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ADA1B_HUMAN
ID   ADA1B_HUMAN             Reviewed;         520 AA.
AC   P35368; B0LPE1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Alpha-1B adrenergic receptor;
DE   AltName: Full=Alpha-1B adrenoreceptor;
DE            Short=Alpha-1B adrenoceptor;
GN   Name=ADRA1B;
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=1328250; DOI=10.1016/s0021-9258(19)36703-1;
RA   Ramarao C.S., Denker J.M., Perez D.M., Gaivin R.J., Riek R.P., Graham R.M.;
RT   "Genomic organization and expression of the human alpha 1B-adrenergic
RT   receptor.";
RL   J. Biol. Chem. 267:21936-21945(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8183249;
RA   Forray C., Bard J.A., Wetzel J.M., Chiu G., Shapiro E., Tang R., Lepor H.,
RA   Hartig P.R., Weinshank R.L., Branchek T.A., Gluchowski C.;
RT   "The alpha 1-adrenergic receptor that mediates smooth muscle contraction in
RT   human prostate has the pharmacological properties of the cloned human alpha
RT   1c subtype.";
RL   Mol. Pharmacol. 45:703-708(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7815325;
RA   Schwinn D.A., Johnston G.I., Page S.O., Mosley M.J., Wilson K.H.,
RA   Worman N.P., Campbell S., Fidock M.D., Furness L.M., Parry-Smith D.J.,
RA   Peter B., Bailey D.S.;
RT   "Cloning and pharmacological characterization of human alpha-1 adrenergic
RT   receptors: sequence corrections and direct comparison with other species
RT   homologues.";
RL   J. Pharmacol. Exp. Ther. 272:134-142(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=18802028; DOI=10.1161/circresaha.108.176024;
RA   Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S.,
RA   O'Connell T.D.;
RT   "Nuclear alpha1-adrenergic receptors signal activated ERK localization to
RT   caveolae in adult cardiac myocytes.";
RL   Circ. Res. 103:992-1000(2008).
RN   [7]
RP   SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, AND MUTAGENESIS OF
RP   368-ARG--ARG-380.
RX   PubMed=22120526; DOI=10.1016/j.cellsig.2011.11.014;
RA   Wright C.D., Wu S.C., Dahl E.F., Sazama A.J., O'Connell T.D.;
RT   "Nuclear localization drives alpha1-adrenergic receptor oligomerization and
RT   signaling in cardiac myocytes.";
RL   Cell. Signal. 24:794-802(2012).
RN   [8]
RP   INTERACTION WITH CAVIN4, AND SUBCELLULAR LOCATION.
RX   PubMed=24567387; DOI=10.1073/pnas.1315359111;
RA   Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T., Miyagawa K.,
RA   Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H., Oh H., Ueyama T.;
RT   "MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric
RT   cardiac hypertrophy induced by alpha1-adrenergic receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014).
CC   -!- FUNCTION: This alpha-adrenergic receptor mediates its action by
CC       association with G proteins that activate a phosphatidylinositol-
CC       calcium second messenger system. Its effect is mediated by G(q) and
CC       G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate
CC       phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes.
CC       {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}.
CC   -!- SUBUNIT: Homo- and heterooligomer. Heterooligomerizes with ADRA1B
CC       homooligomers in cardiac myocytes (PubMed:22120526). Interacts with
CC       CAVIN4 (PubMed:24567387). {ECO:0000269|PubMed:22120526,
CC       ECO:0000269|PubMed:24567387}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein.
CC       Cell membrane {ECO:0000269|PubMed:24567387}; Multi-pass membrane
CC       protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:24567387}.
CC       Membrane, caveola {ECO:0000269|PubMed:24567387}. Note=Location at the
CC       nuclear membrane facilitates heterooligomerization and regulates ERK-
CC       mediated signaling in cardiac myocytes. signaling in cardiac myocytes.
CC       Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of
CC       cardiac myocytes.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRA1B sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; M99589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M99590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U03865; AAB60352.1; -; mRNA.
DR   EMBL; L31773; AAB59485.1; -; mRNA.
DR   EMBL; EU332831; ABY87520.1; -; Genomic_DNA.
DR   EMBL; BC136568; AAI36569.1; -; mRNA.
DR   EMBL; BC136569; AAI36570.1; -; mRNA.
DR   CCDS; CCDS4347.1; -.
DR   PIR; A45121; A45121.
DR   RefSeq; NP_000670.1; NM_000679.3.
DR   AlphaFoldDB; P35368; -.
DR   SMR; P35368; -.
DR   BioGRID; 106657; 6.
DR   DIP; DIP-33399N; -.
DR   IntAct; P35368; 9.
DR   MINT; P35368; -.
DR   STRING; 9606.ENSP00000306662; -.
DR   BindingDB; P35368; -.
DR   ChEMBL; CHEMBL232; -.
DR   DrugBank; DB01614; Acepromazine.
DR   DrugBank; DB00346; Alfuzosin.
DR   DrugBank; DB00321; Amitriptyline.
