ADA1A_BOVIN
ID ADA1A_BOVIN Reviewed; 466 AA.
AC P18130;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 135.
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; Synonyms=ADRA1C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1970822; DOI=10.1016/s0021-9258(19)39055-6;
RA Schwinn D.A., Lomasney J.W., Lorenz W., Szklut P.J., Fremeau R.T. Jr.,
RA Yang-Feng T.L., Caron M.G., Lefkowitz R.J., Cotecchia S.;
RT "Molecular cloning and expression of the cDNA for a novel alpha 1-
RT adrenergic receptor subtype.";
RL J. Biol. Chem. 265:8183-8189(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1966743;
RA Schwinn D.A., Cotecchia S., Lorenz W., Caron M.G., Lefkowitz R.J.;
RT "The alpha 1C-adrenergic receptor: a new member in the alpha 1-adrenergic
RT receptor family.";
RL Trans. Assoc. Am. Physicians 103:112-118(1990).
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; J05426; AAA30374.1; -; mRNA.
DR PIR; A35375; A35375.
DR RefSeq; NP_776923.1; NM_174498.2.
DR AlphaFoldDB; P18130; -.
DR SMR; P18130; -.
DR STRING; 9913.ENSBTAP00000042306; -.
DR BindingDB; P18130; -.
DR ChEMBL; CHEMBL4892; -.
DR DrugCentral; P18130; -.
DR PaxDb; P18130; -.
DR GeneID; 282134; -.
DR KEGG; bta:282134; -.
DR CTD; 148; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P18130; -.
DR OrthoDB; 1095345at2759; -.
DR PRO; PR:P18130; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; 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; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Nucleus; Palmitate; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..466
FT /note="Alpha-1A adrenergic receptor"
FT /id="PRO_0000069060"
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..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 274..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..305
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 306..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 MOD_RES 215
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
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"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 466 AA; 51466 MW; 77635153B39E85EC CRC64;
MVFLSGNASD SSNCTHPPPP VNISKAILLG VILGGLILFG VLGNILVILS VACHRHLHSV
THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN VWAAVDVLCC TASIMGLCII
SIDRYIGVSY PLRYPTIVTQ KRGLMALLCV WALSLVISIG PLFGWRQPAP EDETICQINE
EPGYVLFSAL GSFYVPLTII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN
AQVGGSGVTS AKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPD
FRPSETVFKI AFWLGYLNSC INPIIYPCSS QEFKKAFQNV LRIQCLRRKQ SSKHTLGYTL
HAPSHVLEGQ HKDLVRIPVG SAETFYKISK TDGVCEWKIF SSLPRGSARM AVARDPSACT
TARVRSKSFL QVCCCLGPST PSHGENHQIP TIKIHTISLS ENGEEV
