ID   ADA2B_HUMAN             Reviewed;         450 AA.
AC   P18089; A2RUS0; Q4TUH9; Q53RF2; Q9BZK0;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 4.
DT   29-MAY-2024, entry version 221.
DE   RecName: Full=Alpha-2B adrenergic receptor;
DE   AltName: Full=Alpha-2 adrenergic receptor subtype C2;
DE   AltName: Full=Alpha-2B adrenoreceptor;
DE            Short=Alpha-2B adrenoceptor;
DE            Short=Alpha-2BAR;
GN   Name=ADRA2B; Synonyms=ADRA2L1, ADRA2RL1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2164221; DOI=10.1073/pnas.87.13.5094;
RA   Lomasney J.W., Lorenz W., Allen L.F., King K., Regan J.W., Yang-Feng T.L.,
RA   Caron M.G., Lefkowitz R.J.;
RT   "Expansion of the alpha 2-adrenergic receptor family: cloning and
RT   characterization of a human alpha 2-adrenergic receptor subtype, the gene
RT   for which is located on chromosome 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5094-5098(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2172775;
RA   Weinshank R.L., Zgombick J.M., Macchi M., Adham N., Lichtblau H.,
RA   Branchek T.A., Hartig P.R.;
RT   "Cloning, expression, and pharmacological characterization of a human alpha
RT   2B-adrenergic receptor.";
RL   Mol. Pharmacol. 38:681-688(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT 301-GLU--GLU-303 DEL.
RX   PubMed=11056163; DOI=10.1074/jbc.m008118200;
RA   Small K.M., Brown K.M., Forbes S.L., Liggett S.B.;
RT   "Polymorphic deletion of three intracellular acidic residues of the alpha
RT   2B-adrenergic receptor decreases G protein-coupled receptor kinase-mediated
RT   phosphorylation and desensitization.";
RL   J. Biol. Chem. 276:4917-4922(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15037199; DOI=10.1016/j.bcp.2003.09.029;
RA   Cayla C., Heinonen P., Viikari L., Schaak S., Snapir A., Bouloumie A.,
RA   Karvonen M.K., Pesonen U., Scheinin M., Paris H.;
RT   "Cloning, characterisation and identification of several polymorphisms in
RT   the promoter region of the human alpha2B-adrenergic receptor gene.";
RL   Biochem. Pharmacol. 67:469-478(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT   "Isolation of complete coding sequence for adrenergic receptor alpha 2B
RT   (ADRA2B).";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-211 AND GLY-379, AND
RP   FRAMESHIFT POLYMORPHISM.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT 301-GLU--GLU-303
RP   DEL.
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-389.
RX   PubMed=2173582; DOI=10.1016/0006-291x(90)90748-c;
RA   Chang A.C., Ho T.F., Chang N.-C.A.;
RT   "In vitro amplification by polymerase chain reaction of a partial gene
RT   encoding the third subtype of alpha-2 adrenergic receptor in humans.";
RL   Biochem. Biophys. Res. Commun. 172:817-823(1990).
RN   [11]
RP   FUNCTION, INTERACTION WITH RAB26, AND SUBCELLULAR LOCATION.
RX   PubMed=23105096; DOI=10.1074/jbc.m112.410936;
RA   Li C., Fan Y., Lan T.H., Lambert N.A., Wu G.;
RT   "Rab26 modulates the cell surface transport of alpha2-adrenergic receptors
RT   from the Golgi.";
RL   J. Biol. Chem. 287:42784-42794(2012).
RN   [12]
RP   INTERACTION WITH PPP1R9B, INVOLVEMENT IN FAME2, VARIANT FAME2
RP   225-HIS--LEU-229 DELINS GLN-PHE-GLY-ARG, AND CHARACTERIZATION OF VARIANT
RP   FAME2 225-HIS--LEU-229 DELINS GLN-PHE-GLY-ARG.
RX   PubMed=24114805; DOI=10.1002/ana.24028;
RA   De Fusco M., Vago R., Striano P., Di Bonaventura C., Zara F., Mei D.,
RA   Kim M.S., Muallem S., Chen Y., Wang Q., Guerrini R., Casari G.;
RT   "The alpha2B-adrenergic receptor is mutant in cortical myoclonus and
RT   epilepsy.";
RL   Ann. Neurol. 75:77-87(2014).
