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   08-NOV-2023, entry version 156.
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   GlyCosmos; P97717; 4 sites, No reported glycans.
DR   GlyGen; P97717; 4 sites.
DR   iPTMnet; P97717; -.
DR   PhosphoSitePlus; P97717; -.
DR   MaxQB; P97717; -.
DR   PaxDb; 10090-ENSMUSP00000070200; -.
DR   ProteomicsDB; 285858; -.
DR   AGR; MGI:104774; -.
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:0014704; C:intercalated disc; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA: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: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: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:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR   GO; GO:0019229; P:regulation of vasoconstriction; 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   CDD; cd15326; 7tmA_alpha1B_AR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR001115; ADRA1B_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:SF17; ALPHA-1B ADRENERGIC RECEPTOR; 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   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   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
//