ADA1D_MOUSE
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 25-MAY-2022, entry version 146.
DE RecName: Full=Alpha-1D adrenergic receptor;
DE AltName: Full=Alpha-1A adrenergic receptor;
DE AltName: Full=Alpha-1D adrenoreceptor;
DE Short=Alpha-1D adrenoceptor;
GN Name=Adra1d; 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: This alpha-adrenergic receptor mediates its effect through
CC the influx of extracellular calcium.
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}.
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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 STRING; 10090.ENSMUSP00000099473; -.
DR BindingDB; P97714; -.
DR ChEMBL; CHEMBL2130; -.
DR GlyGen; P97714; 2 sites.
DR PhosphoSitePlus; P97714; -.
DR PRIDE; P97714; -.
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 ChiTaRS; Adra1a; mouse.
DR PRO; PR:P97714; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97714; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0060073; P:micturition; ISO:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
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:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; 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:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000363; ADRA1D_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248:SF14; PTHR24248:SF14; 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 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 53..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
