ADA1D_RABIT
ID ADA1D_RABIT Reviewed; 576 AA.
AC O02666;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Alpha-1D adrenergic receptor;
DE AltName: Full=Alpha-1D adrenoreceptor;
DE Short=Alpha-1D adrenoceptor;
GN Name=ADRA1D;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9030207; DOI=10.1016/s0005-2736(96)00229-5;
RA Suzuki F., Miyamoto S., Takita M., Oshita M., Watanabe Y., Kakizuka A.,
RA Narumiya S., Taniguchi T., Muramatsu I.;
RT "Cloning, functional expression and tissue distribution of rabbit alpha 1d-
RT adrenoceptor.";
RL Biochim. Biophys. Acta 1323:6-11(1997).
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; U64032; AAB53098.1; -; mRNA.
DR RefSeq; NP_001076147.1; NM_001082678.1.
DR AlphaFoldDB; O02666; -.
DR SMR; O02666; -.
DR GeneID; 100009398; -.
DR KEGG; ocu:100009398; -.
DR CTD; 146; -.
DR InParanoid; O02666; -.
DR OrthoDB; 1095345at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..576
FT /note="Alpha-1D adrenergic receptor"
FT /id="PRO_0000069076"
FT TOPO_DOM 1..101
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 102..126
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 127..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..164
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 165..174
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..197
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 198..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 219..243
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 244..256
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 257..280
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 281..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 354..378
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 379..385
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 386..410
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 411..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 424
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 576 AA; 60267 MW; 21EDF1025D0144CE CRC64;
MTFRDLLSVT FEGPRPDISA GGSGAGGGAG AGAGAGDTAS SESPAVGGVP GAAGGGGGGS
VVGAGSGEDN RSSAGEPGGA GGGGEVNGTA AVGGLVVSAQ SVGVGVFLAA FILTAVAGNL
LVILSVACNR HLQTVTNYFI VNLAVADLLL SATVLPFSAT MEVLGFWAFG RAFCDVWAAV
DVLCCTASIL SLCTISVDRY VGVRHSLKYP AIMTERKAAA ILALLWAVAL VVSMGPLLGW
KEPVPPDERF CGITEEVGYA VFSSLCSFYL PMAVIVVMYC RVYVVARSTT RSLEAGVKRE
RGKASEVVLR IHCRGAASGA DGAPGTRGAK GHTFRSSLSV RLLKFSREKK AAKTLAIVVG
VFVLCWFPFF FVLPLGSLFP QLKPSEGVFK VIFWLGYFNS CVNPLIYPCS SREFKRAFLR
LLRCQCRRRR RRRPLWRVYG HHWRASAGGG PHPDCALSAG AALPGAALAL TAAPAPSSAA
APEGQAAGAG RRKPPCAFRE WRLLGPLRRP TTQLRAKVSS LSHKIRAGGA QRAEAACALR
SEVEAVALSV ARDVAEDNTC QAYELADYRN LRETDI
