AA3R_SHEEP
ID AA3R_SHEEP Reviewed; 317 AA.
AC P35342;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Adenosine receptor A3;
GN Name=ADORA3;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary pars tuberalis;
RX PubMed=8396714;
RA Linden J., Taylor H.E., Robeva A.S., Tucker A.L., Stehle J.H.,
RA Rivkees S.A., Fink J.S., Reppert S.M.;
RT "Molecular cloning and functional expression of a sheep A3 adenosine
RT receptor with widespread tissue distribution.";
RL Mol. Pharmacol. 44:524-532(1993).
CC -!- FUNCTION: Receptor for adenosine. The activity of this receptor is
CC mediated by G proteins which inhibits adenylyl cyclase.
CC {ECO:0000269|PubMed:8396714}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28309};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Most abundant in lung, spleen and pineal gland.
CC Moderate expression in brain, kidney and testis.
CC {ECO:0000269|PubMed:8396714}.
CC -!- PTM: Phosphorylation on Thr-315 and Ser-316 may be crucial for rapid
CC desensitization. Phosphorylation on Thr-315 may be necessary for
CC phosphorylation on Ser-316 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; S65334; AAB28171.1; -; mRNA.
DR RefSeq; NP_001009775.2; NM_001009775.2.
DR AlphaFoldDB; P35342; -.
DR SMR; P35342; -.
DR STRING; 9940.ENSOARP00000021084; -.
DR BindingDB; P35342; -.
DR ChEMBL; CHEMBL3309064; -.
DR GeneID; 443330; -.
DR KEGG; oas:443330; -.
DR CTD; 140; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 550297at2759; -.
DR Proteomes; UP000002356; 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 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..317
FT /note="Adenosine receptor A3"
FT /id="PRO_0000069014"
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..176
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 177..197
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 198..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 231..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 255..260
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 261..283
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 284..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 302
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
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 83..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 317 AA; 36141 MW; CE362B80F9B8BE56 CRC64;
MPVNSTAVSW TSVTYITVEI LIGLCAIVGN VLVIWVVKLN PSLQTTTFYF IVSLALADIA
VGVLVMPLAI VISLGVTIHF YSCLFMTCLM LIFTHASIMS LLAIAVDRYL RVKLTVRYRR
VTTQRRIWLA LGLCWLVSFL VGLTPMFGWN MKLSSADENL TFLPCRFRSV MRMDYMVYFS
FFLWILVPLV VMCAIYFDIF YIIRNRLSQS FSGSRETGAF YGREFKTAKS LLLVLFLFAL
CWLPLSIINC ILYFDGQVPQ TVLYLGILLS HANSMMNPIV YAYKIKKFKE TYLLILKACV
MCQPSKSMDP STEQTSE
