AA3R_CANLF
ID AA3R_CANLF Reviewed; 314 AA.
AC Q28309;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Adenosine receptor A3;
GN Name=ADORA3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9351976; DOI=10.1124/mol.52.5.846;
RA Auchampach J.A., Jin X., Wan T.C., Caughey G.H., Linden J.;
RT "Canine mast cell adenosine receptors: cloning and expression of the A3
RT receptor and evidence that degranulation is mediated by the A2B receptor.";
RL Mol. Pharmacol. 52:846-860(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:9351976}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9351976};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U54792; AAB03503.1; -; mRNA.
DR RefSeq; NP_001003178.1; NM_001003178.1.
DR AlphaFoldDB; Q28309; -.
DR SMR; Q28309; -.
DR STRING; 9612.ENSCAFP00000031533; -.
DR BindingDB; Q28309; -.
DR ChEMBL; CHEMBL3611963; -.
DR PaxDb; Q28309; -.
DR Ensembl; ENSCAFT00030038007; ENSCAFP00030033162; ENSCAFG00030020709.
DR Ensembl; ENSCAFT00040026920; ENSCAFP00040023393; ENSCAFG00040014600.
DR Ensembl; ENSCAFT00845014825; ENSCAFP00845011489; ENSCAFG00845008429.
DR GeneID; 403805; -.
DR KEGG; cfa:403805; -.
DR CTD; 140; -.
DR VEuPathDB; HostDB:ENSCAFG00845008429; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234555; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; Q28309; -.
DR OMA; INCITYF; -.
DR OrthoDB; 550297at2759; -.
DR TreeFam; TF325296; -.
DR Reactome; R-CFA-417973; Adenosine P1 receptors.
DR Reactome; R-CFA-418594; G alpha (i) signalling events.
DR Proteomes; UP000002254; Chromosome 17.
DR Bgee; ENSCAFG00000013692; Expressed in granulocyte and 42 other tissues.
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:0001973; P:G protein-coupled adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
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; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..314
FT /note="Adenosine receptor A3"
FT /id="PRO_0000069009"
FT TOPO_DOM 1..14
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 15..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 38..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..72
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 73..84
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..106
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 127..148
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 149..177
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 178..198
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 199..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 232..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 256..261
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 262..284
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 285..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 303
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 314 AA; 35903 MW; 62BB04E558BA102A CRC64;
MAVNGTALLL ANVTYITVEI LIGLCAIVGN VLVIWVVKLN PSLQTTTFYF IVSLALADIA
VGVLVMPLAI VISLGITIQF YNCLFMTCLL LIFTHASIMS LLAIAVDRYL RVKLTVRYRR
VTTQRRIWLA LGLCWLVSFL VGLTPMFGWN MKLTSEHQRN VTFLSCQFSS VMRMDYMVYF
SFFTWILIPL VVMCAIYLDI FYVIRNKLNQ NFSSSKETGA FYGREFKTAK SLFLVLFLFA
FSWLPLSIIN CITYFHGEVP QIILYLGILL SHANSMMNPI VYAYKIKKFK ETYLLIFKTY
MICQSSDSLD SSTE