DR   DrugBank; DB00543; Amoxapine.
DR   DrugBank; DB00182; Amphetamine.
DR   DrugBank; DB09229; Aranidipine.
DR   DrugBank; DB01238; Aripiprazole.
DR   DrugBank; DB14185; Aripiprazole lauroxil.
DR   DrugBank; DB09204; Arotinolol.
DR   DrugBank; DB09128; Brexpiprazole.
DR   DrugBank; DB01200; Bromocriptine.
DR   DrugBank; DB00490; Buspirone.
DR   DrugBank; DB00248; Cabergoline.
DR   DrugBank; DB01136; Carvedilol.
DR   DrugBank; DB00477; Chlorpromazine.
DR   DrugBank; DB09202; Cirazoline.
DR   DrugBank; DB00575; Clonidine.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB00298; Dapiprazole.
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; DB00841; Dobutamine.
DR   DrugBank; DB09167; Dosulepin.
DR   DrugBank; DB00590; Doxazosin.
DR   DrugBank; DB01142; Doxepin.
DR   DrugBank; DB04855; Dronedarone.
DR   DrugBank; DB06262; Droxidopa.
DR   DrugBank; DB05492; Epicept NP-1.
DR   DrugBank; DB00668; Epinephrine.
DR   DrugBank; DB01049; Ergoloid mesylate.
DR   DrugBank; DB00696; Ergotamine.
DR   DrugBank; DB01175; Escitalopram.
DR   DrugBank; DB09194; Etoperidone.
DR   DrugBank; DB00800; Fenoldopam.
DR   DrugBank; DB00458; Imipramine.
DR   DrugBank; DB11577; Indigotindisulfonic acid.
DR   DrugBank; DB00598; Labetalol.
DR   DrugBank; DB09195; Lorpiprazole.
DR   DrugBank; DB00408; Loxapine.
DR   DrugBank; DB00934; Maprotiline.
DR   DrugBank; DB01365; Mephentermine.
DR   DrugBank; DB01403; Methotrimeprazine.
DR   DrugBank; DB00723; Methoxamine.
DR   DrugBank; DB06148; Mianserin.
DR   DrugBank; DB00211; Midodrine.
DR   DrugBank; DB00370; Mirtazapine.
DR   DrugBank; DB00745; Modafinil.
DR   DrugBank; DB09205; Moxisylyte.
DR   DrugBank; DB01149; Nefazodone.
DR   DrugBank; DB00622; Nicardipine.
DR   DrugBank; DB00368; Norepinephrine.
DR   DrugBank; DB00540; Nortriptyline.
DR   DrugBank; DB06229; Ocaperidone.
DR   DrugBank; DB00334; Olanzapine.
DR   DrugBank; DB00935; Oxymetazoline.
DR   DrugBank; DB01267; Paliperidone.
DR   DrugBank; DB00715; Paroxetine.
DR   DrugBank; DB01186; Pergolide.
DR   DrugBank; DB01608; Periciazine.
DR   DrugBank; DB08922; Perospirone.
DR   DrugBank; DB01579; Phendimetrazine.
DR   DrugBank; DB00925; Phenoxybenzamine.
DR   DrugBank; DB00692; Phentolamine.
DR   DrugBank; DB00388; Phenylephrine.
DR   DrugBank; DB09286; Pipamperone.
DR   DrugBank; DB06153; Pizotifen.
DR   DrugBank; DB00457; Prazosin.
DR   DrugBank; DB00433; Prochlorperazine.
DR   DrugBank; DB01069; Promethazine.
DR   DrugBank; DB01224; Quetiapine.
DR   DrugBank; DB00908; Quinidine.
DR   DrugBank; DB05469; R450.
DR   DrugBank; DB11124; Racepinephrine.
DR   DrugBank; DB00243; Ranolazine.
DR   DrugBank; DB00734; Risperidone.
DR   DrugBank; DB00268; Ropinirole.
DR   DrugBank; DB06144; Sertindole.
DR   DrugBank; DB06207; Silodosin.
DR   DrugBank; DB09203; Synephrine.
DR   DrugBank; DB00706; Tamsulosin.
DR   DrugBank; DB01162; Terazosin.
DR   DrugBank; DB06764; Tetryzoline.
DR   DrugBank; DB01622; Thioproperazine.
DR   DrugBank; DB00679; Thioridazine.
DR   DrugBank; DB13025; Tiapride.
DR   DrugBank; DB00697; Tizanidine.
DR   DrugBank; DB00726; Trimipramine.
DR   DrugBank; DB00661; Verapamil.
DR   DrugBank; DB06694; Xylometazoline.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugCentral; P35368; -.
DR   GuidetoPHARMACOLOGY; 23; -.
DR   GlyGen; P35368; 4 sites.
DR   iPTMnet; P35368; -.
DR   PhosphoSitePlus; P35368; -.
DR   BioMuta; ADRA1B; -.
DR   DMDM; 116241241; -.
DR   MassIVE; P35368; -.
DR   MaxQB; P35368; -.
DR   PaxDb; P35368; -.
