ID ADA1D_MOUSE Reviewed; 562 AA. AC P97714; Q61619; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 10-JUN-2026, entry version 161. DE RecName: Full=Alpha-1D adrenergic receptor {ECO:0000303|PubMed:7595531}; DE AltName: Full=Alpha-1A adrenergic receptor {ECO:0000250|UniProtKB:P25100}; DE AltName: Full=Alpha-1D adrenoreceptor; DE Short=Alpha-1D adrenoceptor {ECO:0000250|UniProtKB:O02666}; GN Name=Adra1d {ECO:0000312|MGI:MGI:106673}; Synonyms=Adra1a, Gpcr8; 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 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10622215; DOI=10.1254/jjp.81.271; RA Arai K., Tanoue A., Goda N., Takeda M., Takahashi K., Tsujimoto G.; RT "Characterization of the mouse alpha1D-adrenergic receptor gene."; RL Jpn. J. Pharmacol. 81:271-278(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 190-350. RC TISSUE=Testis; RX PubMed=8288218; DOI=10.1006/geno.1993.1452; RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., RA Copeland N.G., Jenkins N.A.; RT "Identification, chromosomal location, and genome organization of mammalian RT G-protein-coupled receptors."; RL Genomics 18:175-184(1993). RN [4] RP PALMITOYLATION BY ZDHHC21. RX PubMed=26715683; DOI=10.1161/atvbaha.115.306942; RA Marin E.P., Jozsef L., Di Lorenzo A., Held K.F., Luciano A.K., Melendez J., RA Milstone L.M., Velazquez H., Sessa W.C.; RT "The Protein Acyl Transferase ZDHHC21 Modulates alpha1 Adrenergic Receptor RT Function and Regulates Hemodynamics."; RL Arterioscler. Thromb. Vasc. Biol. 36:370-379(2016). CC -!- FUNCTION: Alpha-1 adrenergic receptors are G protein-coupled receptors CC for catecholamines that signal through the G(q) family of G proteins, CC including G(q) and G(11). Upon activation, they stimulate the CC phosphatidylinositol-calcium second messenger pathway, leading to CC calcium release from intracellular stores and activation of protein CC kinase C (By similarity). ADRA1D binds the catecholamine ligands CC norepinephrine and epinephrine (By similarity). CC {ECO:0000250|UniProtKB:P25100}. CC -!- SUBUNIT: Interacts with FLNA (via filamin repeat 21); increases PKA- CC mediated phosphorylation of FLNA. {ECO:0000250|UniProtKB:P25100}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- PTM: Palmitoylated (PubMed:26715683). Palmitoylation by ZDHHC21 may CC increase the expression of the receptor and regulate downstream CC signaling (PubMed:26715683). {ECO:0000269|PubMed:26715683}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC Adrenergic receptor subfamily. ADRA1D sub-subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S80044; AAB47042.1; -; mRNA. DR EMBL; AB030642; BAA90312.1; -; Genomic_DNA. DR EMBL; L20333; AAA16854.1; -; mRNA. DR PIR; D48909; D48909. DR AlphaFoldDB; P97714; -. DR SMR; P97714; -. DR CORUM; P97714; -. DR FunCoup; P97714; 491. DR STRING; 10090.ENSMUSP00000099473; -. DR BindingDB; P97714; -. DR ChEMBL; CHEMBL2130; -. DR GlyCosmos; P97714; 2 sites, No reported glycans. DR GlyGen; P97714; 2 sites. DR PhosphoSitePlus; P97714; -. DR PaxDb; 10090-ENSMUSP00000099473; -. DR AGR; MGI:106673; -. DR MGI; MGI:106673; Adra1d. DR InParanoid; P97714; -. 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 PRO; PR:P97714; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P97714; protein. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central. DR GO; GO:0001986; P:negative regulation of the force of heart contraction involved in baroreceptor response to increased systemic arterial blood pressure; IMP: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: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; IBA:GO_Central. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:GO_Central. DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI. DR FunFam; 1.20.1070.10:FF:000208; Alpha-1D adrenergic receptor; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR002233; ADR_fam. DR InterPro; IPR000363; ADRA1D_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:SF14; ALPHA-1D ADRENERGIC RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00240; ADRENRGCA1DR. 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; G protein-coupled receptor; Glycoprotein; Lipoprotein; KW Membrane; Palmitate; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..562 FT /note="Alpha-1D adrenergic receptor" FT /id="PRO_0000069074" FT TOPO_DOM 1..90 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 91..115 FT /note="Helical; Name=1" FT /evidence="ECO:0000250" FT TOPO_DOM 116..127 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 128..153 FT /note="Helical; Name=2" FT /evidence="ECO:0000250" FT TOPO_DOM 154..163 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 164..186 FT /note="Helical; Name=3" FT /evidence="ECO:0000250" FT TOPO_DOM 187..207 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 208..232 FT /note="Helical; Name=4" FT /evidence="ECO:0000250" FT TOPO_DOM 233..245 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 246..269 FT /note="Helical; Name=5" FT /evidence="ECO:0000250" FT TOPO_DOM 270..342 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 343..367 FT /note="Helical; Name=6" FT /evidence="ECO:0000250" FT TOPO_DOM 368..374 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 375..399 FT /note="Helical; Name=7" FT /evidence="ECO:0000250" FT TOPO_DOM 400..562 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT REGION 13..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 50..69 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 444..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..44 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 170 FT /ligand="(R)-adrenaline" FT /ligand_id="ChEBI:CHEBI:71406" FT /evidence="ECO:0000250|UniProtKB:P35348" FT BINDING 252 FT /ligand="(R)-adrenaline" FT /ligand_id="ChEBI:CHEBI:71406" FT /evidence="ECO:0000250|UniProtKB:P35348" FT LIPID 413 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" FT CARBOHYD 60 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 330 FT /note="R -> G (in Ref. 3; AAA16854)" FT /evidence="ECO:0000305" SQ SEQUENCE 562 AA; 59858 MW; 6CF15515B5F7FA47 CRC64; MTFRDILSVT FEGPRASSST GGSGAGGGAG TVGPEGPAVG GVPGATGGSA VVGTGSGEDN QSSTAEAGAA ASGEVNGSAA VGGLVVSAQG VGVGVFLAAF ILTAVAGNLL VILSVACNRH LQTVTNYFIV NLAVADLLLS AAVLPFSATM EVLGFWPFGR TFCDVWAAVD VLCCTASILS LCTISVDRYV GVRHSLKYPA IMTERKAAAI LALLWAVALV VSVGPLLGWK EPVPPDERFC GITEEVGYAI FSSVCSFYLP MAVIVVMYCR VYVVARSTTR SLEAGIKREP GKASEVVLRI HCRGAATSAK GNPGTQSSKG HTLRSSLSVR LLKFSREKKA AKTLAIVVGV FVLCWFPFFF VLPLGSLFPQ LKPSEGVFKV IFWLGYFNSC VNPLIYPCSS REFKRAFLRL LRCQCRRRRR RLWPSLRPPL ASLDRRPALR LCPQPAHRTP RGSPSPHCTP RPGLRRHAGG AGFGLRPSKA SLRLREWRLL GPLQRPTTQL RAKVSSLSHK FRSGGARRAE TACALRSEVE AVSLNVPQDG AEAVICQAYE PGDLSNLRET DI //