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UniProtKB/Swiss-Prot entry P18089


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADA2B_HUMAN
Primary accession number P18089
Secondary accession numbers Q4TUH9 Q53RF2 Q9BZK0
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on December 13, 2002 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Alpha-2B adrenergic receptor
Synonyms Alpha-2B adrenoreceptor
Alpha-2B adrenoceptor
Alpha-2 adrenergic receptor subtype C2
Gene name
Name: ADRA2B
Synonyms: ADRA2L1, ADRA2RL1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1073/pnas.87.13.5094; PubMed=2164221 [NCBI, ExPASy, EBI, Israel, Japan]
Lomasney J.W., Lorenz W., Allen L.F., King K., Regan J.W., Yang-Feng T.L., Caron M.G., Lefkowitz R.J.;
"Expansion of the alpha 2-adrenergic receptor family: cloning and characterization of a human alpha 2-adrenergic receptor subtype, the gene for which is located on chromosome 2.";
Proc. Natl. Acad. Sci. U.S.A. 87:5094-5098(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2172775 [NCBI, ExPASy, EBI, Israel, Japan]
Weinshank R.L., Zgombick J.M., Macchi M., Adham N., Lichtblau H., Branchek T.A., Hartig P.R.;
"Cloning, expression, and pharmacological characterization of a human alpha 2B-adrenergic receptor.";
Mol. Pharmacol. 38:681-688(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT 301-GLU--GLU-303 DEL.
DOI=10.1074/jbc.M008118200; PubMed=11056163 [NCBI, ExPASy, EBI, Israel, Japan]
Small K.M., Brown K.M., Forbes S.L., Liggett S.B.;
"Polymorphic deletion of three intracellular acidic residues of the alpha 2B-adrenergic receptor decreases G protein-coupled receptor kinase-mediated phosphorylation and desensitization.";
J. Biol. Chem. 276:4917-4922(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/j.bcp.2003.09.029; PubMed=15037199 [NCBI, ExPASy, EBI, Israel, Japan]
Cayla C., Heinonen P., Viikari L., Schaak S., Snapir A., Bouloumie A., Karvonen M.K., Pesonen U., Scheinin M., Paris H.;
"Cloning, characterisation and identification of several polymorphisms in the promoter region of the human alpha2B-adrenergic receptor gene.";
Biochem. Pharmacol. 67:469-478(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"Isolation of complete coding sequence for adrenergic receptor alpha 2B (ADRA2B).";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-211 AND GLY-379, AND FRAMESHIFT POLYMORPHISM.
SeattleSNPs variation discovery resource;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT 301-GLU--GLU-303 DEL.
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-389.
DOI=10.1016/0006-291X(90)90748-C; PubMed=2173582 [NCBI, ExPASy, EBI, Israel, Japan]
Chang A.C., Ho T.F., Chang N.-C.A.;
"In vitro amplification by polymerase chain reaction of a partial gene encoding the third subtype of alpha-2 adrenergic receptor in humans.";
Biochem. Biophys. Res. Commun. 172:817-823(1990).
Comments
  • 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 clonidine > norepinephrine > epinephrine = oxymetazoline > dopamine > p-tyramine = phenylephrine > serotonin > p-synephrine / p-octopamine. For antagonists, the rank order is yohimbine > chlorpromazine > phentolamine > mianserine > spiperone > prazosin > alprenolol > propanolol > pindolol.
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
  • POLYMORPHISM: A rare polymorphic framshift in position 451 produces a protein of 542 residues.
  • SIMILARITY: Belongs to the G-protein coupled receptor 1 family [view classification].
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/adra2b/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M34041; AAA51666.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF316895; AAK01635.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005900; AAB62558.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY548167; AAS55646.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ057076; AAY43127.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC092603; AAX93218.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38742; AAA62823.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00297315; -.
PIR A37223; A37223.
RefSeq NP_000673.2; -.
UniGene Hs.247686
3D structure databases
PDB
2CVA; Model; -; A=97-128.[ExPASy / RCSB / EBI]
PDBsum 2CVA; -.
ModBase P18089.
Protein family/group databases
GPCRDB P18089; ADA2B_HUMAN.
Organism-specific databases
GeneCards GC02M096200; -.
H-InvDB HIX0030044; -.
HGNC HGNC:282; ADRA2B.
