AA3R_BOVIN
ID AA3R_BOVIN Reviewed; 317 AA.
AC Q0VC81;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Adenosine receptor A3;
GN Name=ADORA3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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-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; BC120305; AAI20306.1; -; mRNA.
DR RefSeq; NP_001098081.1; NM_001104611.2.
DR RefSeq; NP_001289697.1; NM_001302768.1.
DR AlphaFoldDB; Q0VC81; -.
DR SMR; Q0VC81; -.
DR STRING; 9913.ENSBTAP00000010057; -.
DR BindingDB; Q0VC81; -.
DR ChEMBL; CHEMBL1287626; -.
DR PaxDb; Q0VC81; -.
DR Ensembl; ENSBTAT00000010057; ENSBTAP00000010057; ENSBTAG00000039738.
DR GeneID; 780806; -.
DR KEGG; bta:780806; -.
DR CTD; 140; -.
DR VEuPathDB; HostDB:ENSBTAG00000039738; -.
DR VGNC; VGNC:50194; TMIGD3.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00930000151073; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; Q0VC81; -.
DR OMA; INCITYF; -.
DR TreeFam; TF325296; -.
DR Reactome; R-BTA-417973; Adenosine P1 receptors.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000039738; Expressed in semen and 101 other tissues.
DR ExpressionAtlas; Q0VC81; baseline.
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_0000290008"
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 DISULFID 83..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 317 AA; 35911 MW; 4843F7A27DDF0907 CRC64;
MPVNSTAVSL ASVTYISVEI LIGLCAIVGN VLVIWVVKLN PSLQTTTFYF IVSLALADIA
VGVLVMPLAI VISLGVTIHF YSCLLMTCLL MIFTHASIMS LLAIAVDRYL RVKLTVRYRR
VTTQRRIWLA LGLCWLVSFL VGLTPMFGWN MKLSSADKNL TFLPCQFRSV MRMDYMVYFS
FFTWILIPLV VMCAIYFDIF YVIRNRLSQN FSGSKETGAF YGREFKTAKS LSLVLFLFAL
SWLPLSIINC IIYFNGEVPQ IVLYLGILLS HANSMMNPIV YAYKIKKFKE TYLLILKACV
ICQPSKSMDP SIEQTSE
