ADA1A_CAVPO
ID ADA1A_CAVPO Reviewed; 466 AA.
AC Q9WU25;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Alpha-1A adrenergic receptor;
DE AltName: Full=Alpha-1A adrenoreceptor;
DE Short=Alpha-1A adrenoceptor;
DE AltName: Full=Alpha-1C adrenergic receptor;
GN Name=ADRA1A;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=11527538; DOI=10.1016/s0014-2999(01)01217-1;
RA Gonzalez-Espinosa C., Romero-Avila M.T., Mora-Rodriguez D.M.,
RA Gonzalez-Espinosa D., Garcia-Sainz J.A.;
RT "Molecular cloning and functional expression of the guinea pig alpha(1a)-
RT adrenoceptor.";
RL Eur. J. Pharmacol. 426:147-155(2001).
CC -!- FUNCTION: This alpha-adrenergic receptor mediates its action by
CC association with G proteins that activate a phosphatidylinositol-
CC calcium second messenger system. Its effect is mediated by G(q) and
CC G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate
CC phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homo- and heterooligomer. Heterooligomerizes with ADRA1B
CC homooligomers in cardiac myocytes. Interacts with CAVIN4.
CC {ECO:0000250|UniProtKB:P35348}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein.
CC Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}.
CC Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the
CC nuclear membrane facilitates heterooligomerization and regulates ERK-
CC mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as
CC well as LAP2 at the nuclear membrane of cardiac myocytes (By
CC similarity). {ECO:0000250}.
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; AF108016; AAD22540.2; -; mRNA.
DR RefSeq; NP_001166383.1; NM_001172912.1.
DR AlphaFoldDB; Q9WU25; -.
DR SMR; Q9WU25; -.
DR STRING; 10141.ENSCPOP00000003324; -.
DR BindingDB; Q9WU25; -.
DR ChEMBL; CHEMBL2150843; -.
DR GeneID; 100135474; -.
DR CTD; 148; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9WU25; -.
DR PRO; PR:Q9WU25; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR001004; ADRA1A_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00557; ADRENRGCA1AR.
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; Cytoplasm; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Nucleus; Palmitate; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..466
FT /note="Alpha-1A adrenergic receptor"
FT /id="PRO_0000069062"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 52..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 64..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..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..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 169..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..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 273..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..304
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 305..329
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 330..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 334..349
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT LIPID 345
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 466 AA; 51578 MW; E0E27E4FF5D3D0CD CRC64;
MVFLSGNASD SSNCTQPPAP VNIPKAILLG VILGVLILFG VPGNILVILS VACHRHLHSV
THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN IWAAVDVLCC TASIMSLCII
SIDRYIGVSY PLRYPTIVTQ RRGLRALLCL WALSLVISIG PLFGWRQPAP QDETICQINE
DPSYVLFSAL GSFYVPLAII LVMYCRVYVV AKRESRGLTS GLKTDKSDSE QVTLRIHRKN
APLGGSGVAS SKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPD
FKPSETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LKIQCLRRKQ SSKHALGYTL
HPPSQAVEGQ HKDMVRIPVG SRETFYKISK TDGVCEWKFF SSMPRGSARI TVPKDQSACT
TARVRSKSFL QVCCCVGPST PNPGENHQVP TIKIHTISLS ENGEEV
