ID THAS_HUMAN Reviewed; 533 AA. AC P24557; B4DJG6; E7EMU9; E7EP08; E7ESB5; O14987; Q16843; Q16844; Q8IUN1; AC Q96CN2; Q9GZW4; Q9HD77; Q9HD78; Q9HD79; Q9HD80; Q9HD81; Q9HD82; Q9HD83; AC Q9HD84; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 3. DT 24-JAN-2024, entry version 231. DE RecName: Full=Thromboxane-A synthase; DE Short=TXA synthase; DE Short=TXS {ECO:0000303|PubMed:8366093}; DE EC=5.3.99.5 {ECO:0000269|PubMed:11097184, ECO:0000269|PubMed:11297515, ECO:0000269|PubMed:22735388, ECO:0000269|PubMed:24009185, ECO:0000269|PubMed:8436233, ECO:0000269|PubMed:9873013}; DE AltName: Full=Cytochrome P450 5A1; DE AltName: Full=Hydroperoxy icosatetraenoate dehydratase {ECO:0000305}; DE EC=4.2.1.152 {ECO:0000269|PubMed:17459323}; GN Name=TBXAS1; GN Synonyms=CYP5, CYP5A1 {ECO:0000303|PubMed:11465543}, TXAS; 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 TISSUE SPECIFICITY. RC TISSUE=Platelet; RX PubMed=1714723; DOI=10.1016/0006-291x(91)91060-p; RA Yokoyama C., Miyata A., Ihara H., Ullrich V., Tanabe T.; RT "Molecular cloning of human platelet thromboxane A synthase."; RL Biochem. Biophys. Res. Commun. 178:1479-1484(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Lung; RX PubMed=1730669; DOI=10.1016/s0021-9258(18)48353-6; RA Ohashi K., Ruan K.H., Kulmacz R.J., Wu K.K., Wang L.-H.; RT "Primary structure of human thromboxane synthase determined from the cDNA RT sequence."; RL J. Biol. Chem. 267:789-793(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RC TISSUE=Peripheral blood; RX PubMed=7925341; DOI=10.1111/j.1432-1033.1994.00273.x; RA Miyata A., Yokoyama C., Ihara H., Bandoh S., Takeda O., Takahashi E., RA Tanabe T.; RT "Characterization of the human gene (TBXAS1) encoding thromboxane RT synthase."; RL Eur. J. Biochem. 224:273-279(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Shen R.-F.; RT "Human thromboxane A2 synthase."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-60; GLU-160; SER-245; RP VAL-356; GLU-416; LYS-449; ASN-450 AND GLN-465. RX PubMed=11465543; DOI=10.1016/s1383-5726(00)00004-2; RA Chevalier D., Lo-Guidice J.-M., Sergent E., Allorge D., Debuysere H., RA Ferrari N., Libersa C., Lhermitte M., Broly F.; RT "Identification of genetic variants in the human thromboxane synthase gene RT (CYP5A1)."; RL Mutat. Res. 432:61-67(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-244 (ISOFORM 1/2). RC TISSUE=Lung; RX PubMed=2043115; DOI=10.1016/0006-291x(91)91980-q; RA Wang L.-H., Oshashi K., Wu K.K.; RT "Isolation of partial complementary DNA encoding human thromboxane RT synthase."; RL Biochem. Biophys. Res. Commun. 177:286-291(1991). RN [11] RP PRELIMINARY PROTEIN SEQUENCE OF 1-26; 96-110 AND 237-280. RX PubMed=2195994; DOI=10.1016/0003-9861(90)90337-x; RA Nuesing R., Schneider-Voss S., Ullrich V.; RT "Immunoaffinity purification of human thromboxane synthase."; RL Arch. Biochem. Biophys. 280:325-330(1990). RN [12] RP PARTIAL PROTEIN SEQUENCE. RA Nuesing R.; RL Thesis (1990), University of Konstanz, Germany. RN [13] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=8436233; DOI=10.1016/0014-5793(93)81335-w; RA Yokoyama C., Miyata A., Suzuki K., Nishikawa Y., Yoshimoto T., Yamamoto S., RA Nuesing R., Ullrich V., Tanabe T.; RT "Expression of human thromboxane synthase using a baculovirus system."; RL FEBS Lett. 318:91-94(1993). RN [14] RP SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=8366093; DOI=10.1016/s0021-9258(19)36541-x; RA Ruan K.H., Wang L.-H., Wu K.K., Kulmacz R.J.; RT "Amino-terminal topology of thromboxane synthase in the endoplasmic RT reticulum."; RL J. Biol. Chem. 268:19483-19490(1993). