AA3R_MOUSE
ID AA3R_MOUSE Reviewed; 319 AA.
AC Q61618; Q9R202;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Adenosine receptor A3;
DE AltName: Full=A3AR;
GN Name=Adora3; Synonyms=Gpcr2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10191095; DOI=10.1006/geno.1998.5696;
RA Zhao Z., Francis C., Ravid K.;
RT "Characterization of the mouse A3 adenosine receptor gene: exon/intron
RT organization and promoter activity.";
RL Genomics 57:152-155(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-239.
RC TISSUE=Testis;
RX PubMed=8288218; DOI=10.1006/geno.1993.1452;
RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I.,
RA Copeland N.G., Jenkins N.A.;
RT "Identification, chromosomal location, and genome organization of mammalian
RT G-protein-coupled receptors.";
RL Genomics 18:175-184(1993).
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which inhibits adenylyl cyclase.
CC {ECO:0000250|UniProtKB:P0DMS8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28309};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylation on Thr-317 and Thr-318 may be crucial for rapid
CC desensitization. Phosphorylation on Thr-317 may be necessary for
CC phosphorylation on Thr-318 to occur. {ECO:0000250|UniProtKB:P28647}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF069778; AAC82643.1; -; Genomic_DNA.
DR EMBL; L20331; AAA16851.1; -; mRNA.
DR CCDS; CCDS17712.1; -.
DR PIR; B48909; B48909.
DR AlphaFoldDB; Q61618; -.
DR SMR; Q61618; -.
DR STRING; 10090.ENSMUSP00000000574; -.
DR BindingDB; Q61618; -.
DR ChEMBL; CHEMBL1075269; -.
DR GuidetoPHARMACOLOGY; 21; -.
DR GlyGen; Q61618; 3 sites.
DR iPTMnet; Q61618; -.
DR PhosphoSitePlus; Q61618; -.
DR PaxDb; Q61618; -.
DR PRIDE; Q61618; -.
DR MGI; MGI:104847; Adora3.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q61618; -.
DR PhylomeDB; Q61618; -.
DR Reactome; R-MMU-417973; Adenosine P1 receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR PRO; PR:Q61618; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61618; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:MGI.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0002553; P:histamine secretion by mast cell; IDA:MGI.
DR GO; GO:0043303; P:mast cell degranulation; IDA:MGI.
DR GO; GO:0070254; P:mucus secretion; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:MGI.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:MGI.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI.
DR InterPro; IPR000466; Adeno_A3_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; PR00555; ADENOSINEA3R.
DR PRINTS; PR00424; ADENOSINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..319
FT /note="Adenosine receptor A3"
FT /id="PRO_0000069011"
FT TOPO_DOM 1..15
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 16..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 39..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 74..85
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 86..107
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 108..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 128..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 150..178
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 179..199
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 200..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 233..256
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 257..262
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 263..285
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 286..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 304
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 184
FT /note="I -> V (in Ref. 2; AAA16851)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="I -> V (in Ref. 2; AAA16851)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="T -> S (in Ref. 2; AAA16851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36449 MW; 6AD7F46A9F03D9CC CRC64;
MEADNTTETD WLNITYITME AAIGLCAVVG NMLVIWVVKL NPTLRTTTVY FIVSLALADI
AVGVLVIPLA IAVSLQVKMH FYACLFMSCV LLIFTHASIM SLLAIAVHRY LRVKLTVRYR
TVTTQRRIWL FLGLCWLVSF LVGLTPMFGW NRKATLASSQ NSSTLLCHFR SVVSLDYMVF
FSFITWILVP LVVMCIIYLD IFYIIRNKLS QNLTGFRETR AFYGREFKTA KSLFLVLFLF
ALCWLPLSII NFVSYFDVKI PDVAMCLGIL LSHANSMMNP IVYACKIKKF KETYFLILRA
VRLCQTSDSL DSNMEQTTE
