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Alpha-2A adrenergic receptor (Alpha-2 adrenergic receptor subtype C10) (Alpha-2A adrenoreceptor) (Alpha-2A adrenoceptor) (Alpha-2AAR)

 ADA2A_HUMAN             Reviewed;         450 AA.
P08913; B0LPF6; Q2I8G2; Q2XN99; Q86TH8; Q9BZK1;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 3.
20-JUN-2018, entry version 202.
RecName: Full=Alpha-2A adrenergic receptor;
AltName: Full=Alpha-2 adrenergic receptor subtype C10;
AltName: Full=Alpha-2A adrenoreceptor;
Short=Alpha-2A adrenoceptor;
Short=Alpha-2AAR;
Name=ADRA2A; Synonyms=ADRA2R, ADRAR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Platelet;
PubMed=2823383; DOI=10.1126/science.2823383;
Kobilka B.K., Matsui H., Kobilka T.S., Yang-Feng T.L., Francke U.,
Caron M.G., Lefkowitz R.J., Regan J.W.;
"Cloning, sequencing, and expression of the gene coding for the human
platelet alpha 2-adrenergic receptor.";
Science 238:650-656(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2568356;
Fraser C.M., Arakawa S., McCombie W.R., Venter J.C.;
"Cloning, sequence analysis, and permanent expression of a human alpha
2-adrenergic receptor in Chinese hamster ovary cells. Evidence for
independent pathways of receptor coupling to adenylate cyclase
attenuation and activation.";
J. Biol. Chem. 264:11754-11761(1989).
[3]
SEQUENCE REVISION TO 333-365.
PubMed=2170371;
Guyer C.A., Horstman D.A., Wilson A.L., Clark J.D., Kragoe E.J. Jr.,
Limbird L.E.;
"Cloning, sequencing, and expression of the gene encoding the porcine
alpha 2-adrenergic receptor. Allosteric modulation by Na+, H+, and
amiloride analogs.";
J. Biol. Chem. 265:17307-17317(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-251.
PubMed=10948191; DOI=10.1074/jbc.M004550200;
Small K.M., Forbes S.L., Brown K.M., Liggett S.B.;
"An Asn to Lys polymorphism in the third intracellular loop of the
human alpha 2A-adrenergic receptor imparts enhanced agonist-promoted
Gi coupling.";
J. Biol. Chem. 275:38518-38523(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-251.
PubMed=16567612; DOI=10.1073/pnas.0601345103;
Small K.M., Brown K.M., Seman C.A., Theiss C.T., Liggett S.B.;
"Complex haplotypes derived from noncoding polymorphisms of the
intronless alpha-2A-adrenergic gene diversify receptor expression.";
Proc. Natl. Acad. Sci. U.S.A. 103:5472-5477(2006).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
Mao Z.-M., Tang K., Li B.-M., Jing N.-H.;
"Cloning and expression of human alpha-2A adrenergic receptor in SY5Y
cells.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Castellano M., Giacche' M., Rossi F., Rivadossi F., Perani C.,
Beschi M., Agabiti Rosei E.;
"A search for genetic variability in the human alpha-2 adrenergic
receptor on chromosome 10.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Liu L., Yuan L.;
"Human alpha-2A adrenergic receptor gene and the genotype of -1296
nucleotide and motionsickness.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-251.
SeattleSNPs variation discovery resource;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-209.
PubMed=1849485; DOI=10.1016/0014-5793(91)80301-I;
Chhajlani V., Rangel N., Uhlen S., Wikberg J.E.S.;
"Identification of an additional gene belonging to the alpha 2
adrenergic receptor family in the human genome by PCR.";
FEBS Lett. 280:241-244(1991).
[14]
MUTAGENESIS OF PHE-412.
PubMed=1678390;
Suryanarayana S., Daunt D.A., von Zastrow M., Kobilka B.K.;
"A point mutation in the seventh hydrophobic domain of the alpha 2
adrenergic receptor increases its affinity for a family of beta
receptor antagonists.";
J. Biol. Chem. 266:15488-15492(1991).
[15]
MUTAGENESIS OF ASPARTIC ACID AND SERINE RESIDUES.
PubMed=1678850;
Wang C.-D., Buck M.A., Fraser C.M.;
"Site-directed mutagenesis of alpha 2a-adrenergic receptors:
Identification of amino acids involved in ligand binding and receptor
activation by agonists.";
Mol. Pharmacol. 40:168-179(1991).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23105096; DOI=10.1074/jbc.M112.410936;
Li C., Fan Y., Lan T.H., Lambert N.A., Wu G.;
"Rab26 modulates the cell surface transport of alpha2-adrenergic
receptors from the Golgi.";
J. Biol. Chem. 287:42784-42794(2012).
[17]
STRUCTURE BY NMR OF 118-149, AND PROBABLE MEMBRANE TOPOLOGY.
