##gff-version 3
P21731	UniProtKB	Chain	1	343	.	.	.	ID=PRO_0000070138;Note=Thromboxane A2 receptor	
P21731	UniProtKB	Topological domain	1	29	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Transmembrane	30	52	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Topological domain	53	66	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Topological domain	88	106	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Transmembrane	107	128	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Topological domain	129	149	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Transmembrane	150	172	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Topological domain	173	193	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Transmembrane	194	219	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Topological domain	220	246	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Transmembrane	247	270	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Topological domain	271	289	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Transmembrane	290	311	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Topological domain	312	343	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P21731	UniProtKB	Modified residue	329	329	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231	
P21731	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P30987	
P21731	UniProtKB	Glycosylation	4	4	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P21731	UniProtKB	Glycosylation	16	16	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P21731	UniProtKB	Disulfide bond	105	183	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
P21731	UniProtKB	Alternative sequence	329	343	.	.	.	ID=VSP_001925;Note=In isoform 2. SLSLQPQLTQRSGLQ->RSLTLWPSLEYSGTISAHCNLRLPGSSDSRASASRAAGITGVSHCARPCMLFDPEFDLLAGVQLLPFEPPTGKALSRKD;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:8034687,ECO:0000303|PubMed:8613548;Dbxref=PMID:8034687,PMID:8613548	
P21731	UniProtKB	Natural variant	60	60	.	.	.	ID=VAR_003515;Note=In BDPLT13%3B does not affect TXA2 binding%3B defective interaction with G proteins%3B impairs phospholipase C and adenylyl cyclase activation%3B isoform 1%3B has no effect on adenylyl cyclase inhibition%3B isoform 2. R->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7929844,ECO:0000269|PubMed:8613548;Dbxref=dbSNP:rs34377097,PMID:7929844,PMID:8613548	
P21731	UniProtKB	Natural variant	68	68	.	.	.	ID=VAR_014688;Note=C->S;Dbxref=dbSNP:rs5743	
P21731	UniProtKB	Natural variant	80	80	.	.	.	ID=VAR_014689;Note=V->E;Dbxref=dbSNP:rs5744	
P21731	UniProtKB	Natural variant	94	94	.	.	.	ID=VAR_014690;Note=E->V;Dbxref=dbSNP:rs5746	
P21731	UniProtKB	Natural variant	160	160	.	.	.	ID=VAR_014691;Note=A->T;Dbxref=dbSNP:rs5749	
P21731	UniProtKB	Natural variant	176	176	.	.	.	ID=VAR_014692;Note=V->E;Dbxref=dbSNP:rs5750	
P21731	UniProtKB	Natural variant	217	217	.	.	.	ID=VAR_014693;Note=V->I;Dbxref=dbSNP:rs5751	
P21731	UniProtKB	Mutagenesis	291	291	.	.	.	Note=Suppresses antagonist binding. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8246916;Dbxref=PMID:8246916	
P21731	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Reduces antagonist binding. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8246916;Dbxref=PMID:8246916	
P21731	UniProtKB	Mutagenesis	299	299	.	.	.	Note=Reduces antagonist binding. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8246916;Dbxref=PMID:8246916	
P21731	UniProtKB	Mutagenesis	299	299	.	.	.	Note=Reduces antagonist binding. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8246916;Dbxref=PMID:8246916	
P21731	UniProtKB	Sequence conflict	263	263	.	.	.	Note=V->W;Ontology_term=ECO:0000305;evidence=ECO:0000305