ADA1D_PIG
ID ADA1D_PIG Reviewed; 571 AA.
AC Q9TTM9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Alpha-1D adrenergic receptor;
DE AltName: Full=Alpha-1D adrenoreceptor;
DE Short=Alpha-1D adrenoceptor;
GN Name=ADRA1D;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Uhlen S., Wraith A.;
RT "Characterization of the pig alpha-1D adrenergic receptor.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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. Palmitoylation by ZDHHC21 may increase the
CC expression of the receptor and regulate downstream signaling.
CC {ECO:0000250|UniProtKB:P97714}.
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; AJ250492; CAB59347.1; -; Genomic_DNA.
DR EMBL; AJ250493; CAB59347.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001116545.1; NM_001123073.1.
DR AlphaFoldDB; Q9TTM9; -.
DR SMR; Q9TTM9; -.
DR STRING; 9823.ENSSSCP00000007601; -.
DR PaxDb; Q9TTM9; -.
DR Ensembl; ENSSSCT00035043847; ENSSSCP00035017550; ENSSSCG00035033096.
DR GeneID; 552898; -.
DR KEGG; ssc:552898; -.
DR CTD; 146; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9TTM9; -.
DR OrthoDB; 1095345at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA: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: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; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..571
FT /note="Alpha-1D adrenergic receptor"
FT /id="PRO_0000069075"
FT TOPO_DOM 1..94
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 95..120
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 121..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 133..158
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 159..168
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 169..191
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 192..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 213..237
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 238..250
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 251..274
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 275..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 349..373
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 374..380
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 381..405
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 406..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 13..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 419
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 571 AA; 60699 MW; BACFFB5C903972B1 CRC64;
MTFRDLLSVN FEGSRSDGSA GGASAGGSGG GSGGAAASEG RAVDGVPGTA GSGGVVGAGS
DENNRSSAGE PGAAGAGGEV NGTAAVGGLV VSAQGVGVGV FLAAFILMAV AGNLLVILSV
ACNRHLQTVT NYFIVNLAVA DLLLSATVLP FSATMEVLGF WAFGRAFCDV WAAVDVLCCT
ASILSLCTIS VDRYVGVRHS LKYPSIMTER KAAAILALLW AVAIVVSVGP LLGWKEPVPP
DERFCGITEE AGYAVFSSLC SFYLPMAVIV VMYCRVYVVA RSTTRSLEAG VKRERGKASE
VVLRIHCRGS STGTDRGHGA MRSTKGHTFR SSLSLRLLKF SREKKAAKTL AIVVGVFVLC
WFPFFFVLPL GSLFPQLKPS EGVFKVIFWL GYFNSCVNPL IYPCSSREFK RAFLRLLRCQ
CHHSRRRRRP LWRAYGHHWL ASNGGPRPDC APGLGAAPRE APLALPAPEA TDTPSAPEAQ
APVVGRRKPP YSFRDWRLLG PFRRPTTQLR AKVSSLSQKI RAGSAPCAEA PCALRSEVEA
VSLNVPHDAA EGATWQAYEL ADYSHLRETD I