PubMed=11888275; DOI=10.1021/bi015811+;
Chung D.A., Zuiderweg E.R.P., Fowler C.B., Soyer O.S., Mosberg H.I.,
Neubig R.R.;
"NMR structure of the second intracellular loop of the alpha 2A
adrenergic receptor: evidence for a novel cytoplasmic helix.";
Biochemistry 41:3596-3604(2002).
-!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
induced inhibition of adenylate cyclase through the action of G
proteins. The rank order of potency for agonists of this receptor
is oxymetazoline > clonidine > epinephrine > norepinephrine >
phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin =
p-octopamine. For antagonists, the rank order is yohimbine >
phentolamine = mianserine > chlorpromazine = spiperone = prazosin
> propanolol > alprenolol = pindolol.
{ECO:0000269|PubMed:23105096}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23105096};
Multi-pass membrane protein {ECO:0000269|PubMed:23105096}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Adrenergic receptor subfamily. ADRA2A sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/adra2a/";
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EMBL; M18415; AAA51664.1; -; Genomic_DNA.
EMBL; M23533; AAA51665.1; -; Genomic_DNA.
EMBL; AF281308; AAF91441.1; -; Genomic_DNA.
EMBL; AF316894; AAK01634.1; -; Genomic_DNA.
EMBL; DQ149926; AAZ73101.1; -; Genomic_DNA.
EMBL; AF284095; AAK26743.1; -; mRNA.
EMBL; AF262016; AAG00447.2; -; Genomic_DNA.
EMBL; AY032736; AAK51162.1; -; Genomic_DNA.
EMBL; DQ285607; ABB72683.1; -; Genomic_DNA.
EMBL; EU332846; ABY87535.1; -; Genomic_DNA.
EMBL; AL158163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035047; AAH35047.1; -; mRNA.
EMBL; BC050414; AAH50414.4; -; mRNA.
PIR; A34169; A34169.
RefSeq; NP_000672.3; NM_000681.3.
UniGene; Hs.249159; -.
PDB; 1HLL; NMR; -; A=118-149.
PDB; 1HO9; NMR; -; A=118-149.
PDB; 1HOD; NMR; -; A=118-149.
PDB; 1HOF; NMR; -; A=118-149.
PDBsum; 1HLL; -.
PDBsum; 1HO9; -.
PDBsum; 1HOD; -.
PDBsum; 1HOF; -.
ProteinModelPortal; P08913; -.
SMR; P08913; -.
BioGrid; 106659; 8.
CORUM; P08913; -.
DIP; DIP-61452N; -.
IntAct; P08913; 6.
STRING; 9606.ENSP00000280155; -.
BindingDB; P08913; -.
ChEMBL; CHEMBL1867; -.
DrugBank; DB01472; 4-Methoxyamphetamine.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00543; Amoxapine.
DrugBank; DB00182; Amphetamine.
DrugBank; DB00714; Apomorphine.
DrugBank; DB00964; Apraclonidine.
DrugBank; DB01238; Aripiprazole.
DrugBank; DB06216; Asenapine.
DrugBank; DB00865; Benzphetamine.
DrugBank; DB00217; Bethanidine.
DrugBank; DB00484; Brimonidine.
DrugBank; DB01200; Bromocriptine.
DrugBank; DB00248; Cabergoline.
DrugBank; DB01136; Carvedilol.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB09202; Cirazoline.
DrugBank; DB00575; Clonidine.
DrugBank; DB00363; Clozapine.
DrugBank; DB01151; Desipramine.
DrugBank; DB00633; Dexmedetomidine.
DrugBank; DB00320; Dihydroergotamine.
DrugBank; DB00449; Dipivefrin.
DrugBank; DB01142; Doxepin.
DrugBank; DB04855; Dronedarone.
DrugBank; DB06262; Droxidopa.
DrugBank; DB01363; Ephedra.
DrugBank; DB05492; Epicept NP-1.
DrugBank; DB00751; Epinastine.
DrugBank; DB00668; Epinephrine.
DrugBank; DB01049; Ergoloid mesylate.
DrugBank; DB00696; Ergotamine.
DrugBank; DB06678; Esmirtazapine.
DrugBank; DB00800; Fenoldopam.
DrugBank; DB06623; Flupirtine.
DrugBank; DB00629; Guanabenz.
DrugBank; DB01018; Guanfacine.
DrugBank; DB06707; Levonordefrin.
DrugBank; DB00589; Lisuride.
DrugBank; DB04948; Lofexidine.
DrugBank; DB00408; Loxapine.
DrugBank; DB08815; Lurasidone.
DrugBank; DB00934; Maprotiline.
DrugBank; DB01365; Mephentermine.
DrugBank; DB01577; Methamphetamine.
