ID   AA1R_CANLF              Reviewed;         326 AA.
AC   P11616;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Adenosine receptor A1;
GN   Name=ADORA1; Synonyms=RDC7;
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=Thyroid;
RX   PubMed=2541503; DOI=10.1126/science.2541503;
RA   Libert F., Parmentier M., Lefort A., Dinsart C., van Sande J., Maenhaut C.,
RA   Simons M.-J., Dumont J.E., Vassart G.;
RT   "Selective amplification and cloning of four new members of the G protein-
RT   coupled receptor family.";
RL   Science 244:569-572(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=2159629; DOI=10.1093/nar/18.7.1915;
RA   Libert F., Parmentier M., Lefort A., Dumont J.E., Vassart G.;
RT   "Complete nucleotide sequence of a putative G protein coupled receptor:
RT   RDC7.";
RL   Nucleic Acids Res. 18:1915-1915(1990).
RN   [3]
RP   FUNCTION.
RX   PubMed=1646713; DOI=10.1002/j.1460-2075.1991.tb07691.x;
RA   Libert F., Schiffmann S.N., Lefort A., Parmentier M., Gerard C.,
RA   Dumont J.E., Vanderhaeghen J.-J., Vassart G.;
RT   "The orphan receptor cDNA RDC7 encodes an A1 adenosine receptor.";
RL   EMBO J. 10:1677-1682(1991).
CC   -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC       mediated by G proteins which inhibit adenylyl cyclase.
CC       {ECO:0000269|PubMed:1646713}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X14051; CAA32209.1; -; mRNA.
DR   PIR; C30341; C30341.
DR   RefSeq; NP_001003279.1; NM_001003279.1.
DR   RefSeq; XP_005622211.1; XM_005622154.2.
DR   RefSeq; XP_005622212.1; XM_005622155.2.
DR   AlphaFoldDB; P11616; -.
DR   SMR; P11616; -.
DR   STRING; 9615.ENSCAFP00000015121; -.
DR   PaxDb; P11616; -.
DR   Ensembl; ENSCAFT00030005877; ENSCAFP00030005209; ENSCAFG00030003141.
DR   Ensembl; ENSCAFT00040004537; ENSCAFP00040003897; ENSCAFG00040002391.
DR   Ensembl; ENSCAFT00845025394; ENSCAFP00845019987; ENSCAFG00845014197.
DR   GeneID; 403961; -.
DR   KEGG; cfa:403961; -.
DR   CTD; 134; -.
DR   VEuPathDB; HostDB:ENSCAFG00845014197; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234555; -.
DR   HOGENOM; CLU_009579_11_5_1; -.
DR   InParanoid; P11616; -.
DR   OMA; IWAVKMN; -.
DR   OrthoDB; 550297at2759; -.
DR   TreeFam; TF325296; -.
DR   Reactome; R-CFA-417973; Adenosine P1 receptors.
DR   Reactome; R-CFA-418594; G alpha (i) signalling events.
DR   Proteomes; UP000002254; Chromosome 7.
DR   Bgee; ENSCAFG00000010298; Expressed in temporal lobe and 34 other tissues.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0110148; P:biomineralization; IEA:Ensembl.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR   GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR   GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
DR   GO; GO:1900453; P:negative regulation of long-term synaptic depression; IEA:Ensembl.
DR   GO; GO:0070256; P:negative regulation of mucus secretion; IEA:Ensembl.
DR   GO; GO:0003093; P:regulation of glomerular filtration; IEA:Ensembl.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR   GO; GO:0014074; P:response to purine-containing compound; IEA:Ensembl.
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_0000068989"
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        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   326 AA;  36400 MW;  D55FCE6914AEA50E CRC64;
     MPPAISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVS LAVADVAVGA
     LVIPLAILIN IGPRTYFHTC LMVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKTVVT
     PRRAAVAIAG CWILSFVVGL TPLFGWNRLG EAQRAWAANG SGGEPVIKCE FEKVISMEYM
     VYFNFFVWVL PPLLLMVLIY LEVFYLIRRQ LGKKVSASSG DPQKYYGKEL KIAKSLALIL
     FLFALSWLPL HILNCITLFC PSCRKPSILM YIAIFLTHGN SAMNPIVYAF RIQKFRVTFL
     KIWNDHFRCQ PTPPVDEDPP EEAPHD