RN   [13]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH GGA1 AND GGA2.
RX   PubMed=27901063; DOI=10.1038/srep37921;
RA   Zhang M., Huang W., Gao J., Terry A.V., Wu G.;
RT   "Regulation of alpha2B-Adrenergic Receptor Cell Surface Transport by GGA1
RT   and GGA2.";
RL   Sci. Rep. 6:37921-37921(2016).
RN   [14]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH GGA3.
RX   PubMed=26811329; DOI=10.1128/mcb.00009-16;
RA   Zhang M., Davis J.E., Li C., Gao J., Huang W., Lambert N.A.,
RA   Terry A.V. Jr., Wu G.;
RT   "GGA3 Interacts with a G Protein-Coupled Receptor and Modulates Its Cell
RT   Surface Export.";
RL   Mol. Cell. Biol. 36:1152-1163(2016).
CC   -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC       induced inhibition of adenylate cyclase through the action of G
CC       proteins. The rank order of potency for agonists of this receptor is
CC       clonidine > norepinephrine > epinephrine = oxymetazoline > dopamine >
CC       p-tyramine = phenylephrine > serotonin > p-synephrine / p-octopamine.
CC       For antagonists, the rank order is yohimbine > chlorpromazine >
CC       phentolamine > mianserine > spiperone > prazosin > alprenolol >
CC       propanolol > pindolol. {ECO:0000269|PubMed:23105096}.
CC   -!- SUBUNIT: Interacts with RAB26 (PubMed:23105096). Interacts with PPP1R9B
CC       (PubMed:24114805). Interacts with GGA1, GGA2 and GGA3 (PubMed:26811329,
CC       PubMed:27901063). {ECO:0000269|PubMed:23105096,
CC       ECO:0000269|PubMed:24114805, ECO:0000269|PubMed:26811329,
CC       ECO:0000269|PubMed:27901063}.
CC   -!- INTERACTION:
CC       P18089; Q9ULW5: RAB26; NbExp=4; IntAct=EBI-9077302, EBI-958239;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23105096,
CC       ECO:0000269|PubMed:26811329, ECO:0000269|PubMed:27901063}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:23105096}. Note=Interaction with
CC       RAB26, GGA1, GGA2 and GGA3 mediates transport from the Golgi to the
CC       cell membrane. {ECO:0000269|PubMed:23105096,
CC       ECO:0000269|PubMed:26811329, ECO:0000269|PubMed:27901063}.
CC   -!- POLYMORPHISM: A rare polymorphic frameshift in position 451 produces a
CC       protein of 545 residues. {ECO:0000269|Ref.6}.
CC   -!- DISEASE: Epilepsy, familial adult myoclonic, 2 (FAME2) [MIM:607876]: A
CC       form of familial myoclonic epilepsy, a neurologic disorder
CC       characterized by cortical hand tremors, myoclonic jerks and occasional
CC       generalized or focal seizures with a non-progressive or very slowly
CC       progressive disease course. Usually, myoclonic tremor is the presenting
CC       symptom, characterized by tremulous finger movements and myoclonic
CC       jerks of the limbs increased by action and posture. In a minority of
CC       patients, seizures are the presenting symptom. Some patients exhibit
CC       mild cognitive impairment. FAME2 inheritance is autosomal dominant.
CC       {ECO:0000269|PubMed:24114805}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRA2B sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/adra2b/";
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DR   EMBL; M34041; AAA51666.1; -; Genomic_DNA.
DR   EMBL; AF316895; AAK01635.1; -; Genomic_DNA.
DR   EMBL; AF005900; AAB62558.1; -; Genomic_DNA.
DR   EMBL; AY548167; AAS55646.1; -; Genomic_DNA.
DR   EMBL; DQ057076; AAY43127.1; -; Genomic_DNA.
DR   EMBL; EU332847; ABY87536.1; -; Genomic_DNA.
DR   EMBL; AC092603; AAX93218.1; -; Genomic_DNA.