DrugBank; DB01403; Methotrimeprazine.
DrugBank; DB00968; Methyldopa.
DrugBank; DB06148; Mianserin.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB06711; Naphazoline.
DrugBank; DB01149; Nefazodone.
DrugBank; DB00368; Norepinephrine.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB00334; Olanzapine.
DrugBank; DB00935; Oxymetazoline.
DrugBank; DB01267; Paliperidone.
DrugBank; DB01186; Pergolide.
DrugBank; DB00925; Phenoxybenzamine.
DrugBank; DB00692; Phentolamine.
DrugBank; DB00397; Phenylpropanolamine.
DrugBank; DB00413; Pramipexole.
DrugBank; DB00457; Prazosin.
DrugBank; DB01608; Propericiazine.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB01224; Quetiapine.
DrugBank; DB00734; Risperidone.
DrugBank; DB00268; Ropinirole.
DrugBank; DB13025; Tiapride.
DrugBank; DB00697; Tizanidine.
DrugBank; DB00797; Tolazoline.
DrugBank; DB00656; Trazodone.
DrugBank; DB00726; Trimipramine.
DrugBank; DB06694; Xylometazoline.
DrugBank; DB01392; Yohimbine.
DrugBank; DB00246; Ziprasidone.
DrugBank; DB01624; Zuclopenthixol.
GuidetoPHARMACOLOGY; 25; -.
iPTMnet; P08913; -.
PhosphoSitePlus; P08913; -.
BioMuta; ADRA2A; -.
DMDM; 1351829; -.
PaxDb; P08913; -.
PeptideAtlas; P08913; -.
PRIDE; P08913; -.
ProteomicsDB; 52176; -.
DNASU; 150; -.
Ensembl; ENST00000280155; ENSP00000280155; ENSG00000150594.
GeneID; 150; -.
KEGG; hsa:150; -.
UCSC; uc001kzo.4; human.
CTD; 150; -.
DisGeNET; 150; -.
EuPathDB; HostDB:ENSG00000150594.6; -.
GeneCards; ADRA2A; -.
H-InvDB; HIX0190540; -.
HGNC; HGNC:281; ADRA2A.
MIM; 104210; gene.
neXtProt; NX_P08913; -.
PharmGKB; PA35; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
HOGENOM; HOG000239242; -.
HOVERGEN; HBG106962; -.
InParanoid; P08913; -.
KO; K04138; -.
OrthoDB; EOG091G06VI; -.
PhylomeDB; P08913; -.
TreeFam; TF316350; -.
Reactome; R-HSA-390696; Adrenoceptors.
Reactome; R-HSA-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-5683826; Surfactant metabolism.
SignaLink; P08913; -.
SIGNOR; P08913; -.
EvolutionaryTrace; P08913; -.
GeneWiki; Alpha-2A_adrenergic_receptor; -.
GenomeRNAi; 150; -.
PRO; PR:P08913; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000150594; -.
CleanEx; HS_ADRA2A; -.
Genevisible; P08913; HS.
GO; GO:0016323; C:basolateral plasma membrane; TAS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0031692; F:alpha-1B adrenergic receptor binding; ISS:BHF-UCL.
GO; GO:0031696; F:alpha-2C adrenergic receptor binding; IPI:BHF-UCL.
GO; GO:0004938; F:alpha2-adrenergic receptor activity; IDA:BHF-UCL.
GO; GO:0051379; F:epinephrine binding; IDA:BHF-UCL.
GO; GO:0032795; F:heterotrimeric G-protein binding; IDA:BHF-UCL.
GO; GO:0051380; F:norepinephrine binding; IDA:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0031996; F:thioesterase binding; IPI:BHF-UCL.
GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
GO; GO:0032147; P:activation of protein kinase activity; IDA:BHF-UCL.
GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0071881; P:adenylate cyclase-inhibiting adrenergic receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0071875; P:adrenergic receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0032870; P:cellular response to hormone stimulus; IGI:BHF-UCL.
GO; GO:0035625; P:epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
GO; GO:0050892; P:intestinal absorption; TAS:BHF-UCL.
GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0051926; P:negative regulation of calcium ion transport; ISS:BHF-UCL.
GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IC:BHF-UCL.
GO; GO:0032811; P:negative regulation of epinephrine secretion; NAS:BHF-UCL.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:BHF-UCL.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IGI:BHF-UCL.
GO; GO:0010700; P:negative regulation of norepinephrine secretion; TAS:BHF-UCL.
GO; GO:0071882; P:phospholipase C-activating adrenergic receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0030168; P:platelet activation; IEA:InterPro.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0001819; P:positive regulation of cytokine production; IDA:BHF-UCL.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0043268; P:positive regulation of potassium ion transport; ISS:BHF-UCL.
GO; GO:0090303; P:positive regulation of wound healing; IMP:BHF-UCL.
GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR002233; ADR_fam.
InterPro; IPR001946; ADRA2A_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01103; ADRENERGICR.
PRINTS; PR00558; ADRENRGCA2AR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Lipoprotein; Membrane; Methylation; Palmitate;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 450 Alpha-2A adrenergic receptor.
/FTId=PRO_0000069080.
TOPO_DOM 1 33 Extracellular. {ECO:0000250}.
TRANSMEM 34 59 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 60 70 Cytoplasmic. {ECO:0000250}.
TRANSMEM 71 96 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 97 106 Extracellular. {ECO:0000250}.
TRANSMEM 107 129 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 130 151 Cytoplasmic. {ECO:0000250}.
TRANSMEM 152 172 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 173 194 Extracellular. {ECO:0000250}.
TRANSMEM 195 217 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 218 374 Cytoplasmic. {ECO:0000250}.
TRANSMEM 375 395 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 396 409 Extracellular. {ECO:0000250}.
TRANSMEM 410 429 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 430 450 Cytoplasmic. {ECO:0000250}.
SITE 113 113 Implicated in ligand binding.
SITE 200 200 Implicated in catechol agonist binding
and receptor activation.
SITE 204 204 Implicated in catechol agonist binding
and receptor activation.
MOD_RES 331 331 Phosphoserine.
{ECO:0000250|UniProtKB:P22909}.
MOD_RES 353 353 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q01338}.
LIPID 442 442 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 10 10 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 14 14 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 106 188 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 251 251 N -> K (rare polymorphism; frequency in
Caucasians 0.004 and in African-Americans
0.05; 40% increase in agonist-promoted Gi
coupling; dbSNP:rs1800035).
{ECO:0000269|PubMed:10948191,
ECO:0000269|PubMed:16567612,
ECO:0000269|Ref.9}.
/FTId=VAR_014957.
VARIANT 401 401 C -> S (in dbSNP:rs35658213).
/FTId=VAR_055908.
MUTAGEN 79 79 D->N: No change in binding affinity.
eliminates guanine nucleotide-sensitive
agonist binding.
{ECO:0000269|PubMed:1678850}.
MUTAGEN 113 113 D->N: No binding to yohimbine. Increase
in adenylate cyclase activity.
{ECO:0000269|PubMed:1678850}.
MUTAGEN 130 130 D->N: Lower affinity for agonists.
Eliminates guanine nucleotide-sensitive
agonist binding.
{ECO:0000269|PubMed:1678850}.
MUTAGEN 200 200 S->A: Lower affinity for agonists. No
change in guanine nucleotide-sensitive
agonist binding.
{ECO:0000269|PubMed:1678850}.
MUTAGEN 204 204 S->A: Lower affinity for agonists.
Reduced guanine nucleotide-sensitive
agonist binding.
{ECO:0000269|PubMed:1678850}.
MUTAGEN 412 412 F->N: 350-fold reduced affinity for
alpha-2 antagonist yohimbine, 3000-fold
increase for beta-antagonist alprenolol.
{ECO:0000269|PubMed:1678390}.
CONFLICT 104 104 A -> T (in Ref. 1; AAA51664).
{ECO:0000305}.
CONFLICT 124 124 L -> P (in Ref. 13). {ECO:0000305}.
CONFLICT 157 157 V -> C (in Ref. 1; AAA51664).
{ECO:0000305}.
CONFLICT 333 365 PRRGPGATGIGTPAAGPGEERVGAAKASRWRGR -> RGAG
RGRRGSGRRLQGRGRSASGLPRRRAGAGG (in Ref. 1;
AAA51664 and 2; AAA51665). {ECO:0000305}.
CONFLICT 368 368 R -> L (in Ref. 1; AAA51664).
{ECO:0000305}.
HELIX 119 128 {ECO:0000244|PDB:1HLL}.
HELIX 130 139 {ECO:0000244|PDB:1HLL}.
HELIX 140 142 {ECO:0000244|PDB:1HLL}.
SEQUENCE 450 AA; 48957 MW; A703CF262F04E8AC CRC64;
MGSLQPDAGN ASWNGTEAPG GGARATPYSL QVTLTLVCLA GLLMLLTVFG NVLVIIAVFT
SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKAWCEIYL ALDVLFCTSS
IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIITVWVI SAVISFPPLI SIEKKGGGGG
PQPAEPRCEI NDQKWYVISS CIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDAVA
APPGGTERRP NGLGPERSAG PGGAEAEPLP TQLNGAPGEP APAGPRDTDA LDLEESSSSD
HAERPPGPRR PERGPRGKGK ARASQVKPGD SLPRRGPGAT GIGTPAAGPG EERVGAAKAS
RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLTAVG CSVPRTLFKF FFWFGYCNSS
LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV


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