ID PGH1_HUMAN Reviewed; 599 AA. AC P23219; A8K1V7; B4DHQ2; B4E2S5; Q15122; Q3HY28; Q3HY29; Q5T7T6; Q5T7T7; AC Q5T7T8; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 27-MAR-2024, entry version 232. DE RecName: Full=Prostaglandin G/H synthase 1 {ECO:0000305}; DE EC=1.14.99.1 {ECO:0000269|PubMed:7947975}; DE AltName: Full=Cyclooxygenase-1 {ECO:0000303|PubMed:15308583}; DE Short=COX-1 {ECO:0000303|PubMed:15308583}; DE AltName: Full=Prostaglandin H2 synthase 1; DE Short=PGH synthase 1; DE Short=PGHS-1; DE Short=PHS 1; DE AltName: Full=Prostaglandin-endoperoxide synthase 1; DE Flags: Precursor; GN Name=PTGS1 {ECO:0000312|HGNC:HGNC:9604}; GN Synonyms=COX1 {ECO:0000303|PubMed:15308583}; 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 [GENOMIC DNA] (ISOFORM 1), AND VARIANT ARG-8. RX PubMed=2512924; DOI=10.1016/s0006-291x(89)80049-x; RA Yokoyama C., Tanabe T.; RT "Cloning of human gene encoding prostaglandin endoperoxide synthase and RT primary structure of the enzyme."; RL Biochem. Biophys. Res. Commun. 165:888-894(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-529, AND VARIANT RP ARG-8. RX PubMed=1907252; DOI=10.1096/fasebj.5.9.1907252; RA Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., Fitzgerald G.A.; RT "Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA RT cloning, expression, and gene chromosomal assignment."; RL FASEB J. 5:2304-2312(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-8. RC TISSUE=Platelet; RX PubMed=1734857; DOI=10.1016/0006-291x(92)91750-k; RA Takahashi Y., Ueda N., Yoshimoto T., Yamamoto S., Yokoyama C., Miyata A., RA Tanabe T., Fuse I., Hattori A., Shibata A.; RT "Immunoaffinity purification and cDNA cloning of human platelet RT prostaglandin endoperoxide synthase (cyclooxygenase)."; RL Biochem. Biophys. Res. Commun. 182:433-438(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ARG-8. RC TISSUE=Lung fibroblast; RX PubMed=1587858; DOI=10.1016/s0021-9258(19)50092-8; RA Diaz A., Reginato A.M., Jimenez S.A.; RT "Alternative splicing of human prostaglandin G/H synthase mRNA and evidence RT of differential regulation of the resulting transcripts by transforming RT growth factor beta 1, interleukin 1 beta, and tumor necrosis factor RT alpha."; RL J. Biol. Chem. 267:10816-10822(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). RX PubMed=16141368; DOI=10.1124/jpet.105.090944; RA Qin N., Zhang S.P., Reitz T.L., Mei J.M., Flores C.M.; RT "Cloning, expression, and functional characterization of human RT cyclooxygenase-1 splicing variants: evidence for intron 1 retention."; RL J. Pharmacol. Exp. Ther. 315:1298-1305(2005). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8 AND RP LEU-17. RX PubMed=12192304; DOI=10.1097/00001721-200209000-00007; RA Scott B.T., Hasstedt S.J., Bovill E.G., Callas P.W., Valliere J.E., RA Wang L.-H., Wu K.K., Long G.L.; RT "Characterization of the human prostaglandin H synthase 1 gene (PTGS1): RT exclusion by genetic linkage analysis as a second modifier gene in familial RT thrombosis."; RL Blood Coagul. Fibrinolysis 13:519-531(2002). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT RP ARG-8. RC TISSUE=Caudate nucleus, Hippocampus, and Trachea; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8; LEU-17; RP HIS-53; LEU-149 AND MET-237. RG SeattleSNPs variation discovery resource; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-8. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-8. RC TISSUE=Brain; 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 [12] RP CHARACTERIZATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=7947975; DOI=10.1016/0167-4838(94)90148-1; RA Barnett J., Chow J., Ives D., Chiou M., Mackenzie R., Osen E., Nguyen B., RA Tsing S., Bach C., Freire J.; RT "Purification, characterization and selective inhibition of human RT prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system."; RL Biochim. Biophys. Acta 1209:130-139(1994). RN [13] RP REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS. RX PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145; RA Smith W.L., DeWitt D.L., Garavito R.M.; RT "Cyclooxygenases: structural, cellular, and molecular biology."; RL Annu. Rev. Biochem. 69:145-182(2000). RN [14] RP REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN COLORECTAL RP CANCER. RX PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40; RA Sostres C., Gargallo C.J., Lanas A.; RT "Aspirin, cyclooxygenase inhibition and colorectal cancer."; RL World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014). RN [15] 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 [16] RP VARIANTS MET-237 AND ILE-481. RX PubMed=15308583; DOI=10.1093/carcin/bgh260; RA Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.; RT "Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms RT and colon cancer risk."; RL Carcinogenesis 25:2467-2472(2004). CC -!- FUNCTION: Dual cyclooxygenase and peroxidase that plays an important CC role in the biosynthesis pathway of prostanoids, a class of C20 CC oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)- CC eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the CC inflammatory response. The cyclooxygenase activity oxygenates AA to the CC hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase CC activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 CC (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. CC This complex transformation is initiated by abstraction of hydrogen at CC carbon 13 (with S-stereochemistry), followed by insertion of molecular CC O2 to form the endoperoxide bridge between carbon 9 and 11 that defines CC prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase CC activity) yields a hydroperoxy group in PGG2 that is then reduced to CC PGH2 by two electrons (PubMed:7947975). Involved in the constitutive CC production of prostanoids in particular in the stomach and platelets. CC In gastric epithelial cells, it is a key step in the generation of CC prostaglandins, such as prostaglandin E2 (PGE2), which plays an CC important role in cytoprotection. In platelets, it is involved in the CC generation of thromboxane A2 (TXA2), which promotes platelet activation CC and aggregation, vasoconstriction and proliferation of vascular smooth CC muscle cells (Probable). Can also use linoleate (LA, (9Z,12Z)- CC octadecadienoate, C18:2(n-6)) as substrate and produce CC hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, CC being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)- CC HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By CC similarity). {ECO:0000250|UniProtKB:P05979, ECO:0000269|PubMed:7947975, CC ECO:0000305|PubMed:10966456, ECO:0000305|PubMed:24605250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + CC prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; CC Evidence={ECO:0000269|PubMed:7947975}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; CC Evidence={ECO:0000305|PubMed:7947975}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; CC Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:82629; Evidence={ECO:0000269|PubMed:7947975}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; CC Evidence={ECO:0000305|PubMed:7947975}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; CC Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; CC Evidence={ECO:0000269|PubMed:7947975}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; CC Evidence={ECO:0000305|PubMed:7947975}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)- CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)- CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)- CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)- CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; CC Evidence={ECO:0000250|UniProtKB:P05979}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {ECO:0000250}; CC -!- ACTIVITY REGULATION: The cyclooxygenase activity is inhibited by CC nonsteroidal anti-inflammatory drugs (NSAIDs) including ibuprofen, CC flurbiprofen, ketoprofen, naproxen, flurbiprofen, anirolac, fenclofenac CC and diclofenac. {ECO:0000269|PubMed:7947975}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5.1 uM for arachidonate {ECO:0000269|PubMed:7947975}; CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis. CC {ECO:0000269|PubMed:7947975}. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC P23219; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-6655935, EBI-2875816; CC P23219; P48645: NMU; NbExp=3; IntAct=EBI-6655935, EBI-10210351; CC P23219; P53801: PTTG1IP; NbExp=3; IntAct=EBI-6655935, EBI-3906138; CC P23219; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-6655935, EBI-25839575; CC -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. CC Endoplasmic reticulum membrane; Peripheral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=Long; CC IsoId=P23219-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P23219-2; Sequence=VSP_004673; CC Name=3; CC IsoId=P23219-3; Sequence=VSP_053936, VSP_004673; CC Name=4; CC IsoId=P23219-4; Sequence=VSP_046932; CC Name=5; Synonyms=1b3; CC IsoId=P23219-5; Sequence=VSP_054862; CC Name=6; Synonyms=1b2; CC IsoId=P23219-6; Sequence=VSP_054863; CC -!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2 is a CC 2 step reaction: a cyclooxygenase (COX) reaction which converts CC arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in CC which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase CC reaction occurs in a hydrophobic channel in the core of the enzyme. The CC peroxidase reaction occurs at a heme-containing active site located CC near the protein surface. The nonsteroidal anti-inflammatory drugs CC (NSAIDs) binding site corresponds to the cyclooxygenase active site. CC -!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is CC mediated by 2 different isozymes: the constitutive PTGS1 and the CC inducible PTGS2. PTGS1 is expressed constitutively and generally CC produces prostanoids acutely in response to hormonal stimuli to fine- CC tune physiological processes requiring instantaneous, continuous CC regulation (e.g. hemostasis). PTGS2 is inducible and typically produces CC prostanoids that mediate responses to physiological stresses such as CC infection and inflammation. CC -!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal anti- CC inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is CC able to produce an irreversible inactivation of the enzyme through a CC serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces CC inflammation, pain, and fever, and long-term use of these drugs reduces CC fatal thrombotic events, as well as the development of colon cancer and CC Alzheimer's disease. PTGS2 is the principal isozyme responsible for CC production of inflammatory prostaglandins. New generation PTGSs CC inhibitors strive to be selective for PTGS2, to avoid side effects such CC as gastrointestinal complications and ulceration. CC -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/ptgs1/"; 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; M31822; AAA36439.1; -; Genomic_DNA. DR EMBL; M31812; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31813; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31814; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31815; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31816; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31817; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31818; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31819; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31820; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M31821; AAA36439.1; JOINED; Genomic_DNA. DR EMBL; M59979; AAA03630.1; -; mRNA. DR EMBL; S78220; AAB21215.1; -; mRNA. DR EMBL; S36219; AAB22216.1; -; mRNA. DR EMBL; S36271; AAB22217.1; -; mRNA. DR EMBL; DQ180741; ABA60098.1; -; mRNA. DR EMBL; DQ180742; ABA60099.1; -; mRNA. DR EMBL; AF440204; AAL33601.1; -; Genomic_DNA. DR EMBL; AK290022; BAF82711.1; -; mRNA. DR EMBL; AK295221; BAG58214.1; -; mRNA. DR EMBL; AK304403; BAG65237.1; -; mRNA. DR EMBL; AY449688; AAR08907.1; -; Genomic_DNA. DR EMBL; AL162424; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359636; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87530.1; -; Genomic_DNA. DR EMBL; BC029840; AAH29840.1; -; mRNA. DR CCDS; CCDS59520.1; -. [P23219-3] DR CCDS; CCDS59521.1; -. [P23219-4] DR CCDS; CCDS6842.1; -. [P23219-1] DR CCDS; CCDS6843.1; -. [P23219-2] DR PIR; JH0259; JH0259. DR RefSeq; NP_000953.2; NM_000962.3. [P23219-1] DR RefSeq; NP_001258094.1; NM_001271165.1. [P23219-4] DR RefSeq; NP_001258095.1; NM_001271166.1. DR RefSeq; NP_001258297.1; NM_001271368.1. [P23219-3] DR RefSeq; NP_542158.1; NM_080591.2. [P23219-2] DR RefSeq; XP_011517178.1; XM_011518876.2. DR PDB; 6Y3C; X-ray; 3.36 A; A=24-599. DR PDBsum; 6Y3C; -. DR AlphaFoldDB; P23219; -. DR SMR; P23219; -. DR BioGRID; 111714; 13. DR CORUM; P23219; -. DR IntAct; P23219; 7. DR MINT; P23219; -. DR STRING; 9606.ENSP00000354612; -. DR BindingDB; P23219; -. DR ChEMBL; CHEMBL221; -. DR DrugBank; DB02047; (+)-2-(4-biphenyl)propionic acid. DR DrugBank; DB02773; (3-Chloro-4-Propoxy-Phenyl)-Acetic Acid. DR DrugBank; DB07983; 1-(4-IODOBENZOYL)-5-METHOXY-2-METHYL INDOLE-3-ACETIC ACID. DR DrugBank; DB07981; 2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]-n-[(1R)-1-(hydroxymethyl)propyl]acetamide. DR DrugBank; DB07984; 2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]-n-[(1S)-1-(hydroxymethyl)propyl]acetamide. DR DrugBank; DB02198; 2-Bromoacetyl Group. DR DrugBank; DB06736; Aceclofenac. DR DrugBank; DB13783; Acemetacin. DR DrugBank; DB00316; Acetaminophen. DR DrugBank; DB03667; Acetic Acid Salicyloyl-Amino-Ester. DR DrugBank; DB00945; Acetylsalicylic acid. DR DrugBank; DB01435; Antipyrine. DR DrugBank; DB01419; Antrafenine. DR DrugBank; DB04557; Arachidonic Acid. DR DrugBank; DB01014; Balsalazide. DR DrugBank; DB13501; Bendazac. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB00963; Bromfenac. DR DrugBank; DB13346; Bufexamac. DR DrugBank; DB13919; Candesartan. DR DrugBank; DB00796; Candesartan cilexetil. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB00821; Carprofen. DR DrugBank; DB00672; Chlorpropamide. DR DrugBank; DB01401; Choline magnesium trisalicylate. DR DrugBank; DB00250; Dapsone. DR DrugBank; DB00035; Desmopressin. DR DrugBank; DB09213; Dexibuprofen. DR DrugBank; DB09214; Dexketoprofen. DR DrugBank; DB00829; Diazepam. DR DrugBank; DB00586; Diclofenac. DR DrugBank; DB00711; Diethylcarbamazine. DR DrugBank; DB00861; Diflunisal. DR DrugBank; DB00154; Dihomo-gamma-linolenic acid. DR DrugBank; DB01075; Diphenhydramine. DR DrugBank; DB00470; Dronabinol. DR DrugBank; DB09215; Droxicam. DR DrugBank; DB00216; Eletriptan. DR DrugBank; DB00749; Etodolac. DR DrugBank; DB00773; Etoposide. DR DrugBank; DB00573; Fenoprofen. DR DrugBank; DB02266; Flufenamic acid. DR DrugBank; DB00712; Flurbiprofen. DR DrugBank; DB03753; Flurbiprofen Methyl Ester. DR DrugBank; DB11323; Glycol salicylate. DR DrugBank; DB01355; Hexobarbital. DR DrugBank; DB01892; Hyperforin. DR DrugBank; DB01050; Ibuprofen. DR DrugBank; DB00159; Icosapent. DR DrugBank; DB01181; Ifosfamide. DR DrugBank; DB00328; Indomethacin. DR DrugBank; DB01029; Irbesartan. DR DrugBank; DB01221; Ketamine. DR DrugBank; DB06738; Ketobemidone. DR DrugBank; DB01009; Ketoprofen. DR DrugBank; DB00465; Ketorolac. DR DrugBank; DB06725; Lornoxicam. DR DrugBank; DB09212; Loxoprofen. DR DrugBank; DB01283; Lumiracoxib. DR DrugBank; DB01397; Magnesium salicylate. DR DrugBank; DB00939; Meclofenamic acid. