ID ADA1A_MOUSE Reviewed; 466 AA.
AC P97718; O54913; Q8BV77;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 24-JAN-2024, entry version 186.
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 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], AND CHARACTERIZATION.
RC STRAIN=CD-1; TISSUE=Brain, and Kidney;
RX PubMed=9630362; DOI=10.1038/sj.bjp.0701812;
RA Xiao L., Scofield M.A., Jeffries W.B.;
RT "Molecular cloning, expression and characterization of cDNA encoding a
RT mouse alpha1a-adrenoceptor.";
RL Br. J. Pharmacol. 124:213-221(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-280.
RC TISSUE=Brain;
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 [6]
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:P35348}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:22120526};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22120526}. Cell
CC membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane,
CC caveola {ECO:0000250|UniProtKB:P35348}. 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. ADRA1A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB47044.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF031431; AAC02658.1; -; mRNA.
DR EMBL; AK079597; BAC37694.1; -; mRNA.
DR EMBL; CH466535; EDL35992.1; -; Genomic_DNA.
DR EMBL; BC113139; AAI13140.1; -; mRNA.
DR EMBL; S80220; AAB47044.1; ALT_INIT; mRNA.
DR CCDS; CCDS27223.1; -.
DR RefSeq; NP_001258689.1; NM_001271760.1.
DR RefSeq; NP_038489.2; NM_013461.4.
DR RefSeq; XP_006518507.1; XM_006518444.3.
DR RefSeq; XP_011243225.1; XM_011244923.2.
DR RefSeq; XP_011243226.1; XM_011244924.2.
DR RefSeq; XP_011243227.1; XM_011244925.2.
DR RefSeq; XP_017171289.1; XM_017315800.1.
DR RefSeq; XP_017171290.1; XM_017315801.1.
DR AlphaFoldDB; P97718; -.
DR SMR; P97718; -.
DR IntAct; P97718; 1.
DR STRING; 10090.ENSMUSP00000124570; -.
DR BindingDB; P97718; -.
DR ChEMBL; CHEMBL2822; -.
DR GlyCosmos; P97718; 3 sites, No reported glycans.
DR GlyGen; P97718; 3 sites.
DR iPTMnet; P97718; -.
DR PhosphoSitePlus; P97718; -.
DR PaxDb; 10090-ENSMUSP00000053703; -.
DR ProteomicsDB; 285607; -.
DR Antibodypedia; 10062; 416 antibodies from 38 providers.
DR DNASU; 11549; -.
DR Ensembl; ENSMUST00000054661.8; ENSMUSP00000053703.2; ENSMUSG00000045875.14.
DR Ensembl; ENSMUST00000159068.2; ENSMUSP00000124570.2; ENSMUSG00000045875.14.
DR Ensembl; ENSMUST00000161339.2; ENSMUSP00000125354.2; ENSMUSG00000045875.14.
DR GeneID; 11549; -.
DR KEGG; mmu:11549; -.
DR UCSC; uc007ukh.2; mouse.
DR AGR; MGI:104773; -.
DR CTD; 148; -.
DR MGI; MGI:104773; Adra1a.
DR VEuPathDB; HostDB:ENSMUSG00000045875; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000159105; -.
DR InParanoid; P97718; -.
DR OMA; FLQECCC; -.
DR OrthoDB; 4073525at2759; -.
DR PhylomeDB; P97718; -.
DR TreeFam; TF331895; -.
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 BioGRID-ORCS; 11549; 5 hits in 79 CRISPR screens.
DR ChiTaRS; Adra1a; mouse.
DR PRO; PR:P97718; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97718; Protein.
DR Bgee; ENSMUSG00000045875; Expressed in right kidney and 40 other cell types or tissues.
DR ExpressionAtlas; P97718; baseline and differential.
DR Genevisible; P97718; MM.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0030018; C:Z disc; 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:0060402; P:calcium ion transport into cytosol; ISO: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:0000165; P:MAPK cascade; IGI:MGI.
DR GO; GO:0010507; P:negative regulation of autophagy; IDA:MGI.
DR GO; GO:0001985; P:negative regulation of heart rate involved in baroreceptor response to increased systemic arterial blood pressure; 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:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0035265; P:organ growth; IGI:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0097195; P:pilomotor reflex; IDA:BHF-UCL.
DR GO; GO:0045760; P:positive regulation of action potential; ISO:MGI.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISO:MGI.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IDA:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO: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; IGI:MGI.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISO:MGI.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:BHF-UCL.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISO:MGI.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR CDD; cd15325; 7tmA_alpha1A_AR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR001004; ADRA1A_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:SF16; ALPHA-1A ADRENERGIC RECEPTOR; 1.
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 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..466
FT /note="Alpha-1A adrenergic receptor"
FT /id="PRO_0000069064"
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 369
FT /note="G -> E (in Ref. 1; AAC02658)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="R -> C (in Ref. 1; AAC02658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51744 MW; 8C5FE5C67E885795 CRC64;
MVLLSENASE GSNCTHPPAQ VNISKAILLG VILGGLIIFG VLGNILVILS VACHRHLHSV
THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN IWAAVDVLCC TASIMGLCII
SIDRYIGVSY PLRYPTIVTQ RRGVRALLCV WALSLVISIG PLFGWRQQAP EDETICQINE
EPGYVLFSAL GSFYVPLTII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN
VPAEGSGVSS AKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPN
FKPPETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LRIQCLRRRQ SSKHALGYTL
HPPSQAVEGQ HRGMVRIPVG SGETFYKISK TDGVREWKFF SSMPQGSARI TMPKDQSACT
TARVRSKSFL QVCCCVGSST PRPEENHQVP TIKIHTISLG ENGEEV
//
