ADA1A_CANLF
ID ADA1A_CANLF Reviewed; 295 AA.
AC O77621;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 123.
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;
DE Flags: Fragment;
GN Name=ADRA1A; Synonyms=ADRA1C;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Prostate;
RX PubMed=11046098;
RA Argyle S.A., McGrath J.C.;
RT "An alpha(1A)/alpha(1L)-adrenoceptor mediates contraction of canine
RT subcutaneous resistance arteries.";
RL J. Pharmacol. Exp. Ther. 295:627-633(2000).
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; AF068283; AAC23861.1; -; mRNA.
DR AlphaFoldDB; O77621; -.
DR SMR; O77621; -.
DR STRING; 9612.ENSCAFP00000012820; -.
DR BindingDB; O77621; -.
DR PaxDb; O77621; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; O77621; -.
DR Proteomes; UP000002254; 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; Membrane; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..>295
FT /note="Alpha-1A adrenergic receptor"
FT /id="PRO_0000069061"
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..>295
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="Phosphoserine; by PKA"
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"
FT NON_TER 295
SQ SEQUENCE 295 AA; 32254 MW; 20DB7DA0797A474C CRC64;
MVFLSGNASD SSNCTHPPAP VNISKAILLG VILGGLIIFG VLGNILVILS VACHRHLHSV
THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN IWAAVDVLCC TASIMGLCII
SIDRYIGVSY PLRYPTIVTQ KRGLMALLCV WALSLVISIG PLFGWRQPAP EDETICQITE
EPGYVLFSAL GSFYVPLTII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN
APVGGTGVSS AKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIG