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB00784; Mefenamic acid. DR DrugBank; DB00814; Meloxicam. DR DrugBank; DB11201; Menthyl salicylate. DR DrugBank; DB00244; Mesalazine. DR DrugBank; DB04817; Metamizole. DR DrugBank; DB00350; Minoxidil. DR DrugBank; DB00471; Montelukast. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB00461; Nabumetone. DR DrugBank; DB00788; Naproxen. DR DrugBank; DB00731; Nateglinide. DR DrugBank; DB06802; Nepafenac. DR DrugBank; DB04552; Niflumic acid. DR DrugBank; DB12445; Nitroaspirin. DR DrugBank; DB01837; O-acetyl-L-serine. DR DrugBank; DB00991; Oxaprozin. DR DrugBank; DB03752; P-(2'-Iodo-5'-Thenoyl)Hydrotropic Acid. DR DrugBank; DB03783; Phenacetin. DR DrugBank; DB11071; Phenyl salicylate. DR DrugBank; DB00812; Phenylbutazone. DR DrugBank; DB00554; Piroxicam. DR DrugBank; DB13514; Pranoprofen. DR DrugBank; DB09288; Propacetamol. DR DrugBank; DB02110; Protoporphyrin Ix Containing Co. DR DrugBank; DB02709; Resveratrol. DR DrugBank; DB00533; Rofecoxib. DR DrugBank; DB00412; Rosiglitazone. DR DrugBank; DB00936; Salicylic acid. DR DrugBank; DB01399; Salsalate. DR DrugBank; DB06739; Seratrodast. DR DrugBank; DB00795; Sulfasalazine. DR DrugBank; DB00605; Sulindac. DR DrugBank; DB00870; Suprofen. DR DrugBank; DB09295; Talniflumate. DR DrugBank; DB00469; Tenoxicam. DR DrugBank; DB00857; Terbinafine. DR DrugBank; DB01041; Thalidomide. DR DrugBank; DB01600; Tiaprofenic acid. DR DrugBank; DB09216; Tolfenamic acid. DR DrugBank; DB00500; Tolmetin. DR DrugBank; DB05109; Trabectedin. DR DrugBank; DB08814; Triflusal. DR DrugBank; DB11079; Trolamine salicylate. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB00582; Voriconazole. DR DrugBank; DB00549; Zafirlukast. DR DrugBank; DB06737; Zaltoprofen. DR DrugBank; DB00744; Zileuton. DR DrugBank; DB01198; Zopiclone. DR DrugCentral; P23219; -. DR GuidetoPHARMACOLOGY; 1375; -. DR SwissLipids; SLP:000001103; -. DR MoonDB; P23219; Curated. DR PeroxiBase; 3320; HsPGHS01. DR GlyConnect; 1648; 1 N-Linked glycan (1 site). DR GlyCosmos; P23219; 3 sites, 1 glycan. DR GlyGen; P23219; 3 sites, 1 N-linked glycan (1 site). DR iPTMnet; P23219; -. DR PhosphoSitePlus; P23219; -. DR BioMuta; PTGS1; -. DR DMDM; 317373262; -. DR EPD; P23219; -. DR jPOST; P23219; -. DR MassIVE; P23219; -. DR MaxQB; P23219; -. DR PaxDb; 9606-ENSP00000354612; -. DR PeptideAtlas; P23219; -. DR ProteomicsDB; 4239; -. DR ProteomicsDB; 54063; -. [P23219-1] DR ProteomicsDB; 54064; -. [P23219-2] DR Pumba; P23219; -. DR Antibodypedia; 775; 774 antibodies from 45 providers. DR DNASU; 5742; -. DR Ensembl; ENST00000223423.8; ENSP00000223423.4; ENSG00000095303.17. [P23219-2] DR Ensembl; ENST00000362012.7; ENSP00000354612.2; ENSG00000095303.17. [P23219-1] DR Ensembl; ENST00000373698.7; ENSP00000362802.5; ENSG00000095303.17. [P23219-4] DR Ensembl; ENST00000540753.6; ENSP00000437709.1; ENSG00000095303.17. [P23219-3] DR GeneID; 5742; -. DR KEGG; hsa:5742; -. DR MANE-Select; ENST00000362012.7; ENSP00000354612.2; NM_000962.4; NP_000953.2. DR UCSC; uc004bmf.3; human. [P23219-1] DR AGR; HGNC:9604; -. DR CTD; 5742; -. DR DisGeNET; 5742; -. DR GeneCards; PTGS1; -. DR HGNC; HGNC:9604; PTGS1. DR HPA; ENSG00000095303; Tissue enhanced (intestine, skin, urinary bladder). DR MIM; 176805; gene. DR neXtProt; NX_P23219; -. DR OpenTargets; ENSG00000095303; -. DR PharmGKB; PA24346; -. DR VEuPathDB; HostDB:ENSG00000095303; -. DR eggNOG; KOG2408; Eukaryota. DR GeneTree; ENSGT00390000010743; -. DR HOGENOM; CLU_022428_0_0_1; -. DR InParanoid; P23219; -. DR OMA; LFGSQFQ; -. DR OrthoDB; 1086441at2759; -. DR PhylomeDB; P23219; -. DR TreeFam; TF329675; -. DR BioCyc; MetaCyc:HS01815-MONOMER; -. DR BRENDA; 1.14.99.1; 2681. DR PathwayCommons; P23219; -. DR Reactome; R-HSA-140180; COX