ID PGH2_MOUSE Reviewed; 604 AA. AC Q05769; Q543K3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 225. DE RecName: Full=Prostaglandin G/H synthase 2 {ECO:0000305}; DE EC=1.14.99.1 {ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:22942274}; DE AltName: Full=Cyclooxygenase-2; DE Short=COX-2; DE AltName: Full=Glucocorticoid-regulated inflammatory cyclooxygenase; DE AltName: Full=Gripghs; DE AltName: Full=Macrophage activation-associated marker protein P71/73; DE AltName: Full=PES-2; DE AltName: Full=PHS II; DE AltName: Full=Prostaglandin H2 synthase 2; DE Short=PGH synthase 2; DE Short=PGHS-2; DE AltName: Full=Prostaglandin-endoperoxide synthase 2; DE AltName: Full=TIS10 protein; DE Flags: Precursor; GN Name=Ptgs2 {ECO:0000312|MGI:MGI:97798}; GN Synonyms=Cox-2, Cox2, Pghs-b, Tis10; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=SWR/J; RX PubMed=1712772; DOI=10.1016/s0021-9258(18)98774-0; RA Kujubu D.A., Fletcher B.S., Varnum B.C., Lim R.W., Herschman H.R.; RT "TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, RT encodes a novel prostaglandin synthase/cyclooxygenase homologue."; RL J. Biol. Chem. 266:12866-12872(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RX PubMed=1339449; DOI=10.1016/s0021-9258(18)42840-2; RA Fletcher B.S., Kujubu D.A., Perrin D.M., Herschman H.R.; RT "Structure of the mitogen-inducible TIS10 gene and demonstration that the RT TIS10-encoded protein is a functional prostaglandin G/H synthase."; RL J. Biol. Chem. 267:4338-4344(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1419907; RA Ryseck R.-P., Raynoschek C., Macdonald-Bravo H., Dorfman K., Mattei M.-G., RA Bravo R.; RT "Identification of an immediate early gene, pghs-B, whose protein product RT has prostaglandin synthase/cyclooxygenase activity."; RL Cell Growth Differ. 3:443-450(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1594589; DOI=10.1073/pnas.89.11.4888; RA O'Banion M.K., Winn V.D., Young D.A.; RT "cDNA cloning and functional activity of a glucocorticoid-regulated RT inflammatory cyclooxygenase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:4888-4892(1992). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Hippocampus, Mammary gland, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-360. RX PubMed=1744122; DOI=10.1016/s0021-9258(18)54491-4; RA O'Banion M.K., Sadowski H.B., Winn V., Young D.A.; RT "A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a RT cyclooxygenase-related protein."; RL J. Biol. Chem. 266:23261-23267(1991). RN [8] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=8482922; DOI=10.1002/jlb.53.4.411; RA Phillips T.A., Kujubu D.A., Mackay R.J., Herschman H.R., Russell S.W., RA Pace J.L.; RT "The mouse macrophage activation-associated marker protein, p71/73, is an RT inducible prostaglandin endoperoxide synthase (cyclooxygenase)."; RL J. Leukoc. Biol. 53:411-419(1993). RN [9] RP GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580, AND LACK OF RP GLYCOSYLATION AT ASN-592. RX PubMed=8349699; DOI=10.1016/s0021-9258(17)46835-9; RA Otto J.C., Dewitt D.L., Smith W.L.; RT "N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their RT orientations in the endoplasmic reticulum."; RL J. Biol. Chem. 268:18234-18242(1993). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=9545330; DOI=10.1074/jbc.273.16.9886; RA Spencer A.G., Woods J.W., Arakawa T., Singer I.I., Smith W.L.; RT "Subcellular localization of prostaglandin endoperoxide H synthases-1 and RT -2 by immunoelectron microscopy."; RL J. Biol. Chem. 273:9886-9893(1998). RN [11] RP CATALYTIC ACTIVITY. RX PubMed=12244105; DOI=10.1074/jbc.m206788200; RA Kozak K.R., Crews B.C., Morrow J.D., Wang L.H., Ma Y.H., Weinander R., RA Jakobsson P.J., Marnett L.J.; RT "Metabolism of the endocannabinoids, 2-arachidonylglycerol and anandamide, RT into prostaglandin, thromboxane, and prostacyclin glycerol esters and RT ethanolamides."; RL J. Biol. Chem. 277:44877-44885(2002). RN [12] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=22465430; DOI=10.1053/j.gastro.2012.03.037; RA Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.; RT "Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic RT mesenchymal stem cells in mice."; RL Gastroenterology 143:110-121(2012). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-374. RX PubMed=22942274; DOI=10.1074/jbc.m112.381202; RA Musee J., Marnett L.J.; RT "Prostaglandin H synthase-2-catalyzed oxygenation of 2-arachidonoylglycerol RT is more sensitive to peroxide tone than oxygenation of arachidonic acid."; RL J. Biol. Chem. 287:37383-37394(2012). RN [14] RP FUNCTION, ACETYLATION AT SER-565, AND MUTAGENESIS OF SER-565. RX PubMed=29662056; DOI=10.1038/s41467-018-03674-2; RA Lee J.Y., Han S.H., Park M.H., Baek B., Song I.S., Choi M.K., Takuwa Y., RA Ryu H., Kim S.H., He X., Schuchman E.H., Bae J.S., Jin H.K.; RT "Neuronal SphK1 acetylates COX2 and contributes to pathogenesis in a model RT of Alzheimer's Disease."; RL Nat. Commun. 