ADA1A_RAT
ID ADA1A_RAT Reviewed; 466 AA.
AC P43140;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Alpha-1A adrenergic receptor;
DE AltName: Full=Alpha-1A adrenoreceptor;
DE Short=Alpha-1A adrenoceptor;
DE AltName: Full=Alpha-1C adrenergic receptor;
GN Name=Adra1a; Synonyms=Adra1c;
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=Heart muscle;
RX PubMed=7923624; DOI=10.1161/01.res.75.4.796;
RA Stewart A.F., Rokosh D.G., Bailey B.A., Karns L.R., Chang K.C., Long C.S.,
RA Kariya K., Simpson P.C.;
RT "Cloning of the rat alpha 1C-adrenergic receptor from cardiac myocytes.
RT Alpha 1C, alpha 1B, and alpha 1D mRNAs are present in cardiac myocytes but
RT not in cardiac fibroblasts.";
RL Circ. Res. 75:796-802(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7935320;
RA Laz T.M., Forray C., Smith K.E., Bard J.A., Vaysse P.J., Branchek T.A.,
RA Weinshank R.L.;
RT "The rat homologue of the bovine alpha 1c-adrenergic receptor shows the
RT pharmacological properties of the classical alpha 1A subtype.";
RL Mol. Pharmacol. 46:414-422(1994).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=8185565; DOI=10.1006/bbrc.1994.1575;
RA Rokosh D.G., Bailey B.A., Stewart A.F., Karns L.R., Long C.S.,
RA Simpson P.C.;
RT "Distribution of alpha 1C-adrenergic receptor mRNA in adult rat tissues by
RT RNase protection assay and comparison with alpha 1B and alpha 1D.";
RL Biochem. Biophys. Res. Commun. 200:1177-1184(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:P35348}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein.
CC Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}.
CC Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the
CC nuclear membrane facilitates heterooligomerization and regulates ERK-
CC mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as
CC well as LAP2 at the nuclear membrane of cardiac myocytes (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Abundant in heart, brain, aorta, vena cava, vas
CC deferens, submaxillary gland, lung, and kidney. Found at lower levels
CC in prostate, parotid gland and skeletal muscle.
CC {ECO:0000269|PubMed:8185565}.
CC -!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA1A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U13368; AAA52103.1; -; mRNA.
DR EMBL; U07126; AAA62866.1; -; mRNA.
DR PIR; I57959; I57959.
DR RefSeq; NP_058887.2; NM_017191.2.
DR RefSeq; XP_006252169.1; XM_006252107.3.
DR RefSeq; XP_008768966.1; XM_008770744.2.
DR AlphaFoldDB; P43140; -.
DR SMR; P43140; -.
DR IntAct; P43140; 1.
DR STRING; 10116.ENSRNOP00000012736; -.
DR BindingDB; P43140; -.
DR ChEMBL; CHEMBL319; -.
DR DrugCentral; P43140; -.
DR GuidetoPHARMACOLOGY; 22; -.
DR GlyGen; P43140; 3 sites.
DR PhosphoSitePlus; P43140; -.
DR PaxDb; P43140; -.
DR GeneID; 29412; -.
DR KEGG; rno:29412; -.
DR UCSC; RGD:2055; rat.
DR CTD; 148; -.
DR RGD; 2055; Adra1a.
DR VEuPathDB; HostDB:ENSRNOG00000009522; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_6_1; -.
DR InParanoid; P43140; -.
DR OMA; KHHFSVR; -.
DR OrthoDB; 1095345at2759; -.
DR PhylomeDB; P43140; -.
DR TreeFam; TF331895; -.
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:P43140; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000009522; Expressed in heart and 10 other tissues.
DR Genevisible; P43140; RN.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0030018; C:Z disc; 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:0007202; P:activation of phospholipase C activity; IDA:RGD.
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:0007568; P:aging; IDA:RGD.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IMP:BHF-UCL.
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:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0060073; P:micturition; IMP:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0001985; P:negative regulation of heart rate involved in baroreceptor response to increased systemic arterial blood pressure; 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:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; 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; ISO:RGD.
DR GO; GO:0097195; P:pilomotor reflex; ISO:RGD.
DR GO; GO:0045760; P:positive regulation of action potential; IMP:RGD.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR GO; GO:0010460; P:positive regulation of heart rate; IMP: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:1903997; P:positive regulation of non-membrane spanning protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IDA:RGD.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:RGD.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:RGD.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:RGD.
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; IDA:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0009725; P:response to hormone; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:RGD.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR001004; ADRA1A_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00557; ADRENRGCA1AR.
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..466
FT /note="Alpha-1A adrenergic receptor"
FT /id="PRO_0000069066"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 28..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 52..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..99
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 100..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 123..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 144..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 168..181
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 206..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 274..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..305
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 306..329
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 330..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 334..349
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 345
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 39
FT /note="F -> L (in Ref. 1; AAA52103)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="N -> G (in Ref. 1; AAA52103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51598 MW; 4962D3A72E971A36 CRC64;
MVLLSENASE GSNCTHPPAP VNISKAILLG VILGGLIIFG VLGNILVILS VACHRHLHSV
THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN IWAAVDVLCC TASIMGLCII
SIDRYIGVSY PLRYPTIVTQ RRGVRALLCV WVLSLVISIG PLFGWRQPAP EDETICQINE
EPGYVLFSAL GSFYVPLAII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN
VPAEGGGVSS AKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPD
FKPSETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LRIQCLRRRQ SSKHALGYTL
HPPSQALEGQ HRDMVRIPVG SGETFYKISK TDGVCEWKFF SSMPQGSARI TVPKDQSACT
TARVRSKSFL QVCCCVGSSA PRPEENHQVP TIKIHTISLG ENGEEV