DR   EMBL; KF573706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471207; EAW71390.1; -; Genomic_DNA.
DR   EMBL; BC133021; AAI33022.1; -; mRNA.
DR   EMBL; BC136537; AAI36538.1; -; mRNA.
DR   EMBL; M38742; AAA62823.1; -; Genomic_DNA.
DR   CCDS; CCDS56129.1; -.
DR   PIR; A37223; A37223.
DR   RefSeq; NP_000673.2; NM_000682.6.
DR   PDB; 6K41; EM; 2.90 A; R=9-450.
DR   PDB; 6K42; EM; 4.10 A; R=7-450.
DR   PDBsum; 6K41; -.
DR   PDBsum; 6K42; -.
DR   AlphaFoldDB; P18089; -.
DR   EMDB; EMD-9911; -.
DR   SMR; P18089; -.
DR   BioGRID; 106660; 7.
DR   DIP; DIP-61453N; -.
DR   IntAct; P18089; 5.
DR   STRING; 9606.ENSP00000480573; -.
DR   BindingDB; P18089; -.
DR   ChEMBL; CHEMBL1942; -.
DR   DrugBank; DB00543; Amoxapine.
DR   DrugBank; DB00182; Amphetamine.
DR   DrugBank; DB00714; Apomorphine.
DR   DrugBank; DB00964; Apraclonidine.
DR   DrugBank; DB09229; Aranidipine.
DR   DrugBank; DB01238; Aripiprazole.
DR   DrugBank; DB14185; Aripiprazole lauroxil.
DR   DrugBank; DB06216; Asenapine.
DR   DrugBank; DB00217; Bethanidine.
DR   DrugBank; DB00484; Brimonidine.
DR   DrugBank; DB01200; Bromocriptine.
DR   DrugBank; DB00248; Cabergoline.
DR   DrugBank; DB01136; Carvedilol.
DR   DrugBank; DB04846; Celiprolol.
DR   DrugBank; DB00477; Chlorpromazine.
DR   DrugBank; DB09202; Cirazoline.
DR   DrugBank; DB00575; Clonidine.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB01151; Desipramine.
DR   DrugBank; DB01576; Dextroamphetamine.
DR   DrugBank; DB11273; Dihydroergocornine.
DR   DrugBank; DB13345; Dihydroergocristine.
DR   DrugBank; DB00320; Dihydroergotamine.
DR   DrugBank; DB11278; DL-Methylephedrine.
DR   DrugBank; DB09167; Dosulepin.
DR   DrugBank; DB04855; Dronedarone.
DR   DrugBank; DB06262; Droxidopa.
DR   DrugBank; DB01363; Ephedra sinica root.
DR   DrugBank; DB05492; Epicept NP-1.
DR   DrugBank; DB00668; Epinephrine.
DR   DrugBank; DB01049; Ergoloid mesylate.
DR   DrugBank; DB01175; Escitalopram.
DR   DrugBank; DB06678; Esmirtazapine.
DR   DrugBank; DB00292; Etomidate.
DR   DrugBank; DB09194; Etoperidone.
DR   DrugBank; DB00800; Fenoldopam.
DR   DrugBank; DB00629; Guanabenz.
DR   DrugBank; DB01018; Guanfacine.
DR   DrugBank; DB00502; Haloperidol.
DR   DrugBank; DB11577; Indigotindisulfonic acid.
DR   DrugBank; DB06707; Levonordefrin.
DR   DrugBank; DB00589; Lisuride.
DR   DrugBank; DB09195; Lorpiprazole.
DR   DrugBank; DB00408; Loxapine.
DR   DrugBank; DB00934; Maprotiline.
DR   DrugBank; DB01365; Mephentermine.
DR   DrugBank; DB01577; Metamfetamine.
DR   DrugBank; DB01403; Methotrimeprazine.
DR   DrugBank; DB06148; Mianserin.
DR   DrugBank; DB09205; Moxisylyte.
DR   DrugBank; DB00368; Norepinephrine.
DR   DrugBank; DB00540; Nortriptyline.
DR   DrugBank; DB06229; Ocaperidone.
DR   DrugBank; DB05461; OPC-28326.