9:1479-1479(2018). RN [15] 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 [16] 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 [17] {ECO:0007744|PDB:1CX2, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH (S)-FLURBIPROFEN; RP INDOMETHACIN; HEME AND RP 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE, COFACTOR, RP GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396, AND DISULFIDE BONDS. RX PubMed=8967954; DOI=10.1038/384644a0; RA Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J., Stegeman R.A., RA Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D., Seibert K., RA Isakson P.C., Stallings W.C.; RT "Structural basis for selective inhibition of cyclooxygenase-2 by anti- RT inflammatory agents."; RL Nature 384:644-648(1996). RN [18] RP ERRATUM OF PUBMED:8967954. RA Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J., Stegeman R.A., RA Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D., Seibert K., RA Isakson P.C., Stallings W.C.; RL Nature 385:555-555(1997). RN [19] {ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1DDX} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-569 IN COMPLEX WITH RP ARACHIDONIC ACID, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396, AND RP DISULFIDE BONDS. RX PubMed=10811226; DOI=10.1038/35011103; RA Kiefer J.R., Pawlitz J.L., Moreland K.T., Stegeman R.A., Hood W.F., RA Gierse J.K., Stevens A.M., Goodwin D.C., Rowlinson S.W., Marnett L.J., RA Stallings W.C., Kurumbail R.G.; RT "Structural insights into the stereochemistry of the cyclooxygenase RT reaction."; RL Nature 405:97-101(2000). RN [20] {ECO:0007744|PDB:1PXX} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME AND DICLOFENAC, RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BONDS, ACTIVITY RP REGULATION, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396. RX PubMed=12925531; DOI=10.1074/jbc.m305481200; RA Rowlinson S.W., Kiefer J.R., Prusakiewicz J.J., Pawlitz J.L., Kozak K.R., RA Kalgutkar A.S., Stallings W.C., Kurumbail R.G., Marnett L.J.; RT "A novel mechanism of cyclooxygenase-2 inhibition involving interactions RT with Ser-530 and Tyr-385."; RL J. Biol. Chem. 278:45763-45769(2003). RN [21] {ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-604 IN COMPLEX WITH HEME; RP ACRYLIC ACID; ARACHIDONIC ACID AND DOCOSAHEXAENOIC ACID, CATALYTIC RP ACTIVITY, ACTIVE SITE, SUBUNIT, COFACTOR, FUNCTION, DISULFIDE BONDS, RP MUTAGENESIS OF LEU-517 AND ASN-580, AND GLYCOSYLATION AT ASN-53; ASN-130; RP ASN-396 AND ASN-580. RX PubMed=20463020; DOI=10.1074/jbc.m110.119867; RA Vecchio A.J., Simmons D.M., Malkowski M.G.; RT "Structural basis of fatty acid substrate binding to cyclooxygenase-2."; RL J. Biol. Chem. 285:22152-22163(2010). RN [22] {ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB} RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 18-604 IN COMPLEXES WITH HEME AND RP NAPROXEN ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396. RX PubMed=20810665; DOI=10.1074/jbc.m110.162982; RA Duggan K.C., Walters M.J., Musee J., Harp J.M., Kiefer J.R., Oates J.A., RA Marnett L.J.; RT "Molecular basis for cyclooxygenase inhibition by the non-steroidal anti- RT inflammatory drug naproxen."; RL J. Biol. Chem. 285:34950-34959(2010). RN [23] {ECO:0007744|PDB:3QH0} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), GLYCOSYLATION AT ASN-53; ASN-130 RP AND ASN-396, AND DISULFIDE BONDS. RX PubMed=21467029; DOI=10.1074/jbc.m111.231969; RA Dong L., Vecchio A.J., Sharma N.P., Jurban B.J., Malkowski M.G., RA Smith W.L.; RT "Human cyclooxygenase-2 is a sequence homodimer that functions as a RT conformational heterodimer."; RL J. Biol. Chem. 286:19035-19046(2011). RN [24] {ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-599 IN COMPLEX WITH HEME; RP ACRYLIC ACID AND ARACHIDONIC ACID, FUNCTION, CATALYTIC ACTIVITY, RP GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396, AND DISULFIDE BONDS. RX PubMed=21489986; DOI=10.1074/jbc.m111.230367; RA Vecchio A.J., Malkowski M.G.; RT "The structural basis of endocannabinoid oxygenation by cyclooxygenase-2."; RL J. Biol. Chem. 286:20736-20745(2011). CC -!- FUNCTION: Dual cyclooxygenase and peroxidase in the biosynthesis CC pathway of prostanoids, a class of C20 oxylipins mainly derived from CC arachidonate, with a particular role in the inflammatory response CC (PubMed:22942274, PubMed:12925531, PubMed:20463020, PubMed:20810665, CC PubMed:21489986). The cyclooxygenase activity oxygenates arachidonate CC (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 CC (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy CC endoperoxide PGH2, the precursor of all 2-series prostaglandins and CC thromboxanes. This complex transformation is initiated by abstraction CC of hydrogen at carbon 13 (with S-stereochemistry), followed by CC insertion of molecular O2 to form the endoperoxide bridge between CC carbon 9 and 11 that defines prostaglandins. The insertion of a second CC molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in CC PGG2 that is then reduced to PGH2 by two electrons (PubMed:22942274, CC PubMed:12925531, PubMed:20463020, PubMed:20810665, PubMed:21489986). CC Similarly catalyzes successive cyclooxygenation and peroxidation of CC dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, CC C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3- CC series prostaglandins (By similarity). In an alternative pathway of CC prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to CC prostanoid lysophopholipids, which are then hydrolyzed by intracellular CC phospholipases to release free prostanoids (By similarity). Metabolizes CC 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process CC that can contribute