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Database: UniProt
Entry: P18871
LinkDB: P18871
Original site: P18871 
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   29-OCT-2014, entry version 113.
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, AND PALMITOYLATION AT 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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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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   STRING; 9823.ENSSSCP00000011323; -.
DR   BindingDB; P18871; -.
DR   ChEMBL; CHEMBL2350; -.
DR   Ensembl; ENSSSCT00000011625; ENSSSCP00000011323; ENSSSCG00000010629.
DR   GeneID; 399501; -.
DR   KEGG; ssc:399501; -.
DR   CTD; 150; -.
DR   eggNOG; NOG249628; -.
DR   GeneTree; ENSGT00760000118795; -.
DR   HOGENOM; HOG000239242; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; P18871; -.
DR   KO; K04138; -.
DR   OMA; ITVWVIS; -.
DR   OrthoDB; EOG7J9VPT; -.
DR   TreeFam; TF316350; -.
DR   Reactome; REACT_202825; G alpha (i) signalling events.
DR   Reactome; REACT_211638; Adrenoceptors.
DR   Reactome; REACT_215643; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR   Reactome; REACT_221740; G alpha (z) signalling events.
DR   Reactome; REACT_225925; Adrenaline,noradrenaline inhibits insulin secretion.
DR   SABIO-RK; P18871; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0031692; F:alpha-1B adrenergic receptor binding; IPI:BHF-UCL.
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:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0071883; P:activation of MAPK activity by adrenergic receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR   GO; GO:0071881; P:adenylate cyclase-inhibiting adrenergic receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR   GO; GO:0035625; P:epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042596; P:fear response; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
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:0030818; P:negative regulation of cAMP biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR   GO; GO:0071882; P:phospholipase C-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   Gene3D; 1.20.1070.10; -; 2.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR001946; ADRA2A_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248:SF24; PTHR24248:SF24; 1.
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. {ECO:0000250}.
FT   TRANSMEM     34     59       Helical; Name=1. {ECO:0000250}.
FT   TOPO_DOM     60     70       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     71     96       Helical; Name=2. {ECO:0000250}.
FT   TOPO_DOM     97    106       Extracellular. {ECO:0000250}.
FT   TRANSMEM    107    129       Helical; Name=3. {ECO:0000250}.
FT   TOPO_DOM    130    149       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    150    173       Helical; Name=4. {ECO:0000250}.
FT   TOPO_DOM    174    192       Extracellular. {ECO:0000250}.
FT   TRANSMEM    193    217       Helical; Name=5. {ECO:0000250}.
FT   TOPO_DOM    218    374       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    375    399       Helical; Name=6. {ECO:0000250}.
FT   TOPO_DOM    400    409       Extracellular. {ECO:0000250}.
FT   TRANSMEM    410    430       Helical; Name=7. {ECO:0000250}.
FT   TOPO_DOM    431    450       Cytoplasmic. {ECO:0000250}.
FT   SITE        113    113       Implicated in ligand binding.
FT                                {ECO:0000250}.
FT   SITE        200    200       Implicated in catechol agonist binding.
FT                                {ECO:0000250}.
FT   SITE        204    204       Implicated in catechol agonist binding.
FT                                {ECO:0000250}.
FT   LIPID       442    442       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:8385131}.
FT   CARBOHYD     10     10       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     14     14       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    106    188       {ECO:0000255|PROSITE-ProRule:PRU00521}.
FT   MUTAGEN     442    442       C->A,S: Loss of palmitoylation.
FT                                {ECO:0000269|PubMed:8385131}.
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
//
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