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=9873013; DOI=10.1074/jbc.274.2.762; RA Hsu P.Y., Tsai A.L., Kulmacz R.J., Wang L.H.; RT "Expression, purification, and spectroscopic characterization of human RT thromboxane synthase."; RL J. Biol. Chem. 274:762-769(1999). RN [16] RP INVOLVEMENT IN THROMBOXANE SYNTHETASE DEFICIENCY. RX PubMed=6101498; DOI=10.1016/s0140-6736(80)90642-x; RA Mestel F., Oetliker O., Beck E., Felix R., Imbach P., Wagner H.P.; RT "Severe bleeding associated with defective thromboxane synthetase."; RL Lancet 1:157-157(1980). RN [17] RP HEME-BINDING, MUTAGENESIS OF ASN-109; TRP-132; GLU-134; ARG-136; ARG-409; RP ARG-412; ALA-414 AND ARG-477, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=11097184; DOI=10.1006/abbi.2000.2041; RA Hsu P.Y., Tsai A.L., Wang L.H.; RT "Identification of thromboxane synthase amino acid residues involved in RT heme-propionate binding."; RL Arch. Biochem. Biophys. 383:119-127(2000). RN [18] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=11297515; DOI=10.1074/jbc.m009177200; RA Wang L.H., Tsai A.L., Hsu P.Y.; RT "Substrate binding is the rate-limiting step in thromboxane synthase RT catalysis."; RL J. Biol. Chem. 276:14737-14743(2001). RN [19] RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17459323; DOI=10.1016/j.abb.2007.03.012; RA Yeh H.C., Tsai A.L., Wang L.H.; RT "Reaction mechanisms of 15-hydroperoxyeicosatetraenoic acid catalyzed by RT human prostacyclin and thromboxane synthases."; RL Arch. Biochem. Biophys. 461:159-168(2007). RN [20] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=24009185; DOI=10.1194/jlr.m037754; RA Matsunobu T., Okuno T., Yokoyama C., Yokomizo T.; RT "Thromboxane A synthase-independent production of 12- RT hydroxyheptadecatrienoic acid, a BLT2 ligand."; RL J. Lipid Res. 54:2979-2987(2013). RN [21] 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 [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP VARIANTS HIS-60; ILE-162; THR-331; VAL-356; GLU-416 AND THR-429. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [24] RP ERRATUM OF PUBMED:10391209. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). RN [25] RP VARIANTS GLU-160; VAL-356; GLU-416; CYS-424 AND THR-429. RX PubMed=10391210; DOI=10.1038/10297; RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., RA Cooper R., Lipshutz R., Chakravarti A.; RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood- RT pressure homeostasis."; RL Nat. Genet. 22:239-247(1999). RN [26] RP VARIANTS ILE-124; LYS-388; LYS-449 AND GLN-501. RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7; RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., RA Nakamura Y.; RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine RT esterase genes, and two other genes in the Japanese population."; RL J. Hum. Genet. 48:249-270(2003). RN [27] RP VARIANT [LARGE SCALE ANALYSIS] TRP-85. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [28] RP VARIANTS GHDD PRO-82; GLN-412; TRP-481 AND PRO-487, INVOLVEMENT IN GHDD, RP AND MUTAGENESIS OF CYS-479. RX PubMed=18264100; DOI=10.1038/ng.2007.66; RA Genevieve D., Proulle V., Isidor B., Bellais S., Serre V., Djouadi F., RA Picard C., Vignon-Savoye C., Bader-Meunier B., Blanche S., RA de Vernejoul M.-C., Legeai-Mallet L., Fischer A.-M., Le Merrer M., RA Dreyfus M., Gaussem P., Munnich A., Cormier-Daire V.; RT "Thromboxane synthase mutations in an increased bone density disorder RT (Ghosal syndrome)."; RL Nat. Genet. 40:284-286(2008). RN [29] RP CATALYTIC ACTIVITY, FUNCTION, CHARACTERIZATION OF VARIANTS GLU-257; RP VAL-356; GLU-416; LYS-449 AND ASN-450, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22735388; DOI=10.1097/fpc.0b013e3283562d82; RA Chen C.Y., Poole E.M., Ulrich C.M., Kulmacz R.J., Wang L.H.; RT "Functional analysis of human thromboxane synthase polymorphic variants."; RL Pharmacogenet. Genomics 22:653-658(2012). CC -!- FUNCTION: Catalyzes the conversion of prostaglandin H2 (PGH2) to CC thromboxane A2 (TXA2), a potent inducer of blood vessel constriction CC and platelet aggregation (PubMed:8436233, PubMed:11297515, CC PubMed:9873013, PubMed:11097184, PubMed:24009185, PubMed:22735388). CC Cleaves also PGH2 to 12-hydroxy-heptadecatrienoicacid (12-HHT) and CC malondialdehyde, which is known to act as a mediator of DNA damage. 