AA1R_RAT
ID AA1R_RAT Reviewed; 326 AA.
AC P25099;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Adenosine receptor A1;
GN Name=Adora1;
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 [MRNA].
RX PubMed=1658635; DOI=10.1210/mend-5-8-1037;
RA Reppert S.M., Weaver D.R., Stehle J.H., Rivkees S.A.;
RT "Molecular cloning and characterization of a rat A1-adenosine receptor that
RT is widely expressed in brain and spinal cord.";
RL Mol. Endocrinol. 5:1037-1048(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1857334;
RA Mahan L.C., McVittie L.D., Smyk-Randall E.M., Nakata H., Monsma F.J. Jr.,
RA Gerfen C.R., Sibley D.R.;
RT "Cloning and expression of an A1 adenosine receptor from rat brain.";
RL Mol. Pharmacol. 40:1-7(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Hirabatake Y., Takao K., Hagiwara S., Kasanuki H., Hosoda S., Kokubun S.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Yip L., Mourelatos K., Hewitt J., Kwok Y.N.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which inhibit adenylyl cyclase.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed in brain and spinal cord.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M69045; AAB07231.1; -; mRNA.
DR EMBL; M64299; AAA74471.1; -; mRNA.
DR EMBL; AB001089; BAA19231.1; -; mRNA.
DR EMBL; AF042079; AAC03772.1; -; mRNA.
DR PIR; A40376; A40376.
DR RefSeq; NP_058851.2; NM_017155.2.
DR RefSeq; XP_006249921.1; XM_006249859.3.
DR RefSeq; XP_006249923.1; XM_006249861.3.
DR AlphaFoldDB; P25099; -.
DR SMR; P25099; -.
DR BioGRID; 247960; 2.
DR IntAct; P25099; 1.
DR MINT; P25099; -.
DR STRING; 10116.ENSRNOP00000004602; -.
DR BindingDB; P25099; -.
DR ChEMBL; CHEMBL318; -.
DR DrugCentral; P25099; -.
DR GuidetoPHARMACOLOGY; 18; -.
DR GlyGen; P25099; 2 sites.
DR iPTMnet; P25099; -.
DR PhosphoSitePlus; P25099; -.
DR PaxDb; P25099; -.
DR PRIDE; P25099; -.
DR DNASU; 29290; -.
DR Ensembl; ENSRNOT00000004602; ENSRNOP00000004602; ENSRNOG00000003442.
DR GeneID; 29290; -.
DR KEGG; rno:29290; -.
DR UCSC; RGD:2048; rat.
DR CTD; 134; -.
DR RGD; 2048; Adora1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; P25099; -.
DR OMA; IWAVKMN; -.
DR OrthoDB; 550297at2759; -.
DR PhylomeDB; P25099; -.
DR TreeFam; TF325296; -.
DR Reactome; R-RNO-417973; Adenosine P1 receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P25099; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003442; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P25099; RN.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0030673; C:axolemma; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0044297; C:cell body; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO-UCL.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:BHF-UCL.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:RGD.
DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR GO; GO:0032795; F:heterotrimeric G-protein binding; IDA:RGD.
DR GO; GO:0099582; F:neurotransmitter receptor activity involved in regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0001883; F:purine nucleoside binding; IPI:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0110148; P:biomineralization; ISO:RGD.
DR GO; GO:0050890; P:cognition; IMP:RGD.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:0055089; P:fatty acid homeostasis; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IMP:RGD.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0042323; P:negative regulation of circadian sleep/wake cycle, non-REM sleep; IMP:RGD.
DR GO; GO:0042321; P:negative regulation of circadian sleep/wake cycle, sleep; IDA:RGD.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; IDA:RGD.
DR GO; GO:0045822; P:negative regulation of heart contraction; IMP:RGD.
DR GO; GO:0046888; P:negative regulation of hormone secretion; IMP:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; ISO:RGD.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:RGD.
DR GO; GO:1900453; P:negative regulation of long-term synaptic depression; ISO:RGD.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:0070256; P:negative regulation of mucus secretion; ISO:RGD.
DR GO; GO:0032900; P:negative regulation of neurotrophin production; IMP:RGD.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IMP:RGD.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IDA:RGD.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IDA:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:RGD.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IMP:RGD.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IDA:RGD.
DR GO; GO:0032244; P:positive regulation of nucleoside transport; IDA:RGD.
DR GO; GO:0002793; P:positive regulation of peptide secretion; IMP:RGD.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:RGD.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:RGD.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:RGD.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IDA:RGD.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:RGD.
DR GO; GO:0003093; P:regulation of glomerular filtration; ISO:RGD.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IMP:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:RGD.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IMP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IMP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; ISO:RGD.
DR GO; GO:0014074; P:response to purine-containing compound; ISO:RGD.
DR GO; GO:0001659; P:temperature homeostasis; IMP:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; IDA:RGD.
DR GO; GO:0042311; P:vasodilation; IDA:RGD.
DR InterPro; IPR001068; Adeno_A1_rcpt.
DR InterPro; IPR001634; Adenosn_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00552; ADENOSINEA1R.
DR PRINTS; PR00424; ADENOSINER.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Adenosine receptor A1"
FT /id="PRO_0000068994"
FT TOPO_DOM 1..10
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..69
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..146
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 309
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 229..230
FT /note="EL -> DV (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36695 MW; E43785CA993CFF15 CRC64;
MPPYISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVS LAVADVAVGA
LVIPLAILIN IGPQTYFHTC LMVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKTVVT
QRRAAVAIAG CWILSLVVGL TPMFGWNNLS VVEQDWRANG SVGEPVIKCE FEKVISMEYM
VYFNFFVWVL PPLLLMVLIY LEVFYLIRKQ LNKKVSASSG DPQKYYGKEL KIAKSLALIL
FLFALSWLPL HILNCITLFC PTCQKPSILI YIAIFLTHGN SAMNPIVYAF RIHKFRVTFL
KIWNDHFRCQ PKPPIDEDLP EEKAED