AA1R_BOVIN
ID AA1R_BOVIN Reviewed; 326 AA.
AC P28190; A5PJR1; Q58D38;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Adenosine receptor A1;
GN Name=ADORA1;
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=1551415; DOI=10.1016/0014-5793(92)80338-h;
RA Tucker A.L., Linden J., Robeva A.S., D'Angelo D.D., Lynch K.R.;
RT "Cloning and expression of a bovine adenosine A1 receptor cDNA.";
RL FEBS Lett. 297:107-111(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1587851; DOI=10.1016/s0021-9258(19)50084-9;
RA Olah M.E., Ren H., Ostrowski J., Jacobson K., Stiles G.L.;
RT "Cloning, expression, and characterization of the unique bovine A1
RT adenosine receptor. Studies on the ligand binding site by site-directed
RT mutagenesis.";
RL J. Biol. Chem. 267:10764-10770(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons, and Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X63592; CAA45135.1; -; mRNA.
DR EMBL; M86261; AAA30350.1; -; mRNA.
DR EMBL; BT021759; AAX46606.1; -; mRNA.
DR EMBL; BC142208; AAI42209.1; -; mRNA.
DR EMBL; BC142265; AAI42266.1; -; mRNA.
DR PIR; A38144; A38144.
DR RefSeq; NP_776922.2; NM_174497.3.
DR RefSeq; XP_005216709.1; XM_005216652.3.
DR RefSeq; XP_005216710.1; XM_005216653.3.
DR RefSeq; XP_010811315.1; XM_010813013.2.
DR AlphaFoldDB; P28190; -.
DR SMR; P28190; -.
DR STRING; 9913.ENSBTAP00000015230; -.
DR BindingDB; P28190; -.
DR ChEMBL; CHEMBL4975; -.
DR DrugCentral; P28190; -.
DR PaxDb; P28190; -.
DR PRIDE; P28190; -.
DR Ensembl; ENSBTAT00000015230; ENSBTAP00000015230; ENSBTAG00000011461.
DR Ensembl; ENSBTAT00000072690; ENSBTAP00000071730; ENSBTAG00000011461.
DR GeneID; 282133; -.
DR KEGG; bta:282133; -.
DR CTD; 134; -.
DR VEuPathDB; HostDB:ENSBTAG00000011461; -.
DR VGNC; VGNC:25686; ADORA1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; P28190; -.
DR OMA; IWAVKMN; -.
DR OrthoDB; 550297at2759; -.
DR TreeFam; TF325296; -.
DR Reactome; R-BTA-417973; Adenosine P1 receptors.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR PRO; PR:P28190; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000011461; Expressed in pons and 76 other tissues.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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_0000068988"
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 212
FT /note="N -> S (in Ref. 1; CAA45135 and 2; AAA30350)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="V -> I (in Ref. 1; CAA45135 and 2; AAA30350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36593 MW; 6F4557FCEFEBC66E CRC64;
MPPSISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVS LAVADVAVGA
LVIPLAILIN IGPRTYFHTC LKVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKTVVT
PRRAVVAITG CWILSFVVGL TPMFGWNNLS AVERDWLANG SVGEPVIECQ FEKVISMEYM
VYFNFFVWVL PPLLLMVLIY MEVFYLIRKQ LNKKVSASSG DPQKYYGKEL KIAKSLALIL
FLFALSWLPL HILNCITLFC PSCHMPRILI YIAIFLSHGN SAMNPIVYAF RIQKFRVTFL
KIWNDHFRCQ PAPPVDEDAP AERPDD