12- CC HHT and malondialdehyde are formed stoichiometrically in the same CC amounts as TXA2 (PubMed:11297515, PubMed:9873013, PubMed:22735388). CC Additionally, displays dehydratase activity, toward (15S)-hydroperoxy- CC (5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) producing 15-KETE and CC 15-HETE (PubMed:17459323). {ECO:0000269|PubMed:11097184, CC ECO:0000269|PubMed:11297515, ECO:0000269|PubMed:17459323, CC ECO:0000269|PubMed:22735388, ECO:0000269|PubMed:24009185, CC ECO:0000269|PubMed:8436233, ECO:0000269|PubMed:9873013}. CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin H2 = thromboxane A2; Xref=Rhea:RHEA:17137, CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57445; EC=5.3.99.5; CC Evidence={ECO:0000269|PubMed:11097184, ECO:0000269|PubMed:11297515, CC ECO:0000269|PubMed:22735388, ECO:0000269|PubMed:24009185, CC ECO:0000269|PubMed:8436233, ECO:0000269|PubMed:9873013}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17138; CC Evidence={ECO:0000305|PubMed:11297515, ECO:0000305|PubMed:8436233, CC ECO:0000305|PubMed:9873013}; CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)- CC heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644, CC ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274; CC Evidence={ECO:0000269|PubMed:11297515, ECO:0000269|PubMed:22735388, CC ECO:0000269|PubMed:9873013}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate + CC H2O; Xref=Rhea:RHEA:55556, ChEBI:CHEBI:15377, ChEBI:CHEBI:59720, CC ChEBI:CHEBI:131859; EC=4.2.1.152; CC Evidence={ECO:0000269|PubMed:17459323}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55557; CC Evidence={ECO:0000305|PubMed:17459323}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo- CC (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; CC Evidence={ECO:0000269|PubMed:17459323}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637; CC Evidence={ECO:0000305|PubMed:17459323}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = CC (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; CC Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; CC Evidence={ECO:0000269|PubMed:17459323}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857; CC Evidence={ECO:0000305|PubMed:17459323}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:11097184}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=80 uM for (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate CC (15-HPETE) {ECO:0000269|PubMed:17459323}; CC KM=32 uM for prostaglandin H2 {ECO:0000269|PubMed:22735388}; CC KM=20 uM for prostaglandin H2 {ECO:0000269|PubMed:9873013}; CC Vmax=12 umol/min/mg enzyme for prostaglandin H2 as substrate CC {ECO:0000269|PubMed:9873013}; CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9873013}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:8366093}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P24557-1; Sequence=Displayed; CC Name=2; CC IsoId=P24557-2; Sequence=VSP_047217; CC Name=3; CC IsoId=P24557-3; Sequence=VSP_054121; CC Name=4; CC IsoId=P24557-4; Sequence=VSP_054122, VSP_054123; CC -!- TISSUE SPECIFICITY: Platelets, lung, kidney, spleen, macrophages and CC lung fibroblasts. {ECO:0000269|PubMed:1714723, CC ECO:0000269|PubMed:7925341}. CC -!- DISEASE: Ghosal hematodiaphyseal dysplasia (GHDD) [MIM:231095]: Rare CC autosomal recessive disorder characterized by increased bone density CC with predominant diaphyseal involvement and aregenerative CC corticosteroid-sensitive anemia. Aregenerative anemia is characterized CC by bone marrow failure, so that functional marrow cells are regenerated CC slowly or not at all. {ECO:0000269|PubMed:18264100}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Note=Thromboxane synthetase deficiency has been detected in CC some patients with a bleeding disorder due to platelet dysfunction. CC {ECO:0000269|PubMed:6101498}. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 is the initiator. An alternative CC upstream Met is found in primates, but not in other mammals. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA60617.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAA60618.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAC01761.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAC01761.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99269.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99270.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99271.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99272.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99273.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99274.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99275.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99276.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99277.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99278.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF99279.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH41157.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG58828.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW83934.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=PharmVar Pharmacogen Variation Consortium; CC Note=CYP5A1 alleles; CC URL="https://www.pharmvar.org/gene/TBXAS1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M80646; AAA60617.1; ALT_INIT; mRNA. DR EMBL; M80647; AAA60618.1; ALT_INIT; mRNA. DR EMBL; D34625; BAA07011.1; -; Genomic_DNA. DR EMBL; L36085; AAC01761.1; ALT_INIT; Genomic_DNA. DR EMBL; L36075; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36076; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36077; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36078; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36079; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36080; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36081; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36082; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36083; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; L36084; AAC01761.1; JOINED; Genomic_DNA. DR EMBL; AF233615; AAF99269.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233616; AAF99270.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233617; AAF99271.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233618; AAF99272.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233619; AAF99273.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233620; AAF99274.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233621; AAF99275.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233622; AAF99276.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233623; AAF99277.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233624; AAF99278.1; ALT_INIT; Genomic_DNA. DR EMBL; AF233625; AAF99279.1; ALT_INIT; Genomic_DNA. DR EMBL; AK296069; BAG58828.1; ALT_INIT; mRNA. DR EMBL; AC004914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC004961; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006021; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471070; EAW83934.1; ALT_INIT; Genomic_DNA. DR EMBL; BC014117; AAH14117.1; -; mRNA. DR EMBL; BC041157; AAH41157.1; ALT_INIT; mRNA. DR EMBL; M74055; AAA36742.1; -; mRNA. DR CCDS; CCDS55174.2; -. [P24557-3] DR CCDS; CCDS55175.1; -. [P24557-2] DR CCDS; CCDS5855.2; -. [P24557-1] DR CCDS; CCDS5856.2; -. [P24557-4] DR PIR; A41766; A41766. DR PIR; S48161; S48161. DR RefSeq; NP_001052.2; NM_001061.4. [P24557-1] DR RefSeq; NP_001124438.1; NM_001130966.2. [P24557-1] DR RefSeq; NP_001159725.1; NM_001166253.1. [P24557-3] DR RefSeq; NP_001159726.1; NM_001166254.1. [P24557-2] DR RefSeq; NP_112246.2; NM_030984.3. [P24557-4] DR AlphaFoldDB; P24557; -. DR SMR; P24557; -. DR BioGRID; 