ADA2B_HUMAN
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 03-AUG-2022, entry version 211.
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:27901063,
CC PubMed:26811329). {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 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; 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 PaxDb; P18089; -.
DR PeptideAtlas; P18089; -.
DR PRIDE; P18089; -.
DR ProteomicsDB; 53548; -.
DR Antibodypedia; 72874; 131 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 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; 737211at2759; -.
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; 10 hits in 1073 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 tissues.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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 InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000207; ADRA2B_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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 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
