ID   TA2R_RAT                Reviewed;         341 AA.
AC   P34978;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Thromboxane A2 receptor;
DE            Short=TXA2-R;
DE   AltName: Full=Prostanoid TP receptor;
DE   AltName: Full=TXR2;
GN   Name=Tbxa2r;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=7635958; DOI=10.1172/jci118108;
RA   Abe T., Takeuchi K., Takahashi N., Tsutsumi E., Taniyama Y., Abe K.;
RT   "Rat kidney thromboxane receptor: molecular cloning, signal transduction,
RT   and intrarenal expression localization.";
RL   J. Clin. Invest. 96:657-664(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=7696353; DOI=10.1016/0167-4889(94)00225-4;
RA   Kitanaka J., Hashimoto H., Sugimoto Y., Sawada M., Negishi M., Suzumura A.,
RA   Marunouchi T., Ichikawa A., Baba A.;
RT   "cDNA cloning of a thromboxane A2 receptor from rat astrocytes.";
RL   Biochim. Biophys. Acta 1265:220-223(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=8936585; DOI=10.1016/s0090-6980(96)00091-3;
RA   D'Angelo D.D., Terasawa T., Carlisle S.J., Dorn G.W. II, Lynch K.R.;
RT   "Characterization of a rat kidney thromboxane A2 receptor: high affinity
RT   for the agonist ligand I-BOP.";
RL   Prostaglandins 52:303-316(1996).
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   -!- TISSUE SPECIFICITY: In the brain, expressed in all types of glial
CC       cells. In the kidney, expressed in the mesangial cells of the
CC       glomerulus, smooth muscle cells of the renal arterioles, and in
CC       transitional cell epithelium of renal pelvis.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; D21158; BAA04694.1; -; mRNA.
DR   EMBL; D32080; BAA06844.1; -; mRNA.
DR   PIR; I55623; I55623.
DR   RefSeq; NP_058750.1; NM_017054.1.
DR   RefSeq; XP_006240908.1; XM_006240846.2.
DR   AlphaFoldDB; P34978; -.
DR   SMR; P34978; -.
DR   DIP; DIP-60433N; -.
DR   IntAct; P34978; 1.
DR   STRING; 10116.ENSRNOP00000027932; -.
DR   BindingDB; P34978; -.
DR   ChEMBL; CHEMBL3156; -.
DR   GuidetoPHARMACOLOGY; 346; -.
DR   GlyGen; P34978; 2 sites.
DR   PhosphoSitePlus; P34978; -.
DR   PaxDb; P34978; -.
DR   Ensembl; ENSRNOT00000027932; ENSRNOP00000027932; ENSRNOG00000020585.
DR   GeneID; 24816; -.
DR   KEGG; rno:24816; -.
DR   UCSC; RGD:3825; rat.
DR   CTD; 6915; -.
DR   RGD; 3825; Tbxa2r.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234559; -.
DR   HOGENOM; CLU_045991_3_0_1; -.
DR   InParanoid; P34978; -.
DR   OMA; ASVCWMP; -.
DR   OrthoDB; 972015at2759; -.
DR   PhylomeDB; P34978; -.
DR   TreeFam; TF324982; -.
DR   Reactome; R-RNO-391908; Prostanoid ligand receptors.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR   Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR   PRO; PR:P34978; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000020585; Expressed in thymus and 19 other tissues.
DR   Genevisible; P34978; RN.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0004961; F:thromboxane A2 receptor activity; IBA:GO_Central.
DR   GO; GO:0004960; F:thromboxane receptor activity; IDA:RGD.
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; IMP:RGD.
DR   GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IDA:RGD.
DR   GO; GO:0030194; P:positive regulation of blood coagulation; IMP:RGD.
DR   GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:RGD.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR   GO; GO:0019229; P:regulation of vasoconstriction; ISO:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0019932; P:second-messenger-mediated signaling; ISO:RGD.
DR   GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0030104; P:water homeostasis; TAS:RGD.
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   2: Evidence at transcript 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_0000070140"
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:0000250|UniProtKB:P30987"
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"
FT   CONFLICT        188
FT                   /note="E -> G (in Ref. 2; BAA06844)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   341 AA;  36928 MW;  E85843FE54C1CD94 CRC64;
     MWLNSTSLGA CFRPVNITLQ ERRAIASPWF AASFCALGLG SNLLALSVLA GARPGAGPRS
     SFLALLCGLV LTDFLGLLVT GAVVASQHAA LLDWRATDPG CRLCHFMGAA MVFFGLCPLL
     LGAAMAAERF VGITRPFSRP AATSRRAWAT VGLVWVGAGT LGLLPLLGLG RYSVQYPGSW
     CFLTLGAERG DVAFGLMFAL LGSVSVGLSL LLNTVSVATL CRVYHAREAT QRPRDCEVEM
     MVQLVGIMVV ATVCWMPLLV FILQTLLQTL PVMSPSGQLL RTTERQLLIY LRVATWNQIL
     DPWVYILFRR SVLRRLHPRF TSQLQAVSLH SPPTQAMLSG P