to pain response (By similarity). Generates lipid CC mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a CC lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds CC and then reduces them to corresponding alcohols (By similarity). Plays CC a role in the generation of resolution phase interaction products CC (resolvins) during both sterile and infectious inflammation. CC Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor CC of the D-series resolvins (RvDs). As a component of the biosynthetic CC pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, CC C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 CC and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial CC cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a CC precursor for 13-series resolvins (RvTs) shown to activate macrophage CC phagocytosis during bacterial infection (By similarity). In activated CC leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates CC (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (By similarity). Can CC also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as CC substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and CC stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)- CC octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)- CC octadecadienoate) its major products (By similarity). During CC neuroinflammation, plays a role in neuronal secretion of specialized CC preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic CC microglia (PubMed:29662056). {ECO:0000250|UniProtKB:P35354, CC ECO:0000250|UniProtKB:P79208, ECO:0000269|PubMed:12925531, CC ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, CC ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:22942274, CC ECO:0000269|PubMed:29662056}. 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:12925531, ECO:0000269|PubMed:20463020, CC ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, CC ECO:0000269|PubMed:22942274}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; CC Evidence={ECO:0000305|PubMed:12925531, ECO:0000305|PubMed:20463020, CC ECO:0000305|PubMed:20810665, ECO:0000305|PubMed:21489986, CC ECO:0000305|PubMed:22942274}; 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:12244105, CC ECO:0000269|PubMed:22942274}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; CC Evidence={ECO:0000305|PubMed:12244105, ECO:0000305|PubMed:22942274}; 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:12244105, ECO:0000269|PubMed:22942274}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; CC Evidence={ECO:0000305|PubMed:12244105, ECO:0000305|PubMed:22942274}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 O2 = prostaglandin CC G3; Xref=Rhea:RHEA:50444, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, CC ChEBI:CHEBI:133133; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50445; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + prostaglandin G3 = A + H2O + prostaglandin H3; CC Xref=Rhea:RHEA:50448, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:133133, ChEBI:CHEBI:133134; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50449; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(8Z,11Z,14Z)-eicosatrienoate + 2 O2 = prostaglandin G1; CC Xref=Rhea:RHEA:50424, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, CC ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50425; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + prostaglandin G1 = A + H2O + prostaglandin H1; CC Xref=Rhea:RHEA:50432, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:90793, ChEBI:CHEBI:133084; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50433; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3- CC phosphoethanolamine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3- CC phosphoethanolamine; Xref=Rhea:RHEA:54204, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:76091, ChEBI:CHEBI:138098; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54205; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine + AH2 = CC 2-(prostaglandin H2)-sn-glycero-3-phosphoethanolamine + A + H2O; CC Xref=Rhea:RHEA:54208, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:138098, ChEBI:CHEBI:138099; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54209; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine CC + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphocholine; CC Xref=Rhea:RHEA:54212, ChEBI:CHEBI:15379, ChEBI:CHEBI:76079, CC ChEBI:CHEBI:138100; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54213; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphocholine + AH2 = 2- CC (prostaglandin H2)-sn-glycero-3-phosphocholine + A + H2O; CC Xref=Rhea:RHEA:54216, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:138100, ChEBI:CHEBI:138101; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54217; CC Evidence={ECO:0000250|UniProtKB:P35354}; 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:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine CC + AH2 + O2 = 2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn- CC glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53684, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137584; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53685; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine CC + AH2 + O2 = 