TA2R_HUMAN
ID TA2R_HUMAN Reviewed; 343 AA.
AC P21731; O75228; Q6DK52; Q9UCY1; Q9UCY2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Thromboxane A2 receptor;
DE Short=TXA2-R;
DE AltName: Full=Prostanoid TP receptor;
GN Name=TBXA2R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=1825698; DOI=10.1038/349617a0;
RA Hirata M., Hayashi Y., Ushikubi F., Yokota Y., Kageyama R., Nakanishi S.,
RA Narumiya S.;
RT "Cloning and expression of cDNA for a human thromboxane A2 receptor.";
RL Nature 349:617-620(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8227091; DOI=10.1016/s0021-9258(19)74595-5;
RA Nuesing R.M., Hirata M., Kakizuka A., Eki T., Ozawa K., Narumiya S.;
RT "Characterization and chromosomal mapping of the human thromboxane A2
RT receptor gene.";
RL J. Biol. Chem. 268:25253-25259(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=8034687; DOI=10.1016/s0021-9258(17)32161-0;
RA Raychowdhury M.K., Yukawa M., Collins L.J., McGrail S.H., Kent K.C.,
RA Ware J.A.;
RT "Alternative splicing produces a divergent cytoplasmic tail in the human
RT endothelial thromboxane A2 receptor.";
RL J. Biol. Chem. 269:19256-19261(1994).
RN [4]
RP ERRATUM OF PUBMED:8034687.
RX PubMed=7896853; DOI=10.1074/jbc.270.12.7011;
RA Raychowdhury M.K., Yukawa M., Collins L.J., McGrail S.H., Kent K.C.,
RA Ware J.A.;
RL J. Biol. Chem. 270:7011-7011(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7965765;
RA D'Angelo D.D., Davis M.G., Ali S., Dorn G.W. II;
RT "Cloning and pharmacologic characterization of a thromboxane A2 receptor
RT from K562 (human chronic myelogenous leukemia) cells.";
RL J. Pharmacol. Exp. Ther. 271:1034-1041(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 329-343 (ISOFORMS 1 AND 2), FUNCTION,
RP ALTERNATIVE SPLICING, AND CHARACTERIZATION OF VARIANT BDPLT13 LEU-60.
RC TISSUE=Platelet;
RX PubMed=8613548; DOI=10.1172/jci118518;
RA Hirata T., Ushikubi F., Kakizuka A., Okuma M., Narumiya S.;
RT "Two thromboxane A2 receptor isoforms in human platelets. Opposite coupling
RT to adenylyl cyclase with different sensitivity to Arg60 to Leu mutation.";
RL J. Clin. Invest. 97:949-956(1996).
RN [12]
RP MUTAGENESIS OF LEU-291; ARG-295 AND TRP-299.
RX PubMed=8246916;
RA Funk C.D., Furci L., Moran N., Fitzgerald G.A.;
RT "Point mutation in the seventh hydrophobic domain of the human thromboxane
RT A2 receptor allows discrimination between agonist and antagonist binding
RT sites.";
RL Mol. Pharmacol. 44:934-939(1993).
RN [13]
RP INTERACTION WITH PSMA3.
RX PubMed=17499743; DOI=10.1016/j.prostaglandins.2006.12.001;
RA Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S., Nakahata N.;
RT "Low expression of cell-surface thromboxane A2 receptor beta-isoform
RT through the negative regulation of its membrane traffic by proteasomes.";
RL Prostaglandins Other Lipid Mediat. 83:237-249(2007).
RN [14]
RP INTERACTION WITH RACK1.
RX PubMed=18088317; DOI=10.1111/j.1600-0854.2007.00692.x;
RA Parent A., Laroche G., Hamelin E., Parent J.L.;
RT "RACK1 regulates the cell surface expression of the G protein-coupled
RT receptor for thromboxane A(2).";
RL Traffic 9:394-407(2008).
RN [15]
RP INTERACTION WITH RPGRIP1L.
RX PubMed=19464661; DOI=10.1016/j.prostaglandins.2009.02.001;
RA Tokue S., Sasaki M., Nakahata N.;
RT "Thromboxane A2-induced signal transduction is negatively regulated by
RT KIAA1005 that directly interacts with thromboxane A2 receptor.";
RL Prostaglandins Other Lipid Mediat. 89:8-15(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP VARIANT BDPLT13 LEU-60, AND CHARACTERIZATION OF VARIANT BDPLT13 LEU-60.
RX PubMed=7929844; DOI=10.1172/jci117510;
RA Hirata T., Kakizuka A., Ushikubi F., Fuse I., Okuma M., Narumiya S.;
RT "Arg60 to Leu mutation of the human thromboxane A2 receptor in a dominantly
RT inherited bleeding disorder.";
RL J. Clin. Invest. 94:1662-1667(1994).
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.
CC {ECO:0000269|PubMed:8613548}.
