AA1R_RABIT
ID AA1R_RABIT Reviewed; 328 AA.
AC P34970;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Adenosine receptor A1;
GN Name=ADORA1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8514195; DOI=10.1016/0378-1119(93)90576-o;
RA Bhattacharya S., Dewitt D.L., Burnatowska-Hledin M., Smith W.L.,
RA Spielman W.S.;
RT "Cloning of an adenosine A1 receptor-encoding gene from rabbit.";
RL Gene 128:285-288(1993).
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; L01700; AAA31148.1; -; mRNA.
DR PIR; JN0675; JN0675.
DR RefSeq; NP_001164544.1; NM_001171073.1.
DR AlphaFoldDB; P34970; -.
DR SMR; P34970; -.
DR STRING; 9986.ENSOCUP00000009475; -.
DR BindingDB; P34970; -.
DR ChEMBL; CHEMBL3947; -.
DR PRIDE; P34970; -.
DR Ensembl; ENSOCUT00000011015; ENSOCUP00000009475; ENSOCUG00000011017.
DR GeneID; 100328615; -.
DR KEGG; ocu:100328615; -.
DR CTD; 134; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR InParanoid; P34970; -.
DR OrthoDB; 550297at2759; -.
DR Proteomes; UP000001811; Chromosome 16.
DR Bgee; ENSOCUG00000011017; Expressed in brain and 17 other tissues.
DR ExpressionAtlas; P34970; baseline.
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..328
FT /note="Adenosine receptor A1"
FT /id="PRO_0000068993"
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..328
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 328 AA; 36556 MW; 0F9B53E6AEC25968 CRC64;
MPPSISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVS LAVADVAVGA
LVIPLAILIN IGPETYFHTC LMVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKAVVT
PRRAAVAIAG CWILSLVVGL TPMFGWNNLR EVQRAWAANG SVGEPVIKCE FEKVISMEYM
VYFNFFVWVL PPLLLMVLIY LEVFYLIRRQ LSKKASASSG DPHKYYGKEL KIAKSLALIL
FLFALSWLPL HILNCVTLFC PSCQKPSILV YTAIFLTHGN SAMNPIVYAF RIHKFRVTFL
KIWNDHFRCR PAPAGDGDED LPEEKPND