DR   DrugBank; DB00935; Oxymetazoline.
DR   DrugBank; DB01267; Paliperidone.
DR   DrugBank; DB00715; Paroxetine.
DR   DrugBank; DB01186; Pergolide.
DR   DrugBank; DB00925; Phenoxybenzamine.
DR   DrugBank; DB00692; Phentolamine.
DR   DrugBank; DB00397; Phenylpropanolamine.
DR   DrugBank; DB06153; Pizotifen.
DR   DrugBank; DB00457; Prazosin.
DR   DrugBank; DB00433; Prochlorperazine.
DR   DrugBank; DB01069; Promethazine.
DR   DrugBank; DB01224; Quetiapine.
DR   DrugBank; DB11124; Racepinephrine.
DR   DrugBank; DB00734; Risperidone.
DR   DrugBank; DB00268; Ropinirole.
DR   DrugBank; DB05271; Rotigotine.
DR   DrugBank; DB09304; Setiptiline.
DR   DrugBank; DB06764; Tetryzoline.
DR   DrugBank; DB13025; Tiapride.
DR   DrugBank; DB00697; Tizanidine.
DR   DrugBank; DB00797; Tolazoline.
DR   DrugBank; DB00193; Tramadol.
DR   DrugBank; DB00726; Trimipramine.
DR   DrugBank; DB11477; Xylazine.
DR   DrugBank; DB06694; Xylometazoline.
DR   DrugBank; DB01392; Yohimbine.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugCentral; P18089; -.
DR   GuidetoPHARMACOLOGY; 26; -.
DR   PhosphoSitePlus; P18089; -.
DR   BioMuta; ADRA2B; -.
DR   DMDM; 27151763; -.
DR   MassIVE; P18089; -.
DR   PaxDb; 9606-ENSP00000480573; -.
DR   PeptideAtlas; P18089; -.
DR   ProteomicsDB; 53548; -.
DR   Antibodypedia; 72874; 149 antibodies from 26 providers.
DR   DNASU; 151; -.
DR   Ensembl; ENST00000620793.2; ENSP00000480573.1; ENSG00000274286.2.
DR   GeneID; 151; -.
DR   KEGG; hsa:151; -.
DR   MANE-Select; ENST00000620793.2; ENSP00000480573.1; NM_000682.7; NP_000673.2.
DR   UCSC; uc032nvj.2; human.
DR   AGR; HGNC:282; -.
DR   CTD; 151; -.
DR   DisGeNET; 151; -.
DR   GeneCards; ADRA2B; -.
DR   HGNC; HGNC:282; ADRA2B.
DR   HPA; ENSG00000274286; Low tissue specificity.
DR   MalaCards; ADRA2B; -.
DR   MIM; 104260; gene.
DR   MIM; 607876; phenotype.
DR   neXtProt; NX_P18089; -.
DR   OpenTargets; ENSG00000274286; -.
DR   Orphanet; 86814; Benign adult familial myoclonic epilepsy.
DR   PharmGKB; PA36; -.
DR   VEuPathDB; HostDB:ENSG00000274286; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000161915; -.
DR   InParanoid; P18089; -.
DR   OMA; CEPQAVP; -.
DR   OrthoDB; 3087922at2759; -.
DR   PhylomeDB; P18089; -.
DR   TreeFam; TF316350; -.
DR   PathwayCommons; P18089; -.
DR   Reactome; R-HSA-390696; Adrenoceptors.
DR   Reactome; R-HSA-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-418597; G alpha (z) signalling events.
DR   SignaLink; P18089; -.
DR   SIGNOR; P18089; -.
DR   BioGRID-ORCS; 151; 11 hits in 1156 CRISPR screens.
DR   ChiTaRS; ADRA2B; human.
DR   GeneWiki; Alpha-2B_adrenergic_receptor; -.
DR   GenomeRNAi; 151; -.
DR   Pharos; P18089; Tclin.
DR   PRO; PR:P18089; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P18089; Protein.
DR   Bgee; ENSG00000274286; Expressed in apex of heart and 97 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0071875; P:adrenergic receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0032811; P:negative regulation of epinephrine secretion; NAS:BHF-UCL.
