ADA1B_MOUSE
ID ADA1B_MOUSE Reviewed; 514 AA.
AC P97717;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Alpha-1B adrenergic receptor;
DE AltName: Full=Alpha-1B adrenoreceptor;
DE Short=Alpha-1B adrenoceptor;
GN Name=Adra1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Cotecchia S., Lattion-Zellweger A.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 238-276.
RX PubMed=7595531; DOI=10.1046/j.1471-4159.1995.65062387.x;
RA Alonso-Llamazares A., Zamanillo D., Casanova E., Ovalle S., Calvo P.,
RA Chinchetru M.A.;
RT "Molecular cloning of alpha 1d-adrenergic receptor and tissue distribution
RT of three alpha 1-adrenergic receptor subtypes in mouse.";
RL J. Neurochem. 65:2387-2392(1995).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUBCELLULAR LOCATION.
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).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homo- and heterooligomer. Heterooligomerizes with ADRA1B
CC homooligomers in cardiac myocytes. Interacts with CAVIN4.
CC {ECO:0000250|UniProtKB:P35368}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:22120526};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22120526}. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola
CC {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane
CC facilitates heterooligomerization and regulates ERK-mediated signaling
CC in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at
CC the nuclear membrane of cardiac myocytes (By similarity).
CC {ECO:0000250}.
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; Y12738; CAA73272.1; -; mRNA.
DR EMBL; S80219; AAB47043.1; -; mRNA.
DR AlphaFoldDB; P97717; -.
DR SMR; P97717; -.
DR IntAct; P97717; 1.
DR STRING; 10090.ENSMUSP00000070200; -.
DR BindingDB; P97717; -.
DR ChEMBL; CHEMBL2486; -.
DR GlyGen; P97717; 4 sites.
DR iPTMnet; P97717; -.
DR PhosphoSitePlus; P97717; -.
DR MaxQB; P97717; -.
DR PaxDb; P97717; -.
DR PRIDE; P97717; -.
DR ProteomicsDB; 285858; -.
DR MGI; MGI:104774; Adra1b.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P97717; -.
DR Reactome; R-MMU-390696; Adrenoceptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR ChiTaRS; Adra1b; mouse.
DR PRO; PR:P97717; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97717; protein.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007512; P:adult heart development; IGI:MGI.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IGI:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0045818; P:negative regulation of glycogen catabolic process; IMP:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0150099; P:neuron-glial cell signaling; IGI:ARUK-UCL.
DR GO; GO:0035265; P:organ growth; IGI:MGI.
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; ISO:MGI.
DR GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:MGI.
DR GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IGI:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IGI:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
DR GO; GO:0043278; P:response to morphine; IMP:MGI.
DR GO; GO:0048545; P:response to steroid hormone; ISO:MGI.
DR GO; GO:0001987; P:vasoconstriction of artery involved in baroreceptor response to lowering of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
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..514
FT /note="Alpha-1B adrenergic receptor"
FT /id="PRO_0000069071"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 70..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 105..114
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 115..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 141..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 161..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 184..200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 224..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 295..318
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 319..325
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 326..350
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 351..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 391..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 367..377
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 404..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 364
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 117..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 514 AA; 56418 MW; 17CFD10123DC2B29 CRC64;
MNPDLDTGHN TSAPAHWGEL KDANFTGPNQ TSSNSTLPQL DVTRAISVGC LGAFILFAIV
GNILVILSVA CNRHLRTPTN YFIVNLAIAD LLLSFTDLPF SATLEVLGYW VLGRIFCDIW
AAVDVLCCTA SILSLCAISI DRYIGVRYSL QYPTLVTRRK AILALLSVWV LSTVISIGPL
LGWKEPAPND DKECGVTEEP FYALFSSLGS FYIPLAVILV MYCRVYIVAK RTTKNLEAGV
MKEMSNSKEL TLRIHSKNFH EDTLSSTKAK GHNPRSSIAV KLFKFSREKK AAKTLGIVVG
MFILCWLPFF IALPLGSLFS TLKPPDAVFK VVFWLGYFNS CLNPIIYPCS SKEFKRAFMR
ILGCQCRGGR RRRRRRRLGA CAYTYRPWTR GGSLERSQSR KDSLDDSGSC MSGSQRTLPS
ASPSPGYLGR GTQPPVELCA FPEWKPGALL SLPEPPGRRG RLDSGPLFTF KLLGEPESPG
TEGDASNGGC DTTTDLANGQ PGFKSNMPLA PGHF