CC -!- FUNCTION: [Isoform 1]: Activates adenylyl cyclase.
CC {ECO:0000269|PubMed:8613548}.
CC -!- FUNCTION: [Isoform 2]: Inhibits adenylyl cyclase.
CC {ECO:0000269|PubMed:8613548}.
CC -!- SUBUNIT: Interacts with RPGRIP1L. Interacts with PSMA3. Interacts with
CC RACK1; the interaction regulates TBXA2R cell surface expression.
CC {ECO:0000269|PubMed:17499743, ECO:0000269|PubMed:18088317,
CC ECO:0000269|PubMed:19464661}.
CC -!- INTERACTION:
CC P21731; Q13162: PRDX4; NbExp=3; IntAct=EBI-2625082, EBI-2211957;
CC P21731-3; Q12791-5: KCNMA1; NbExp=7; IntAct=EBI-15885629, EBI-15861807;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha, Placenta receptor {ECO:0000303|PubMed:8034687};
CC IsoId=P21731-3; Sequence=Displayed;
CC Name=2; Synonyms=Beta, Endothelial receptor
CC {ECO:0000303|PubMed:8034687};
CC IsoId=P21731-2; Sequence=VSP_001925;
CC -!- DISEASE: Bleeding disorder, platelet-type, 13 (BDPLT13) [MIM:614009]: A
CC disorder characterized by reduced platelet aggregation and a tendency
CC to mild mucocutaneous bleeding. {ECO:0000269|PubMed:7929844,
CC ECO:0000269|PubMed:8613548}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAA58957.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tbxa2r/";
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DR EMBL; D38081; BAA07274.1; -; mRNA.
DR EMBL; D15056; BAA03649.1; -; Genomic_DNA.
DR EMBL; U11271; AAA58957.1; ALT_FRAME; mRNA.
DR EMBL; U27325; AAA68608.1; -; mRNA.
DR EMBL; AY429110; AAR07905.1; -; mRNA.
DR EMBL; DQ268653; ABB72549.1; -; Genomic_DNA.
DR EMBL; AC005175; AAC24302.1; -; Genomic_DNA.
DR EMBL; AC005175; AAC24303.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69301.1; -; Genomic_DNA.
DR EMBL; BC074749; AAH74749.1; -; mRNA.
DR EMBL; BC074750; AAH74750.1; -; mRNA.
DR CCDS; CCDS42467.1; -. [P21731-3]
DR CCDS; CCDS54198.1; -. [P21731-2]
DR PIR; A49117; A49117.
DR PIR; A53959; A53959.
DR PIR; A56194; A56194.
DR PIR; T02670; T02670.
DR RefSeq; NP_001051.1; NM_001060.5. [P21731-3]
DR RefSeq; NP_963998.2; NM_201636.2. [P21731-2]
DR RefSeq; XP_011526516.1; XM_011528214.2. [P21731-3]
DR AlphaFoldDB; P21731; -.
DR BMRB; P21731; -.
DR SMR; P21731; -.
DR BioGRID; 112777; 79.
DR DIP; DIP-41465N; -.
DR IntAct; P21731; 7.
DR MINT; P21731; -.
DR STRING; 9606.ENSP00000393333; -.
DR BindingDB; P21731; -.
DR ChEMBL; CHEMBL2069; -.
DR DrugBank; DB09285; Morniflumate.
DR DrugBank; DB01207; Ridogrel.
DR DrugBank; DB06739; Seratrodast.
DR DrugCentral; P21731; -.
DR GuidetoPHARMACOLOGY; 346; -.
DR GlyGen; P21731; 2 sites.
DR iPTMnet; P21731; -.
DR PhosphoSitePlus; P21731; -.
DR SwissPalm; P21731; -.
DR BioMuta; TBXA2R; -.
DR DMDM; 229463010; -.
DR jPOST; P21731; -.
DR MassIVE; P21731; -.
DR PaxDb; P21731; -.
DR PeptideAtlas; P21731; -.
DR PRIDE; P21731; -.
DR ProteomicsDB; 53894; -. [P21731-3]
DR ProteomicsDB; 53895; -. [P21731-2]
DR Antibodypedia; 5899; 188 antibodies from 29 providers.
DR DNASU; 6915; -.
DR Ensembl; ENST00000375190.10; ENSP00000364336.4; ENSG00000006638.13. [P21731-3]
DR Ensembl; ENST00000411851.3; ENSP00000393333.2; ENSG00000006638.13. [P21731-2]
DR GeneID; 6915; -.
DR KEGG; hsa:6915; -.
DR MANE-Select; ENST00000375190.10; ENSP00000364336.4; NM_001060.6; NP_001051.1.
DR UCSC; uc002lyg.3; human. [P21731-3]
DR CTD; 6915; -.
DR DisGeNET; 6915; -.
DR GeneCards; TBXA2R; -.