DR   GO; GO:0010700; P:negative regulation of norepinephrine secretion; TAS:BHF-UCL.
DR   GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR   GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:BHF-UCL.
DR   GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0035624; P:receptor transactivation; IDA:BHF-UCL.
DR   GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IEA:Ensembl.
DR   CDD; cd15321; 7tmA_alpha2B_AR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000207; ADRA2B_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF130; ALPHA-2B ADRENERGIC RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00559; ADRENRGCA2BR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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   3D-structure; Cell membrane; Disulfide bond; Epilepsy;
KW   G-protein coupled receptor; Lipoprotein; Membrane; Palmitate; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..450
FT                   /note="Alpha-2B adrenergic receptor"
FT                   /id="PRO_0000069094"
FT   TOPO_DOM        1..12
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        13..38
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        39..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        49..69
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        70..86
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        108..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        150..172
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        173..193
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        194..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        369..389
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        390..405
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        406..426
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        427..450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          204..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..312
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            92
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            176
FT                   /note="Implicated in catechol agonist binding"
FT                   /evidence="ECO:0000250"
FT   SITE            180
FT                   /note="Implicated in catechol agonist binding"
FT                   /evidence="ECO:0000250"
FT   LIPID           442
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        85..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         211
FT                   /note="G -> A (in dbSNP:rs9333568)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_025099"
FT   VARIANT         225..229
FT                   /note="HGGAL -> QFGR (in FAME2; gain of function; decreases
FT                   interaction with PPP1R9B upon activation by
FT                   neurotransmitter)"
FT                   /evidence="ECO:0000269|PubMed:24114805"
FT                   /id="VAR_073953"
FT   VARIANT         301..303
FT                   /note="Missing (found with a frequency of 0.31 in
FT                   Caucasians and 0.12 in African-Americans; exhibits impaired
FT                   phosphorylation and desensitization by G protein-coupled
FT                   receptor kinases; does not affect ligand-binding)"
FT                   /evidence="ECO:0000269|PubMed:11056163,
FT                   ECO:0000269|PubMed:15815621"
FT                   /id="VAR_070775"
FT   VARIANT         376
FT                   /note="V -> I (in dbSNP:rs1431850417)"
FT                   /id="VAR_033462"
FT   VARIANT         379
FT                   /note="V -> G (in dbSNP:rs527655811)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_025100"
FT   VARIANT         379
FT                   /note="V -> I (in dbSNP:rs29000569)"
FT                   /id="VAR_033463"
FT   CONFLICT        362..363
FT                   /note="QL -> HV (in Ref. 1; AAA51666 and 2; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   HELIX           12..38
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           49..73
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           86..115
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           117..121
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           126..144
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           171..180
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           182..202
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           363..392
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           407..427
FT                   /evidence="ECO:0007829|PDB:6K41"
FT   HELIX           431..441
FT                   /evidence="ECO:0007829|PDB:6K41"
SQ   SEQUENCE   450 AA;  49954 MW;  06E43857152A68ED CRC64;
     MDHQDPYSVQ ATAAIAAAIT FLILFTIFGN ALVILAVLTS RSLRAPQNLF LVSLAAADIL
     VATLIIPFSL ANELLGYWYF RRTWCEVYLA LDVLFCTSSI VHLCAISLDR YWAVSRALEY
     NSKRTPRRIK CIILTVWLIA AVISLPPLIY KGDQGPQPRG RPQCKLNQEA WYILASSIGS
     FFAPCLIMIL VYLRIYLIAK RSNRRGPRAK GGPGQGESKQ PRPDHGGALA SAKLPALASV
     ASAREVNGHS KSTGEKEEGE TPEDTGTRAL PPSWAALPNS GQGQKEGVCG ASPEDEAEEE
     EEEEEEEEEC EPQAVPVSPA SACSPPLQQP QGSRVLATLR GQVLLGRGVG AIGGQWWRRR
     AQLTREKRFT FVLAVVIGVF VLCWFPFFFS YSLGAICPKH CKVPHGLFQF FFWIGYCNSS
     LNPVIYTIFN QDFRRAFRRI LCRPWTQTAW
//