reactions. DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR SABIO-RK; P23219; -. DR SignaLink; P23219; -. DR SIGNOR; P23219; -. DR UniPathway; UPA00662; -. DR BioGRID-ORCS; 5742; 6 hits in 1175 CRISPR screens. DR ChiTaRS; PTGS1; human. DR GeneWiki; PTGS1; -. DR GenomeRNAi; 5742; -. DR Pharos; P23219; Tclin. DR PRO; PR:P23219; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P23219; Protein. DR Bgee; ENSG00000095303; Expressed in stromal cell of endometrium and 180 other cell types or tissues. DR ExpressionAtlas; P23219; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:BHF-UCL. DR GO; GO:0019371; P:cyclooxygenase pathway; IDA:BHF-UCL. DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB. DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR CDD; cd00054; EGF_CA; 1. DR CDD; cd09816; prostaglandin_endoperoxide_synthase; 1. DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1. DR Gene3D; 2.10.25.10; Laminin; 1. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR019791; Haem_peroxidase_animal. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR037120; Haem_peroxidase_sf_animal. DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1. DR PANTHER; PTHR11903:SF6; PROSTAGLANDIN G_H SYNTHASE 1; 1. DR Pfam; PF03098; An_peroxidase; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. DR Genevisible; P23219; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Dioxygenase; Disulfide bond; KW EGF-like domain; Endoplasmic reticulum; Fatty acid biosynthesis; KW Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis; KW Lipid metabolism; Membrane; Metal-binding; Microsome; Oxidoreductase; KW Peroxidase; Prostaglandin biosynthesis; Prostaglandin metabolism; KW Reference proteome; Signal. FT SIGNAL 1..23 FT CHAIN 24..599 FT /note="Prostaglandin G/H synthase 1" FT /id="PRO_0000023868" FT DOMAIN 31..69 FT /note="EGF-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT ACT_SITE 206 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT ACT_SITE 384 FT /note="For cyclooxygenase activity" FT /evidence="ECO:0000250" FT BINDING 387 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT SITE 529 FT /note="Aspirin-acetylated serine" FT CARBOHYD 67 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 35..46 FT /evidence="ECO:0000250" FT DISULFID 36..158 FT /evidence="ECO:0000250" FT DISULFID 40..56 FT /evidence="ECO:0000250" FT DISULFID 58..68 FT /evidence="ECO:0000250" FT DISULFID 568..574 FT /evidence="ECO:0000250" FT VAR_SEQ 1..109 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046932" FT VAR_SEQ 1..32 FT /note="MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPV -> MRKPRLM (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053936" FT VAR_SEQ 1..3 FT /note="MSR -> MSRECDPGARWGIFLASGGALNARLSPSSLSSAG (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:16141368" FT /id="VSP_054862" FT VAR_SEQ 1..3 FT /note="MSR -> MSRECDPGARWGIFLASWWSLECQLSPSSLSSAG (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:16141368" FT /id="VSP_054863" FT VAR_SEQ 396..432 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:1587858" FT /id="VSP_004673" FT VARIANT 8 FT /note="W -> R (in dbSNP:rs1236913)" FT /evidence="ECO:0000269|PubMed:12192304, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:1587858, ECO:0000269|PubMed:1734857, FT ECO:0000269|PubMed:1907252, ECO:0000269|PubMed:2512924, FT ECO:0000269|Ref.10, ECO:0000269|Ref.8" FT /id="VAR_013451" FT VARIANT 17 FT /note="P -> L (in dbSNP:rs3842787)" FT /evidence="ECO:0000269|PubMed:12192304, ECO:0000269|Ref.8" FT /id="VAR_013452" FT VARIANT 53 FT /note="R -> H (in dbSNP:rs3842789)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_019161" FT VARIANT 149 FT /note="R -> L (in dbSNP:rs10306140)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_019162" FT VARIANT 185 FT /note="K -> T (in dbSNP:rs3842792)" FT /id="VAR_056663" FT VARIANT 237 FT /note="L -> M (in