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ADA1D_RAT
ID   ADA1D_RAT               Reviewed;         561 AA.
AC   P23944; Q71UM4;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 140.
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;
DE   AltName: Full=RA42;
GN   Name=Adra1d; Synonyms=Adra1a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX   PubMed=1706716; DOI=10.1016/s0021-9258(18)38126-2;
RA   Lomasney J.W., Cotecchia S., Lorenz W., Leung W.-Y., Schwinn D.A.,
RA   Yang-Feng T.L., Brownstein M., Lefkowitz R.J., Caron M.G.;
RT   "Molecular cloning and expression of the cDNA for the alpha 1A-adrenergic
RT   receptor. The gene for which is located on human chromosome 5.";
RL   J. Biol. Chem. 266:6365-6369(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hippocampus;
RX   PubMed=1661838;
RA   Perez D.M., Piascik M.T., Graham R.M.;
RT   "Solution-phase library screening for the identification of rare clones:
RT   isolation of an alpha 1D-adrenergic receptor cDNA.";
RL   Mol. Pharmacol. 40:876-883(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7815325;
RA   Schwinn D.A., Johnston G.I., Page S.O., Mosley M.J., Wilson K.H.,
RA   Worman N.P., Campbell S., Fidock M.D., Furness L.M., Parry-Smith D.J.,
RA   Peter B., Bailey D.S.;
RT   "Cloning and pharmacological characterization of human alpha-1 adrenergic
RT   receptors: sequence corrections and direct comparison with other species
RT   homologues.";
RL   J. Pharmacol. Exp. Ther. 272:134-142(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
RX   PubMed=10570042; DOI=10.1124/mol.56.6.1152;
RA   Xin X., Yang N., Faber J.E.;
RT   "Platelet-derived growth factor-BB inhibits rat alpha1D-adrenergic receptor
RT   gene expression in vascular smooth muscle cells by inducing AP-2-like
RT   protein binding to alpha1D proximal promoter region.";
RL   Mol. Pharmacol. 56:1152-1161(1999).
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   -!- TISSUE SPECIFICITY: Vas deferens, hippocampus, cerebral cortex, aorta,
CC       brain stem, heart and spleen.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA63477.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M60654; AAA63477.1; ALT_FRAME; mRNA.
DR   EMBL; L31771; AAB59704.1; -; mRNA.
DR   EMBL; AF071014; AAC25396.1; -; Genomic_DNA.
DR   PIR; A38731; A38731.
DR   RefSeq; NP_077809.1; NM_024483.1.
DR   AlphaFoldDB; P23944; -.
DR   SMR; P23944; -.
DR   STRING; 10116.ENSRNOP00000028877; -.
DR   BindingDB; P23944; -.
DR   ChEMBL; CHEMBL326; -.
DR   DrugCentral; P23944; -.
DR   GuidetoPHARMACOLOGY; 24; -.
DR   GlyGen; P23944; 2 sites.
DR   PhosphoSitePlus; P23944; -.
DR   PaxDb; P23944; -.
DR   GeneID; 29413; -.
DR   KEGG; rno:29413; -.
DR   UCSC; RGD:62064; rat.
DR   CTD; 146; -.
DR   RGD; 62064; Adra1d.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P23944; -.
DR   OrthoDB; 1095345at2759; -.
DR   PhylomeDB; P23944; -.
DR   Reactome; R-RNO-390696; Adrenoceptors.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR   PRO; PR:P23944; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004937; F:alpha1-adrenergic receptor activity; IDA:RGD.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007568; P:aging; IDA:RGD.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0060073; P:micturition; IMP:RGD.
DR   GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR   GO; GO:0001986; P:negative regulation of the force of heart contraction involved in baroreceptor response to increased systemic arterial blood pressure; ISO:RGD.
DR   GO; GO:0150099; P:neuron-glial cell signaling; ISO:RGD.
DR   GO; GO:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; ISO:RGD.
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; IMP:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
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..561
FT                   /note="Alpha-1D adrenergic receptor"
FT                   /id="PRO_0000069077"
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..561
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          10..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..480
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"
SQ   SEQUENCE   561 AA;  59354 MW;  B6537DCAD4F7BE27 CRC64;
     MTFRDILSVT FEGPRSSSST GGSGAGGGAG TVGPEGGAVG GVPGATGGGA VVGTGSGEDN
     QSSTGEPGAA ASGEVNGSAA VGGLVVSAQG VGVGVFLAAF ILTAVAGNLL VILSVACNRH
     LQTVTNYFIV NLAVADLLLS AAVLPFSATM EVLGFWAFGR TFCDVWAAVD VLCCTASILS
     LCTISVDRYV GVRHSLKYPA IMTERKAAAI LALLWAVALV VSVGPLLGWK EPVPPDERFC
     GITEEVGYAI FSSVCSFYLP MAVIVVMYCR VYVVARSTTR SLEAGIKREP GKASEVVLRI
     HCRGAATSAK GYPGTQSSKG HTLRSSLSVR LLKFSREKKA AKTLAIVVGV FVLCWFPFFF
     VLPLGSLFPQ LKPSEGVFKV IFWLGYFNSC VNPLIYPCSS REFKRAFLRL LRCQCRRRRR
     RLWAVYGHHW RASTGDARSD CAPSPRIAPP GAPLALTAHP GAGSADTPET QDSVSSSRKP
     ASALREWRLL GPLQRPTTQL RAKVSSLSHK IRSGARRAET ACALRSEVEA VSLNVPQDGA
     EAVICQAYEP GDYSNLRETD I
 
 
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