ADA1B_RAT
ID ADA1B_RAT Reviewed; 515 AA.
AC P15823; Q63215;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Alpha-1B adrenergic receptor;
DE AltName: Full=Alpha-1B adrenoreceptor;
DE Short=Alpha-1B adrenoceptor;
GN Name=Adra1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=2156222; DOI=10.1093/nar/18.4.1053;
RA Voigt M.M., Kispert J., Chin H.;
RT "Sequence of a rat brain cDNA encoding an alpha-1B adrenergic receptor.";
RL Nucleic Acids Res. 18:1053-1053(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1706716; DOI=10.1016/s0021-9258(18)38126-2;
RA Lomasney J.W., Cotecchia S., Lorenz W., Leung W.-Y., Schwinn D.A.,
RA Yang-Feng T.L., Brownstein M., Lefkowitz R.J., Caron M.G.;
RT "Molecular cloning and expression of the cDNA for the alpha 1A-adrenergic
RT receptor. The gene for which is located on human chromosome 5.";
RL J. Biol. Chem. 266:6365-6369(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8406017; DOI=10.1016/0378-1119(93)90300-r;
RA Gao B., Kunos G.;
RT "Isolation and characterization of the gene encoding the rat alpha 1B
RT adrenergic receptor.";
RL Gene 131:243-247(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-253.
RX PubMed=7989580; DOI=10.1172/jci117587;
RA Kanasaki M., Matsubara H., Murasawa S., Masaki H., Nio Y., Inada M.;
RT "cAMP responsive element-mediated regulation of the gene transcription of
RT the alpha 1B adrenergic receptor by thyrotropin.";
RL J. Clin. Invest. 94:2245-2254(1994).
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: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; X51585; CAA35934.1; -; mRNA.
DR EMBL; M60655; AAA63478.1; -; mRNA.
DR EMBL; L08610; AAA40647.1; -; Genomic_DNA.
DR EMBL; L08609; AAA40647.1; JOINED; Genomic_DNA.
DR EMBL; D32045; BAA06806.1; -; Genomic_DNA.
DR PIR; JC1525; JC1525.
DR AlphaFoldDB; P15823; -.
DR SMR; P15823; -.
DR DIP; DIP-59867N; -.
DR IntAct; P15823; 1.
DR BindingDB; P15823; -.
DR ChEMBL; CHEMBL315; -.
DR DrugCentral; P15823; -.
DR GuidetoPHARMACOLOGY; 23; -.
DR GlyGen; P15823; 3 sites.
DR iPTMnet; P15823; -.
DR PhosphoSitePlus; P15823; -.
DR UCSC; RGD:2054; rat.
DR RGD; 2054; Adra1b.
DR InParanoid; P15823; -.
DR PhylomeDB; P15823; -.
DR Reactome; R-RNO-390696; Adrenoceptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR PRO; PR:P15823; -.
DR Proteomes; UP000002494; 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; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:RGD.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0045818; P:negative regulation of glycogen catabolic process; ISO:RGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:MGI.
DR GO; GO:0150099; P:neuron-glial cell signaling; ISO:RGD.
DR GO; GO:0035265; P:organ growth; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0045819; P:positive regulation of glycogen catabolic process; ISO:RGD.
DR GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IMP:RGD.
DR GO; GO:0043278; P:response to morphine; ISO:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0001987; P:vasoconstriction of artery involved in baroreceptor response to lowering of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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 2: Evidence at transcript 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_0000069072"
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..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 183..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..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..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 481..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 CONFLICT 114..116
FT /note="GRI -> LSF (in Ref. 2; AAA63478)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="Y -> C (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> C (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="C -> S (in Ref. 3; AAA40647)"
FT /evidence="ECO:0000305"
FT CONFLICT 415..416
FT /note="TQ -> QK (in Ref. 1; CAA35934)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="C -> Y (in Ref. 3; AAA40647)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..486
FT /note="GDT -> ATA (in Ref. 1; CAA35934)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="T -> S (in Ref. 3; AAA40647)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="A -> G (in Ref. 1; CAA35934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56586 MW; AF0C3759F80C3135 CRC64;
MNPDLDTGHN TSAPAHWGEL KDDNFTGPNQ 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
RILGCQCRGG RRRRRRRRLG ACAYTYRPWT RGGSLERSQS RKDSLDDSGS CMSGTQRTLP
SASPSPGYLG RGTQPPVELC AFPEWKPGAL LSLPEPPGRR GRLDSGPLFT FKLLGDPESP
GTEGDTSNGG CDTTTDLANG QPGFKSNMPL APGHF
