TA2R_MOUSE
ID TA2R_MOUSE Reviewed; 341 AA.
AC P30987;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Thromboxane A2 receptor;
DE Short=TXA2-R;
DE AltName: Full=Prostanoid TP receptor;
GN Name=Tbxa2r;
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 [MRNA].
RC STRAIN=ddY; TISSUE=Lung;
RX PubMed=1375456; DOI=10.1016/s0006-291x(05)80009-9;
RA Namba T., Sugimoto Y., Hirata M., Hayashi Y., Honda A., Watabe A.,
RA Negishi M., Ichikawa A., Narumiya S.;
RT "Mouse thromboxane A2 receptor: cDNA cloning, expression and northern blot
RT analysis.";
RL Biochem. Biophys. Res. Commun. 184:1197-1203(1992).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for thromboxane A2 (TXA2), a potent stimulator of
CC platelet aggregation. The activity of this receptor is mediated by a G-
CC protein that activates a phosphatidylinositol-calcium second messenger
CC system. In the kidney, the binding of TXA2 to glomerular TP receptors
CC causes intense vasoconstriction. Activates phospholipase C and adenylyl
CC cyclase.
CC -!- SUBUNIT: Interacts with RPGRIP1L. Interacts with RACK1; the interaction
CC regulates TBXA2R cell surface expression (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D10849; BAA01622.1; -; mRNA.
DR CCDS; CCDS24053.1; -.
DR PIR; JH0606; JH0606.
DR RefSeq; NP_001264194.1; NM_001277265.1.
DR RefSeq; NP_033351.1; NM_009325.4.
DR RefSeq; XP_006513523.1; XM_006513460.3.
DR AlphaFoldDB; P30987; -.
DR SMR; P30987; -.
DR STRING; 10090.ENSMUSP00000100962; -.
DR BindingDB; P30987; -.
DR ChEMBL; CHEMBL1795181; -.
DR DrugCentral; P30987; -.
DR GuidetoPHARMACOLOGY; 346; -.
DR GlyGen; P30987; 2 sites.
DR iPTMnet; P30987; -.
DR PhosphoSitePlus; P30987; -.
DR jPOST; P30987; -.
DR PaxDb; P30987; -.
DR PRIDE; P30987; -.
DR ProteomicsDB; 259335; -.
DR Antibodypedia; 5899; 188 antibodies from 29 providers.
DR DNASU; 21390; -.
DR Ensembl; ENSMUST00000105325; ENSMUSP00000100962; ENSMUSG00000034881.
DR Ensembl; ENSMUST00000220312; ENSMUSP00000151447; ENSMUSG00000034881.
DR GeneID; 21390; -.
DR KEGG; mmu:21390; -.
DR UCSC; uc007ghg.2; mouse.
DR CTD; 6915; -.
DR MGI; MGI:98496; Tbxa2r.
DR VEuPathDB; HostDB:ENSMUSG00000034881; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234559; -.
DR HOGENOM; CLU_045991_3_0_1; -.
DR InParanoid; P30987; -.
DR OMA; ASVCWMP; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P30987; -.
DR TreeFam; TF324982; -.
DR Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR BioGRID-ORCS; 21390; 4 hits in 74 CRISPR screens.
DR PRO; PR:P30987; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P30987; protein.
DR Bgee; ENSMUSG00000034881; Expressed in thymus and 83 other tissues.
DR ExpressionAtlas; P30987; baseline and differential.
DR Genevisible; P30987; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004961; F:thromboxane A2 receptor activity; IBA:GO_Central.
DR GO; GO:0004960; F:thromboxane receptor activity; IDA:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0019229; P:regulation of vasoconstriction; IGI:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IDA:MGI.
DR GO; GO:0006939; P:smooth muscle contraction; IDA:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR008365; Prostanoid_rcpt.
DR InterPro; IPR001105; Thbox_rcpt.
DR PANTHER; PTHR11866; PTHR11866; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00429; THROMBOXANER.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..341
FT /note="Thromboxane A2 receptor"
FT /id="PRO_0000070139"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 341 AA; 37098 MW; F090F027E7D1F234 CRC64;
MWPNGTSLGA CFRPVNITLQ ERRAIASPWF AASFCALGLG SNLLALSVLA GARPGAGPRS
SFLALLCGLV LTDFLGLLVT GAIVASQHAA LLDWRATDPS CRLCYFMGVA MVFFGLCPLL
LGAAMASERF VGITRPFSRP TATSRRAWAT VGLVWVAAGA LGLLPLLGLG RYSVQYPGSW
CFLTLGTQRG DVVFGLIFAL LGSASVGLSL LLNTVSVATL CRVYHTREAT QRPRDCEVEM
MVQLVGIMVV ATVCWMPLLV FIMQTLLQTP PVMSFSGQLL RATEHQLLIY LRVATWNQIL
DPWVYILFRR SVLRRLHPRF SSQLQAVSLR RPPAQAMLSG P