ADA1A_ORYLA
ID ADA1A_ORYLA Reviewed; 470 AA.
AC Q91175;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Alpha-1A adrenergic receptor;
DE AltName: Full=Alpha-1A adrenoreceptor;
DE Short=Alpha-1A adrenoceptor;
DE AltName: Full=MAR1;
GN Name=adra1a;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8654394; DOI=10.1111/j.1432-1033.1996.00501.x;
RA Yasuoka A., Abe K., Arai S., Emori Y.;
RT "Molecular cloning and functional expression of the alpha1A-adrenoceptor of
RT Medaka fish, Oryzias latipes.";
RL Eur. J. Biochem. 235:501-507(1996).
CC -!- FUNCTION: This alpha-adrenergic receptor mediates its action by
CC association with G proteins that activate a phosphatidylinositol-
CC calcium second messenger system. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA1A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D63859; BAA09921.1; -; Genomic_DNA.
DR AlphaFoldDB; Q91175; -.
DR SMR; Q91175; -.
DR STRING; 8090.ENSORLP00000015226; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q91175; -.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
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; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Alpha-1A adrenergic receptor"
FT /id="PRO_0000069067"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 28..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 52..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..99
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 100..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 123..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 144..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 168..181
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 206..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 272..295
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 296..303
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 304..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 328..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 375..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 343
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 470 AA; 51925 MW; D4F7A83033061D4E CRC64;
MTPSSVTLNC SNCSHVLAPE LNTVKAVVLG MVLGIFILFG VIGNILVILS VVCHRHLQTV
TYYFIVNLAV ADLLLSSTVL PFSAIFEILD RWVFGRVFCN IWAAVDVLCC TASIMSLCVI
SVDRYIGVSY PLRYPAIMTK RRALLAVMLL WVLSVIISIG PLFGWKEPAP EDETVCKITE
EPGYAIFSAV GSFYLPLAII LAMYCRVYVV AQKESRGLKE GQKIEKSDSE QVILRMHRGN
TTVSEDEALR SRTHFALRLL KFSREKKAAK TLGIVVGCFV LCWLPFFLVL PIGSIFPAYR
PSDTVFKITF WLGYFNSCIN PIIYLCSNQE FKKAFQSLLG VHCLRMTPRA HHHHLSVGQS
QTQGHSLTIS LDSKGAPCRL SPSSSVALSR TPSSRDSREW RVFSGGPINS GPGPTEAGRA
KVAKLCNKSL HRTCCCILRA RTPTQDPAPL GDLPTIKIHQ LSLSEKGESV
