ID   TA2R_CHLAE              Reviewed;         343 AA.
AC   P56486;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Thromboxane A2 receptor;
DE            Short=TXA2-R;
DE   AltName: Full=Prostanoid TP receptor;
GN   Name=TBXA2R;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9622606; DOI=10.1016/s0167-4889(98)00019-6;
RA   Becker K.P., Ullian M., Halushka P.V.;
RT   "Cloning and characterization of an endogenous COS-7 cell thromboxane A2
RT   receptor.";
RL   Biochim. Biophys. Acta 1403:109-114(1998).
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 (By similarity). {ECO:0000250}.
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; AF017452; AAB70300.1; -; mRNA.
DR   AlphaFoldDB; P56486; -.
DR   SMR; P56486; -.
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:0004960; F:thromboxane receptor activity; IEA:InterPro.
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; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..343
FT                   /note="Thromboxane A2 receptor"
FT                   /id="PRO_0000070137"
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..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..172
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..219
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..270
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..289
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..311
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        312..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21731"
FT   MOD_RES         331
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        105..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   343 AA;  37487 MW;  78B92DC7E6737015 CRC64;
     MWPNGSSLGP CFRPTNITLE ERRLIASPWF AASFCVVGLA SNLLALSVLA GARQGGSHTR
     SSFLTFLCGL VLTDFLGLLV TGAIVVSQHA ALFEWHAVDP GCRLCRFMGV VMIFFGLSPL
     LLGATMASER FLGITRPFSR PVVTSQRRAW ATVGLVWAAA LALGLLPLLG LGRYTVQYPG
     SWCFLTLGAE SGDVAFGLLF SMLGGLSVGL SFLLNTVSVA TLCHVYHGQE AAQQRPRDSE
     VEMMAQLLGI MLVASVCWLP LLVFIAQTVL RNPPAMSPSG QLSRATEQEL LIYLRVATWN
     QILDPWVYIL FRRAVLRRLQ PRLSTRPRSL SLQPQLTQRS GLQ