ADA1B_MESAU
ID ADA1B_MESAU Reviewed; 515 AA.
AC P18841;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Alpha-1B adrenergic receptor;
DE AltName: Full=Alpha-1B adrenoreceptor;
DE Short=Alpha-1B adrenoceptor;
GN Name=ADRA1B;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2845398; DOI=10.1073/pnas.85.19.7159;
RA Cotecchia S., Schwinn D.A., Randall R.R., Lefkowitz R.J., Caron M.G.,
RA Kobilka B.K.;
RT "Molecular cloning and expression of the cDNA for the hamster alpha 1-
RT adrenergic receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7159-7163(1988).
RN [2]
RP MUTAGENESIS OF ALA-293.
RX PubMed=1346134; DOI=10.1016/s0021-9258(18)45962-5;
RA Kjelsberg M.A., Cotecchia S., Ostrowski J., Caron M.G., Lefkowitz R.J.;
RT "Constitutive activation of the alpha 1B-adrenergic receptor by all amino
RT acid substitutions at a single site. Evidence for a region which constrains
RT receptor activation.";
RL J. Biol. Chem. 267:1430-1433(1992).
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 -!- INTERACTION:
CC P18841; O35796: C1qbp; Xeno; NbExp=5; IntAct=EBI-6391008, EBI-915544;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250|UniProtKB:P35368}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane,
CC caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear
CC membrane facilitates heterooligomerization and regulates ERK-mediated
CC signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as
CC LAP2 at 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; J04084; AAA58964.1; -; mRNA.
DR PIR; A40491; A40491.
DR RefSeq; NP_001268623.1; NM_001281694.1.
DR AlphaFoldDB; P18841; -.
DR SMR; P18841; -.
DR IntAct; P18841; 1.
DR STRING; 10036.XP_005071976.1; -.
DR BindingDB; P18841; -.
DR ChEMBL; CHEMBL3122; -.
DR DrugCentral; P18841; -.
DR iPTMnet; P18841; -.
DR GeneID; 101843941; -.
DR CTD; 147; -.
DR eggNOG; KOG3656; Eukaryota.
DR PRO; PR:P18841; -.
DR Proteomes; UP000189706; Unplaced.
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; IEA:UniProtKB-KW.
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:0004937; F:alpha1-adrenergic receptor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR GO; GO:0019229; P:regulation of vasoconstriction; 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..515
FT /note="Alpha-1B adrenergic receptor"
FT /id="PRO_0000069070"
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..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 392..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 368..378
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 405..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
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 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 293
FT /note="A->X: Confers constitutive activity."
FT /evidence="ECO:0000269|PubMed:1346134"
SQ SEQUENCE 515 AA; 56493 MW; 6DAF1576D1C1CE2D CRC64;
MNPDLDTGHN TSAPAQWGEL KDANFTGPNQ TSSNSTLPQL DVTRAISVGL VLGAFILFAI
VGNILVILSV ACNRHLRTPT NYFIVNLAIA DLLLSFTVLP FSATLEVLGY WVLGRIFCDI
WAAVDVLCCT ASILSLCAIS IDRYIGVRYS LQYPTLVTRR KAILALLSVW VLSTVISIGP
LLGWKEPAPN DDKECGVTEE PFYALFSSLG SFYIPLAVIL VMYCRVYIVA KRTTKNLEAG
VMKEMSNSKE LTLRIHSKNF HEDTLSSTKA KGHNPRSSIA VKLFKFSREK KAAKTLGIVV
GMFILCWLPF FIALPLGSLF STLKPPDAVF KVVFWLGYFN SCLNPIIYPC SSKEFKRAFM
RILGCQCRSG RRRRRRRRLG ACAYTYRPWT RGGSLERSQS RKDSLDDSGS CMSGSQRTLP
SASPSPGYLG RGAQPPLELC AYPEWKSGAL LSLPEPPGRR GRLDSGPLFT FKLLGEPESP
GTEGDASNGG CDATTDLANG QPGFKSNMPL APGHF