dbSNP:rs5789)" FT /evidence="ECO:0000269|PubMed:15308583, ECO:0000269|Ref.8" FT /id="VAR_019163" FT VARIANT 341 FT /note="K -> R (in dbSNP:rs3842799)" FT /id="VAR_056664" FT VARIANT 359 FT /note="K -> R (in dbSNP:rs5791)" FT /id="VAR_013453" FT VARIANT 443 FT /note="I -> V (in dbSNP:rs5792)" FT /id="VAR_013454" FT VARIANT 481 FT /note="V -> I (in dbSNP:rs5794)" FT /evidence="ECO:0000269|PubMed:15308583" FT /id="VAR_028017" FT MUTAGEN 529 FT /note="S->N: Abolishes cyclooxygenase activity." FT /evidence="ECO:0000269|PubMed:1907252" FT CONFLICT 12 FT /note="F -> L (in Ref. 1; AAA36439)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="R -> L (in Ref. 1; AAA36439)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="M -> T (in Ref. 1; AAA36439)" FT /evidence="ECO:0000305" FT CONFLICT 423 FT /note="D -> G (in Ref. 7; BAG65237)" FT /evidence="ECO:0000305" FT HELIX 34..37 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 65..68 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 73..79 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 85..91 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 96..103 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 163..166 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 173..179 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 195..205 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 230..233 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 238..243 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 265..267 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 280..282 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 287..290 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 295..318 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 324..345 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 347..352 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 362..365 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 378..383 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 403..406 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 412..425 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 441..443 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 444..456 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 462..468 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 475..477 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 478..481 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 484..494 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 497..499 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 502..507 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 516..518 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 519..533 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 537..539 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 541..543 FT /evidence="ECO:0007829|PDB:6Y3C" FT TURN 546..550 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 552..558 FT /evidence="ECO:0007829|PDB:6Y3C" FT HELIX 564..567 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 570..573 FT /evidence="ECO:0007829|PDB:6Y3C" FT STRAND 578..580 FT /evidence="ECO:0007829|PDB:6Y3C" SQ SEQUENCE 599 AA; 68686 MW; 1F4F734BCD00346D CRC64; MSRSLLLWFL LFLLLLPPLP VLLADPGAPT PVNPCCYYPC QHQGICVRFG LDRYQCDCTR TGYSGPNCTI PGLWTWLRNS LRPSPSFTHF LLTHGRWFWE FVNATFIREM LMRLVLTVRS NLIPSPPTYN SAHDYISWES FSNVSYYTRI LPSVPKDCPT PMGTKGKKQL PDAQLLARRF LLRRKFIPDP QGTNLMFAFF AQHFTHQFFK TSGKMGPGFT KALGHGVDLG HIYGDNLERQ YQLRLFKDGK LKYQVLDGEM YPPSVEEAPV LMHYPRGIPP QSQMAVGQEV FGLLPGLMLY ATLWLREHNR VCDLLKAEHP TWGDEQLFQT TRLILIGETI KIVIEEYVQQ LSGYFLQLKF DPELLFGVQF QYRNRIAMEF NHLYHWHPLM PDSFKVGSQE YSYEQFLFNT SMLVDYGVEA LVDAFSRQIA GRIGGGRNMD HHILHVAVDV IRESREMRLQ PFNEYRKRFG MKPYTSFQEL VGEKEMAAEL EELYGDIDAL EFYPGLLLEK CHPNSIFGES MIEIGAPFSL KGLLGNPICS PEYWKPSTFG GEVGFNIVKT ATLKKLVCLN TKTCPYVSFR VPDASQDDGP AVERPSTEL //