GenAtlas ADRA2B.
MIM 104260; gene. [NCBI / EBI]
PharmGKB PA36; -.
Gene expression databases
ArrayExpress P18089; -.
CleanEx HS_ADRA2B; -.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0004938; Molecular function: alpha2-adrenergic receptor activity (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000276; 7TM_GPCR_Rhodpsn.
IPR015695; Adren_rcpt_A2A/B/C.
IPR000207; Adren_rcpt_A2B.
IPR002233; Adrnrgc_rcpt.
IPR017452; GPCR_Rhodpsn_supfam.
Graphical view of domain structure.
PANTHER PTHR19266:SF56; Alpha-2A_Recept; 1.
Pfam PF00001; 7tm_1; 1.
Pfam graphical view of domain structure.
PRINTS PR01103; ADRENERGICR.
PR00559; ADRENRGCA2BR.
PR00237; GPCRRHODOPSN.
PROSITE PS00237; G_PROTEIN_RECEP_F1_1; 1.
PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P18089; -.
Genome annotation databases
Ensembl ENSG00000222040; Homo sapiens. [Contig view]
GeneID 151; -.
KEGG hsa:151; -.
Phylogenomic databases
HOVERGEN P18089; -.
Other
DrugBank DB00217; Bethanidine.
DB00484; Brimonidine.
DB04840; Debrisoquin.
DB00696; Ergotamine.
DB00800; Fenoldopam.
DB00226; Guanadrel Sulfate.
DB01170; Guanethidine.
DB04948; Lofexidine.
DB00368; Norepinephrine.
DB01392; Yohimbine.
NextBio 599; -.
SOURCE ADRA2B; Homo sapiens.
GPCRDB-Snakes P18089.
ProtoNet P18089.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor; Transducer; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   450  450     Alpha-2B adrenergic receptor. PRO_0000069094
TOPO_DOM   1    12  12     Extracellular (By similarity). 
TRANSMEM   13    38  26     1 (By similarity). 
TOPO_DOM   39    49  11     Cytoplasmic (By similarity). 
TRANSMEM   50    75  26     2 (By similarity). 
TOPO_DOM   76    85  10     Extracellular (By similarity). 
TRANSMEM   86   108  23     3 (By similarity). 
TOPO_DOM   109   130  22     Cytoplasmic (By similarity). 
TRANSMEM   131   153  23     4 (By similarity). 
TOPO_DOM   154   169  16     Extracellular (By similarity). 
TRANSMEM   170   193  24     5 (By similarity). 
TOPO_DOM   194   372  179     Cytoplasmic (By similarity). 
TRANSMEM   373   396  24     6 (By similarity). 
TOPO_DOM   397   405  9     Extracellular (By similarity). 
TRANSMEM   406   429  24     7 (By similarity). 
TOPO_DOM   430   450  21     Cytoplasmic (By similarity). 
COMPBIAS   294   311  18     Asp/Glu-rich (acidic). 
SITE   92    92  1     Implicated in ligand binding (By similarity). 
SITE   176   176  1     Implicated in catechol agonist binding (By similarity). 
SITE   180   180  1     Implicated in catechol agonist binding (By similarity). 
LIPID   442   442        S-palmitoyl cysteine (Potential). 
DISULFID   85   164        By similarity. 
VARIANT   211   211  1     G -> A (in dbSNP:rs9333568 [NCBI]). VAR_025099 
VARIANT   301   303  3     Missing (common polymorphism; frequency in Caucasians 0.31 and in African-Americans 0.12; impaired phosphorylation and desensitization by GRKs). VAR_014958
VARIANT   376   376  1     V -> I (in dbSNP:rs29000569 [NCBI]). VAR_033462 
VARIANT   379   379  1     V -> G. VAR_025100 
VARIANT   379   379  1     V -> I (in dbSNP:rs29000569 [NCBI]). VAR_033463 
CONFLICT   362   363        QL -> HV (in Ref. 1 and 2). 
Sequence information
Length: 450 AA [This is the length of the unprocessed precursor] Molecular weight: 49954 Da [This is the MW of the unprocessed precursor] CRC64: 06E43857152A68ED [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDHQDPYSVQ ATAAIAAAIT FLILFTIFGN ALVILAVLTS RSLRAPQNLF LVSLAAADIL 

        70         80         90        100        110        120 
VATLIIPFSL ANELLGYWYF RRTWCEVYLA LDVLFCTSSI VHLCAISLDR YWAVSRALEY 

       130        140        150        160        170        180 
NSKRTPRRIK CIILTVWLIA AVISLPPLIY KGDQGPQPRG RPQCKLNQEA WYILASSIGS 

       190        200        210        220        230        240 
FFAPCLIMIL VYLRIYLIAK RSNRRGPRAK GGPGQGESKQ PRPDHGGALA SAKLPALASV 

       250        260        270        280        290        300 
ASAREVNGHS KSTGEKEEGE TPEDTGTRAL PPSWAALPNS GQGQKEGVCG ASPEDEAEEE 

       310        320        330        340        350        360 
EEEEEEEEEC EPQAVPVSPA SACSPPLQQP QGSRVLATLR GQVLLGRGVG AIGGQWWRRR 

       370        380        390        400        410        420 
AQLTREKRFT FVLAVVIGVF VLCWFPFFFS YSLGAICPKH CKVPHGLFQF FFWIGYCNSS 

       430        440        450 
LNPVIYTIFN QDFRRAFRRI LCRPWTQTAW 

P18089 in FASTA format

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