DR   PeptideAtlas; P35368; -.
DR   PRIDE; P35368; -.
DR   ProteomicsDB; 55037; -.
DR   Antibodypedia; 16635; 510 antibodies from 38 providers.
DR   DNASU; 147; -.
DR   Ensembl; ENST00000306675.5; ENSP00000306662.3; ENSG00000170214.5.
DR   GeneID; 147; -.
DR   KEGG; hsa:147; -.
DR   MANE-Select; ENST00000306675.5; ENSP00000306662.3; NM_000679.4; NP_000670.1.
DR   UCSC; uc003lxt.2; human.
DR   CTD; 147; -.
DR   DisGeNET; 147; -.
DR   GeneCards; ADRA1B; -.
DR   HGNC; HGNC:278; ADRA1B.
DR   HPA; ENSG00000170214; Tissue enhanced (brain, liver, lymphoid tissue).
DR   MIM; 104220; gene.
DR   neXtProt; NX_P35368; -.
DR   OpenTargets; ENSG00000170214; -.
DR   PharmGKB; PA33; -.
DR   VEuPathDB; HostDB:ENSG00000170214; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000156944; -.
DR   HOGENOM; CLU_009579_11_6_1; -.
DR   InParanoid; P35368; -.
DR   OMA; STRAKGH; -.
DR   OrthoDB; 1095345at2759; -.
DR   PhylomeDB; P35368; -.
DR   TreeFam; TF331895; -.
DR   PathwayCommons; P35368; -.
DR   Reactome; R-HSA-390696; Adrenoceptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR   SignaLink; P35368; -.
DR   SIGNOR; P35368; -.
DR   BioGRID-ORCS; 147; 11 hits in 1078 CRISPR screens.
DR   ChiTaRS; ADRA1B; human.
DR   GeneWiki; Alpha-1B_adrenergic_receptor; -.
DR   GenomeRNAi; 147; -.
DR   Pharos; P35368; Tclin.
DR   PRO; PR:P35368; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P35368; protein.
DR   Bgee; ENSG00000170214; Expressed in right lobe of liver and 93 other tissues.
DR   ExpressionAtlas; P35368; baseline and differential.
DR   Genevisible; P35368; HS.
DR   GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004937; F:alpha1-adrenergic receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR   GO; GO:0150099; P:neuron-glial cell signaling; ISS:ARUK-UCL.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IBA:GO_Central.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
DR   GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR001115; ADRA1B_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248:SF17; PTHR24248:SF17; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00556; ADRENRGCA1BR.
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   Cell membrane; Cytoplasm; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Nucleus; Palmitate; Phosphoprotein;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..520
FT                   /note="Alpha-1B adrenergic receptor"
FT                   /id="PRO_0000069069"
FT   TOPO_DOM        1..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        46..70
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        71..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        84..105
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        106..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        116..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        142..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        162..184
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        185..201
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        202..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        225..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        296..319
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        320..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        327..351
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        352..520
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          394..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           368..380
FT                   /note="Nuclear localization signal"
FT   COMPBIAS        407..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         264
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P97717"
FT   LIPID           365
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         51
FT                   /note="V -> G (in dbSNP:rs8192448)"
FT                   /id="VAR_019510"
FT   MUTAGEN         368..380
FT                   /note="RGRGRRRRRRRRR->AGAGAAAAAAAAA: Abolishes targeting to
FT                   the nuclear membrane of cardiac myocytes."
FT                   /evidence="ECO:0000269|PubMed:22120526"
FT   CONFLICT        371
FT                   /note="Missing (in Ref. 1 and 3; AAB59485)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        498..501
FT                   /note="AAAD -> PRH (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   520 AA;  56836 MW;  F081A23D2F943F7F CRC64;
     MNPDLDTGHN TSAPAHWGEL KNANFTGPNQ TSSNSTLPQL DITRAISVGL VLGAFILFAI
     VGNILVILSV ACNRHLRTPT NYFIVNLAMA DLLLSFTVLP FSAALEVLGY WVLGRIFCDI
     WAAVDVLCCT ASILSLCAIS IDRYIGVRYS LQYPTLVTRR KAILALLSVW VLSTVISIGP
     LLGWKEPAPN DDKECGVTEE PFYALFSSLG SFYIPLAVIL VMYCRVYIVA KRTTKNLEAG
     VMKEMSNSKE LTLRIHSKNF HEDTLSSTKA KGHNPRSSIA VKLFKFSREK KAAKTLGIVV
     GMFILCWLPF FIALPLGSLF STLKPPDAVF KVVFWLGYFN SCLNPIIYPC SSKEFKRAFV
     RILGCQCRGR GRRRRRRRRR LGGCAYTYRP WTRGGSLERS QSRKDSLDDS GSCLSGSQRT
     LPSASPSPGY LGRGAPPPVE LCAFPEWKAP GALLSLPAPE PPGRRGRHDS GPLFTFKLLT
     EPESPGTDGG ASNGGCEAAA DVANGQPGFK SNMPLAPGQF
 
 
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