DR HGNC; HGNC:11608; TBXA2R.
DR HPA; ENSG00000006638; Low tissue specificity.
DR MalaCards; TBXA2R; -.
DR MIM; 188070; gene.
DR MIM; 614009; phenotype.
DR neXtProt; NX_P21731; -.
DR OpenTargets; ENSG00000006638; -.
DR Orphanet; 220443; Bleeding diathesis due to thromboxane synthesis deficiency.
DR PharmGKB; PA348; -.
DR VEuPathDB; HostDB:ENSG00000006638; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234559; -.
DR HOGENOM; CLU_045991_3_0_1; -.
DR InParanoid; P21731; -.
DR OMA; ASVCWMP; -.
DR PhylomeDB; P21731; -.
DR TreeFam; TF324982; -.
DR PathwayCommons; P21731; -.
DR Reactome; R-HSA-391908; Prostanoid ligand receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR SignaLink; P21731; -.
DR SIGNOR; P21731; -.
DR BioGRID-ORCS; 6915; 14 hits in 1078 CRISPR screens.
DR ChiTaRS; TBXA2R; human.
DR GeneWiki; Thromboxane_receptor; -.
DR GenomeRNAi; 6915; -.
DR Pharos; P21731; Tclin.
DR PRO; PR:P21731; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P21731; protein.
DR Bgee; ENSG00000006638; Expressed in tendon of biceps brachii and 187 other tissues.
DR ExpressionAtlas; P21731; baseline and differential.
DR Genevisible; P21731; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0004961; F:thromboxane A2 receptor activity; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:0045777; P:positive regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
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; PR00237; GPCRRHODOPSN.
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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disease variant; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="Thromboxane A2 receptor"
FT /id="PRO_0000070138"
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:0007744|PubMed:20068231"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30987"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 105..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 329..343
FT /note="SLSLQPQLTQRSGLQ -> RSLTLWPSLEYSGTISAHCNLRLPGSSDSRASA
FT SRAAGITGVSHCARPCMLFDPEFDLLAGVQLLPFEPPTGKALSRKD (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8034687,
FT ECO:0000303|PubMed:8613548"
FT /id="VSP_001925"
FT VARIANT 60
FT /note="R -> L (in BDPLT13; does not affect TXA2 binding;
FT defective interaction with G proteins; impairs
FT phospholipase C and adenylyl cyclase activation; isoform 1;
FT has no effect on adenylyl cyclase inhibition; isoform 2;
FT dbSNP:rs34377097)"
FT /evidence="ECO:0000269|PubMed:7929844,
FT ECO:0000269|PubMed:8613548"
FT /id="VAR_003515"
FT VARIANT 68
FT /note="C -> S (in dbSNP:rs5743)"
FT /id="VAR_014688"
FT VARIANT 80
FT /note="V -> E (in dbSNP:rs5744)"
FT /id="VAR_014689"
FT VARIANT 94
FT /note="E -> V (in dbSNP:rs5746)"
FT /id="VAR_014690"
FT VARIANT 160
FT /note="A -> T (in dbSNP:rs5749)"
FT /id="VAR_014691"
FT VARIANT 176
FT /note="V -> E (in dbSNP:rs5750)"
FT /id="VAR_014692"
FT VARIANT 217
FT /note="V -> I (in dbSNP:rs5751)"
FT /id="VAR_014693"
FT MUTAGEN 291
FT /note="L->R: Suppresses antagonist binding."
FT /evidence="ECO:0000269|PubMed:8246916"
FT MUTAGEN 295
FT /note="R->Q: Reduces antagonist binding."
FT /evidence="ECO:0000269|PubMed:8246916"
FT MUTAGEN 299
FT /note="W->L: Reduces antagonist binding."
FT /evidence="ECO:0000269|PubMed:8246916"
FT MUTAGEN 299
FT /note="W->R: Reduces antagonist binding."
FT /evidence="ECO:0000269|PubMed:8246916"
FT CONFLICT 263
FT /note="V -> W (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 37431 MW; 114A7C3F3F0D35F1 CRC64;
MWPNGSSLGP CFRPTNITLE ERRLIASPWF AASFCVVGLA SNLLALSVLA GARQGGSHTR
SSFLTFLCGL VLTDFLGLLV TGTIVVSQHA ALFEWHAVDP GCRLCRFMGV VMIFFGLSPL
LLGAAMASER YLGITRPFSR PAVASQRRAW ATVGLVWAAA LALGLLPLLG VGRYTVQYPG
SWCFLTLGAE SGDVAFGLLF SMLGGLSVGL SFLLNTVSVA TLCHVYHGQE AAQQRPRDSE
VEMMAQLLGI MVVASVCWLP LLVFIAQTVL RNPPAMSPAG QLSRTTEKEL LIYLRVATWN
QILDPWVYIL FRRAVLRRLQ PRLSTRPRSL SLQPQLTQRS GLQ