2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn- CC glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53680, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137583; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53681; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine CC + AH2 + O2 = 2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn- CC glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53676, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137582; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53677; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 9-hydroxy-(10E,12Z)- CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:50864, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:133820; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50865; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 13-hydroxy-(9Z,11E)- CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:50860, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:133819; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50861; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (15R)-hydroxy- CC (5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50856, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78837; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50857; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (11R)-hydroxy- CC (5Z,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50852, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78836; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50853; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (11R)- CC hydroxy-(5Z,8Z,12E,14Z,17Z)-eicosapentaenoate + A + H2O; CC Xref=Rhea:RHEA:50848, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, CC ChEBI:CHEBI:90820; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50849; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18S)- CC hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; CC Xref=Rhea:RHEA:50200, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, CC ChEBI:CHEBI:132083; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50201; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18R)- CC hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; CC Xref=Rhea:RHEA:48836, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, CC ChEBI:CHEBI:90818; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48837; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15R)- CC hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; CC Xref=Rhea:RHEA:48840, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, CC ChEBI:CHEBI:90819; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48841; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15S)- CC hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; CC Xref=Rhea:RHEA:50196, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, CC ChEBI:CHEBI:132087; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50197; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + AH2 + O2 = 13R- CC hydroxy-(7Z,10Z,14E,16Z,19Z)-docosapentaenoate + A + H2O; CC Xref=Rhea:RHEA:48852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77224, CC ChEBI:CHEBI:90824; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48853; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 13- CC hydroxy-(4Z,7Z,10Z,14E,16Z,19Z)-docosahexaenoate + A + H2O; CC Xref=Rhea:RHEA:48820, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, CC ChEBI:CHEBI:90815; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48821; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = CC (5S,15R)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; CC Xref=Rhea:RHEA:48812, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, CC ChEBI:CHEBI:90812; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48813; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 17R- CC hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + A + H2O; CC Xref=Rhea:RHEA:48816, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, CC ChEBI:CHEBI:90814; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48817; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = CC (5S,15S)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; CC Xref=Rhea:RHEA:48808, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, CC ChEBI:CHEBI:90813; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48809; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = CC (5S,11R)-dihydroxy-(6E,8Z,12E,14Z)-eicosatetraenoate + A + H2O; CC Xref=Rhea:RHEA:48804, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, CC ChEBI:CHEBI:90810; Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48805; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 2 O2 = 2- CC glyceryl-prostaglandin G2; Xref=Rhea:RHEA:45288, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:52392, ChEBI:CHEBI:85165; CC Evidence={ECO:0000269|PubMed:12244105, ECO:0000269|PubMed:22942274}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45289; CC Evidence={ECO:0000305|PubMed:12244105, ECO:0000305|PubMed:22942274}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-glyceryl-prostaglandin G2 + AH2 = 2-glyceryl-prostaglandin CC H2 + A + H2O; Xref=Rhea:RHEA:45292, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:85165, CC ChEBI:CHEBI:85166; Evidence={ECO:0000269|PubMed:12244105, CC