AA1R_CAVPO
ID AA1R_CAVPO Reviewed; 326 AA.
AC P47745;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Adenosine receptor A1;
GN Name=ADORA1;
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 STRAIN=Hartley; TISSUE=Brain;
RX PubMed=7854041; DOI=10.1016/0169-328x(94)90085-x;
RA Meng F., Xie G.X., Chalmers D., Morgan C., Watson S.J. Jr., Akil H.;
RT "Cloning and characterization of a pharmacologically distinct A1 adenosine
RT receptor from guinea pig brain.";
RL Brain Res. Mol. Brain Res. 26:143-155(1994).
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U04279; AAB60505.1; -; mRNA.
DR PIR; I48096; I48096.
DR RefSeq; NP_001166382.1; NM_001172911.1.
DR RefSeq; XP_013013249.1; XM_013157795.1.
DR RefSeq; XP_013013250.1; XM_013157796.1.
DR RefSeq; XP_013013251.1; XM_013157797.1.
DR RefSeq; XP_013013252.1; XM_013157798.1.
DR AlphaFoldDB; P47745; -.
DR SMR; P47745; -.
DR DIP; DIP-440N; -.
DR STRING; 10141.ENSCPOP00000004686; -.
DR BindingDB; P47745; -.
DR ChEMBL; CHEMBL2304404; -.
DR DrugCentral; P47745; -.
DR Ensembl; ENSCPOT00000045914; ENSCPOP00000025301; ENSCPOG00000032582.
DR Ensembl; ENSCPOT00000047692; ENSCPOP00000029279; ENSCPOG00000032582.
DR GeneID; 100135472; -.
DR KEGG; cpoc:100135472; -.
DR CTD; 134; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; P47745; -.
DR OMA; IWAVKMN; -.
DR OrthoDB; 550297at2759; -.
DR TreeFam; TF325296; -.
DR PRO; PR:P47745; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000032582; Expressed in frontal cortex and 12 other tissues.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IEA:InterPro.
DR GO; GO:0110148; P:biomineralization; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
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_0000068990"
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; 36493 MW; A2E8D594F5D6A233 CRC64;
MPHSVSAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIAS LAVADVAVGA
LVIPLAILIN IGPQTYFHTC LMVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKTVVT
PRRAAVAIAG CWILSLVVGL TPMFGWNNLS KIEMAWAANG SVGEPVIKCE FEKVISMEYM
VYFNFFVWVL PPLLLMVLIY LEVFYLIRKQ LSKKVSASSG DPQKYYGKEL KIAKSLALIL
FLFALSWLPL HILNCITLFC PTCHKPTILT YIAIFLTHGN SAMNPIVYAF RIQKFRVTFL
KIWNDHFRCQ PEPPIDEDLP EEKVDD
