ID   AA3R_RABIT              Reviewed;         319 AA.
AC   O02667;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Adenosine receptor A3;
GN   Name=ADORA3;
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], AND FUNCTION.
RC   TISSUE=Lung;
RX   PubMed=8996189;
RA   Hill R.J., Oleynek J.J., Hoth C.F., Kiron M.A., Weng W., Wester R.T.,
RA   Tracey W.R., Knight D.R., Buchholz R.A., Kennedy S.P.;
RT   "Cloning, expression and pharmacological characterization of rabbit
RT   adenosine A1 and A3 receptors.";
RL   J. Pharmacol. Exp. Ther. 280:122-128(1997).
CC   -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC       mediated by G proteins which inhibits adenylyl cyclase.
CC       {ECO:0000269|PubMed:8996189}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28309};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- PTM: Phosphorylation on Ser-318 may be crucial for rapid
CC       desensitization. {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; U90718; AAB50560.1; -; mRNA.
DR   AlphaFoldDB; O02667; -.
DR   SMR; O02667; -.
DR   STRING; 9986.ENSOCUP00000017694; -.
DR   BindingDB; O02667; -.
DR   ChEMBL; CHEMBL2603; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; O02667; -.
DR   Proteomes; UP000001811; Unplaced.
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:0010646; P:regulation of cell communication; IEA:UniProt.
DR   GO; GO:0023051; P:regulation of signaling; IEA:UniProt.
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   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; Phosphoprotein; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..319
FT                   /note="Adenosine receptor A3"
FT                   /id="PRO_0000069012"
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        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        84..167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   319 AA;  36307 MW;  BB82C34B1AF96500 CRC64;
     MPDNSTTLFL AIRASYIVFE IVIGVCAVVG NVLVIWVIKL NPSLKTTTFY FIFSLALADI
     AVGFLVMPLA IVISLGITIG FYSCLVMSCL LLVFTHASIM SLLAIAVDRY LRVKLTVRYR
     RVTTQRRIWL ALGLCWVVSL LVGFTPMFGW NMKPTLESAR NYSDFQCKFD SVIPMEYMVF
     FSFFTWILIP LLLMCALYVY IFYIIRNKLV QSFSSFKETG AFYRREFKTA KSLFLVLALF
     AGCWLPLSII NCVTYFKCKV PDVVLLVGIL LSHANSMMNP IVYACKIQKF KETYLLIFKA
     RVTCQPSDSL DPSSEQNSE