112778; 6. DR IntAct; P24557; 4. DR MINT; P24557; -. DR STRING; 9606.ENSP00000389414; -. DR BindingDB; P24557; -. DR ChEMBL; CHEMBL1835; -. DR DrugBank; DB03052; Dazoxiben. DR DrugBank; DB05505; NM-702. DR DrugBank; DB01207; Ridogrel. DR DrugCentral; P24557; -. DR GuidetoPHARMACOLOGY; 1353; -. DR SwissLipids; SLP:000001099; -. DR GlyGen; P24557; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P24557; -. DR PhosphoSitePlus; P24557; -. DR SwissPalm; P24557; -. DR BioMuta; TBXAS1; -. DR EPD; P24557; -. DR jPOST; P24557; -. DR MassIVE; P24557; -. DR MaxQB; P24557; -. DR PaxDb; 9606-ENSP00000389414; -. DR PeptideAtlas; P24557; -. DR ProteomicsDB; 17017; -. DR ProteomicsDB; 17264; -. DR ProteomicsDB; 17954; -. DR ProteomicsDB; 54216; -. [P24557-1] DR Antibodypedia; 18246; 521 antibodies from 33 providers. DR DNASU; 6916; -. DR Ensembl; ENST00000336425.10; ENSP00000338087.7; ENSG00000059377.19. [P24557-1] DR Ensembl; ENST00000411653.6; ENSP00000411326.3; ENSG00000059377.19. [P24557-4] DR Ensembl; ENST00000425687.5; ENSP00000388736.1; ENSG00000059377.19. [P24557-2] DR Ensembl; ENST00000448866.7; ENSP00000402536.3; ENSG00000059377.19. [P24557-1] DR Ensembl; ENST00000458722.6; ENSP00000411274.3; ENSG00000059377.19. [P24557-3] DR GeneID; 6916; -. DR KEGG; hsa:6916; -. DR MANE-Select; ENST00000448866.7; ENSP00000402536.3; NM_001061.7; NP_001052.3. DR UCSC; uc010lne.4; human. [P24557-1] DR AGR; HGNC:11609; -. DR CTD; 6916; -. DR DisGeNET; 6916; -. DR GeneCards; TBXAS1; -. DR HGNC; HGNC:11609; TBXAS1. DR HPA; ENSG00000059377; Tissue enhanced (lymphoid). DR MalaCards; TBXAS1; -. DR MIM; 231095; phenotype. DR MIM; 274180; gene. DR neXtProt; NX_P24557; -. DR OpenTargets; ENSG00000059377; -. DR Orphanet; 1802; Ghosal hematodiaphyseal dysplasia. DR PharmGKB; PA349; -. DR VEuPathDB; HostDB:ENSG00000059377; -. DR eggNOG; KOG0158; Eukaryota. DR GeneTree; ENSGT00940000157903; -. DR HOGENOM; CLU_001570_5_2_1; -. DR InParanoid; P24557; -. DR OMA; WPHPETF; -. DR OrthoDB; 1611592at2759; -. DR PhylomeDB; P24557; -. DR TreeFam; TF105087; -. DR BioCyc; MetaCyc:HS00728-MONOMER; -. DR PathwayCommons; P24557; -. DR Reactome; R-HSA-211979; Eicosanoids. DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR Reactome; R-HSA-5579032; Defective TBXAS1 causes GHDD. DR SignaLink; P24557; -. DR SIGNOR; P24557; -. DR UniPathway; UPA00199; -. DR BioGRID-ORCS; 6916; 14 hits in 1168 CRISPR screens. DR ChiTaRS; TBXAS1; human. DR GeneWiki; Thromboxane-A_synthase; -. DR GenomeRNAi; 6916; -. DR Pharos; P24557; Tchem. DR PRO; PR:P24557; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P24557; Protein. DR Bgee; ENSG00000059377; Expressed in monocyte and 111 other cell types or tissues. DR ExpressionAtlas; P24557; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0036134; F:12-hydroxyheptadecatrienoic acid synthase activity; TAS:Reactome. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR GO; GO:0004796; F:thromboxane-A synthase activity; IDA:UniProtKB. DR GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome. DR GO; GO:0006690; P:icosanoid metabolic process; IDA:UniProtKB. DR GO; GO:0030644; P:intracellular chloride ion homeostasis; IEA:Ensembl. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl. DR GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:UniProtKB. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl. DR CDD; cd20649; CYP5A1; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR036396; Cyt_P450_sf. DR PANTHER; PTHR24301; THROMBOXANE-A SYNTHASE; 1. DR PANTHER; PTHR24301:SF2; THROMBOXANE-A SYNTHASE; 1. DR Pfam; PF00067; p450; 2. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. DR Genevisible; P24557; HS. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Disease variant; KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; KW Heme; Iron; Isomerase; Lipid biosynthesis; Lipid metabolism; Lyase; KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..533 FT /note="Thromboxane-A synthase" FT /id="PRO_0000052256" FT TOPO_DOM 1..10 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:8366093" FT TRANSMEM 11..31 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 32..75 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:8366093" FT TRANSMEM 76..96 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 97..223 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:8366093" FT TRANSMEM 224..244 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 245..335 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:8366093" FT TRANSMEM 336..356 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 357..533 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:8366093" FT BINDING 479 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P14779" FT VAR_SEQ 1..67 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_047217" FT VAR_SEQ 150 FT /note="E -> ELGLLIMQERIKGHMGGQQAPQRIPPTRLSKPSGIYVNLHYATLPFC FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054121" FT VAR_SEQ 456..459 FT /note="FTAE -> YRCS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:1730669" FT /id="VSP_054122" FT VAR_SEQ 460..533 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:1730669" FT /id="VSP_054123" FT VARIANT 60 FT /note="R -> H (in allele CYP5A1*2; dbSNP:rs6138)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:11465543" FT /id="VAR_014157" FT VARIANT 70 FT /note="L -> P (in dbSNP:rs13306050)" FT /id="VAR_058465" FT VARIANT 70 FT /note="L -> V (in dbSNP:rs4529)" FT /id="VAR_058466" FT VARIANT 82 FT /note="L -> P (in GHDD; dbSNP:rs140005285)" FT /evidence="ECO:0000269|PubMed:18264100" FT /id="VAR_044386" FT VARIANT 85 FT /note="R -> W (in a breast cancer sample; somatic mutation; FT dbSNP:rs1016604233)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036294" FT VARIANT 124 FT /note="V -> I (in dbSNP:rs8192833)" FT /evidence="ECO:0000269|PubMed:12721789" FT /id="VAR_018378" FT VARIANT 160 FT /note="D -> E (in allele CYP5A1*3; dbSNP:rs5768)" FT /evidence="ECO:0000269|PubMed:10391210, FT ECO:0000269|PubMed:11465543" FT /id="VAR_010919" FT VARIANT 162 FT /note="L -> I (in dbSNP:rs6137)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014158" FT VARIANT 245 FT /note="N -> S (in allele CYP5A1*4; dbSNP:rs55856189)" FT /evidence="ECO:0000269|PubMed:11465543" FT /id="VAR_010920" FT VARIANT 257 FT /note="K -> E (the KM value is about 1.5 higher for PEG2; FT in allele CYP5A1*5; KM value about 1.5 higher for PEG2; FT Vmax/KM approximately 50% of that of the wild-type; FT dbSNP:rs5769)" FT /evidence="ECO:0000269|PubMed:22735388" FT /id="VAR_014647" FT VARIANT 260 FT /note="R -> G (in dbSNP:rs5770)" FT /id="VAR_014648" FT VARIANT 316 FT /note="Q -> K (in dbSNP:rs5771)" FT /id="VAR_014649" FT VARIANT 331 FT /note="I -> T (in dbSNP:rs6140)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014159" FT VARIANT 356 FT /note="L -> V (in allele CYP5A1*5; KM value about 1.5 FT higher for PEG2; Vmax/KM approximately 27% of that of the FT wild-type; dbSNP:rs4529)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:10391210, ECO:0000269|PubMed:11465543, FT ECO:0000269|PubMed:22735388" FT /id="VAR_010921" FT VARIANT 357 FT /note="L -> V (in dbSNP:rs4529)" FT /id="VAR_044387" FT VARIANT 387 FT /note="E -> K (in dbSNP:rs3735354)" FT /id="VAR_055565" FT VARIANT 388 FT /note="E -> K (in dbSNP:rs3735354)" FT /evidence="ECO:0000269|PubMed:12721789" FT /id="VAR_018379" FT VARIANT 389 FT /note="G -> V (in dbSNP:rs5760)" FT /id="VAR_016158" FT VARIANT 412 FT /note="R -> Q (in GHDD; dbSNP:rs199422117)" FT /evidence="ECO:0000269|PubMed:18264100" FT /id="VAR_044388" FT VARIANT 416 FT /note="Q -> E (in allele CYP5A1*6; does not affect KM value FT for PEG2; does not affect Vmax/KM value; dbSNP:rs4528)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:10391210, ECO:0000269|PubMed:11465543, FT ECO:0000269|PubMed:22735388" FT /id="VAR_010922" FT VARIANT 424 FT /note="R -> C (in dbSNP:rs5762)" FT /evidence="ECO:0000269|PubMed:10391210" FT /id="VAR_014160" FT VARIANT 429 FT /note="A -> T (in dbSNP:rs4526)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:10391210" FT /id="VAR_014161" FT VARIANT 449 FT /note="E -> K (in allele CYP5A1*7; does not affect KM value FT for PEG2; does not affect Vmax/KM value; dbSNP:rs8192868)" FT /evidence="ECO:0000269|PubMed:11465543, FT ECO:0000269|PubMed:12721789, ECO:0000269|PubMed:22735388" FT /id="VAR_010923" FT VARIANT 450 FT /note="T -> N (in allele CYP5A1*8; KM value about 1.5 FT higher for PEG2; Vmax/KM approximately 56 % of that of the FT wild-type; dbSNP:rs5763)" FT /evidence="ECO:0000269|PubMed:11465543, FT ECO:0000269|PubMed:22735388" FT /id="VAR_010924" FT VARIANT 465 FT /note="R -> Q (in allele CYP5A1*9; dbSNP:rs41311778)" FT /evidence="ECO:0000269|PubMed:11465543" FT /id="VAR_010925" FT VARIANT 481 FT /note="G -> W (in GHDD; dbSNP:rs199422116)" FT /evidence="ECO:0000269|PubMed:18264100" FT /id="VAR_044389" FT VARIANT 487 FT /note="L -> P (in GHDD; dbSNP:rs199422114)" FT /evidence="ECO:0000269|PubMed:18264100" FT /id="VAR_044390" FT VARIANT 501 FT /note="R -> Q (in dbSNP:rs8192864)" FT /evidence="ECO:0000269|PubMed:12721789" FT /id="VAR_018380" FT VARIANT 511 FT /note="P -> L (in dbSNP:rs13306050)" FT /id="VAR_055566" FT VARIANT 512 FT /note="L -> P (in dbSNP:rs13306050)" FT /id="VAR_044391" FT MUTAGEN 109 FT /note="N->I: Loss of thromboxane-A synthase activity. FT Decreased heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 132 FT /note="W->F: Loss of thromboxane-A synthase activity. FT Decreased heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 134 FT /note="E->D: Does not affect thromboxane-A synthase FT activity. Does not affect heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 136 FT /note="R->A,K: Loss of thromboxane-A synthase activity. FT Decreased heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 409 FT /note="R->G: Does not affect thromboxane-A synthase FT activity. Does not affect heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 412 FT /note="R->K: Loss of thromboxane-A synthase activity. FT Decreased heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 414 FT /note="A->V: Does not affect thromboxane-A synthase FT activity. Does not affect heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 477 FT /note="R->A: Loss of thromboxane-A synthase activity. FT Decreased heme-binding." FT /evidence="ECO:0000269|PubMed:11097184" FT MUTAGEN 479 FT /note="C->S,H,Y: Loss of thromboxane-A synthase activity. FT Decreased heme-binding." FT /evidence="ECO:0000269|PubMed:18264100" FT CONFLICT 102 FT /note="E -> Q (in Ref. 10; AAA36742)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="L -> V (in Ref. 4; AAC01761)" FT /evidence="ECO:0000305" FT CONFLICT 194 FT /note="A -> P (in Ref. 2; AAA60617/AAA60618, 4; AAC01761, FT 5; FT AAF99269/AAF99270/AAF99271/AAF99272/AAF99273/AAF99274/AAF99275/AAF99276/AAF99277/AAF99278/AAF99279 FT and 10; AAA36742)" FT /evidence="ECO:0000305" FT CONFLICT 385 FT /note="S -> G (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 483 FT /note="R -> H (in Ref. 3; BAA07011)" FT /evidence="ECO:0000305" SQ SEQUENCE 533 AA; 60518 MW; E95E7B7EA77E6DDC CRC64; MEALGFLKLE VNGPMVTVAL SVALLALLKW YSTSAFSRLE KLGLRHPKPS PFIGNLTFFR QGFWESQMEL RKLYGPLCGY YLGRRMFIVI SEPDMIKQVL VENFSNFTNR MASGLEFKSV ADSVLFLRDK RWEEVRGALM SAFSPEKLNE MVPLISQACD LLLAHLKRYA ESGDAFDIQR CYCNYTTDVV ASVAFGTPVD SWQAPEDPFV KHCKRFFEFC IPRPILVLLL SFPSIMVPLA RILPNKNRDE LNGFFNKLIR NVIALRDQQA AEERRRDFLQ MVLDARHSAS PMGVQDFDIV RDVFSSTGCK PNPSRQHQPS PMARPLTVDE IVGQAFIFLI AGYEIITNTL SFATYLLATN PDCQEKLLRE VDVFKEKHMA PEFCSLEEGL PYLDMVIAET LRMYPPAFRF TREAAQDCEV LGQRIPAGAV LEMAVGALHH DPEHWPSPET FNPERFTAEA RQQHRPFTYL PFGAGPRSCL GVRLGLLEVK LTLLHVLHKF RFQACPETQV PLQLESKSAL GPKNGVYIKI VSR //