAWCEIYL ALDVLFCTSS
IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIVTVWVI SAVISFPPLI SIEKKAGGGG
QQPAEPRCEI NDQKWYVISS CIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDAAA
ALPGGAERRP NGLGPERGVG RVGAEAEPLP VQLNGAPGEP APAGPRDADG LDLEESSSSE
HAERPPGPRR SERGPRAKSK ARASQVKPGD SLPRRGPGAP GPGAPATGAG EERGGVAKAS
RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLTAVG CSVPPTLFKF FFWFGYCNSS
LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV
//