ECO:0000269|PubMed:22942274}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45293; CC Evidence={ECO:0000305|PubMed:12244105, ECO:0000305|PubMed:22942274}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15R)-hydroperoxy- CC (5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:42284, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82626; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42285; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 11R-hydroperoxy- CC (5Z,8Z,12E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:42280, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82628; CC Evidence={ECO:0000250|UniProtKB:P35354}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42281; CC Evidence={ECO:0000250|UniProtKB:P35354}; 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:P79208}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; CC Evidence={ECO:0000250|UniProtKB:P79208}; 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:P79208}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; CC Evidence={ECO:0000250|UniProtKB:P79208}; 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:P79208}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; CC Evidence={ECO:0000250|UniProtKB:P79208}; 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:P79208}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; CC Evidence={ECO:0000250|UniProtKB:P79208}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, CC ECO:0000269|PubMed:8967954}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, CC ECO:0000269|PubMed:8967954}; CC -!- ACTIVITY REGULATION: Inhibited by the nonsteroidal anti-inflammatory CC drugs aspirin, naproxen, diclofenac, meclofenamic acid, indomethacin CC and their analogs. {ECO:0000269|PubMed:12925531, CC ECO:0000269|PubMed:20810665}. CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis. CC {ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, CC ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10811226, CC ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, CC ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, CC ECO:0000269|PubMed:8967954}. CC -!- INTERACTION: CC Q05769; Q9Z0J4: Nos1; NbExp=4; IntAct=EBI-298933, EBI-397596; CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9545330}; CC Peripheral membrane protein. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Nucleus CC inner membrane {ECO:0000305|PubMed:9545330}; Peripheral membrane CC protein. Nucleus outer membrane {ECO:0000305|PubMed:9545330}; CC Peripheral membrane protein. Note=Detected on the lumenal side of the CC endoplasmic reticulum and nuclear envelope. CC {ECO:0000250|UniProtKB:P35354}. CC -!- TISSUE SPECIFICITY: Following colon injury, expressed in the wound bed CC mesenchyme during the first phase of repair, probably by colonic CC mesenchymal stem cells (at protein level). CC {ECO:0000269|PubMed:22465430}. CC -!- DEVELOPMENTAL STAGE: During colonic wound repair, highly up-regulated CC (more than 1600-fold) in the mesenchyme of the wound bed 2 days after CC injury as compared to uninjured mucosa. Further increase in expression CC is observed at day 4 following injury (close to 2200-fold). Down- CC regulated at day 6 (only 93-fold increase as compared to uninjured CC mucosa). {ECO:0000269|PubMed:22465430}. CC -!- INDUCTION: By cytokines and mitogens. {ECO:0000269|PubMed:1339449}. CC -!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S- CC nitrosylation may take place on different Cys residues in addition to CC Cys-526. {ECO:0000250|UniProtKB:P35354}. CC -!- PTM: Acetylated at Ser-565 by SPHK1. During neuroinflammation, CC acetylation by SPHK1 promotes neuronal secretion of specialized CC preresolving mediators (SPMs), especially 15-R-lipoxin A4, which CC results in an increase of phagocytic microglia. CC {ECO:0000269|PubMed:29662056}. CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit defects in colonic mucosal CC wound repair. {ECO:0000269|PubMed:22465430}. 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 --------------------------------------------------------------------------- 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; M64291; AAA39924.1; -; mRNA. DR EMBL; M94967; AAA39918.1; -; mRNA. DR EMBL; M82866; AAA40448.1; -; Genomic_DNA. DR EMBL; M82862; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M82863; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M82864; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M82865; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M88242; AAA37740.1; -; mRNA. DR EMBL; AK049923; BAC33986.1; -; mRNA. DR EMBL; AK144956; BAE26154.1; -; mRNA. DR EMBL; AK166221; BAE38639.1; -; mRNA. DR EMBL; AK172161; BAE42855.1; -; mRNA. DR EMBL; CH466520; EDL39487.1; -; Genomic_DNA. DR CCDS; CCDS15353.1; -. DR PIR; A49010; A49010. DR RefSeq; NP_035328.2; NM_011198.4. DR PDB; 1CVU; X-ray; 2.40 A; A/B=18-569. DR PDB; 1CX2; X-ray; 3.00 A; A/B/C/D=18-604. DR PDB; 1DDX; X-ray; 3.00 A; A/B/C/D=18-569. DR PDB; 1PXX; X-ray; 2.90 A; A/B/C/D=1-604. DR PDB; 3HS5; X-ray; 2.10 A; A/B=20-604. DR PDB; 3HS6; X-ray; 2.40 A; A/B=20-604. DR PDB; 3HS7; X-ray; 2.65 A; A/B=20-604. DR PDB; 3KRK; X-ray; 2.40 A; A/B=20-604. DR PDB; 3LN0; X-ray; 2.20 A; A/B/C/D=18-604. DR PDB; 3LN1; X-ray; 2.40 A; A/B/C/D=18-604. DR PDB; 3MDL; X-ray; 2.20 A; A/B=20-599. DR PDB; 3MQE; X-ray; 2.80 A; A/B/C/D=18-604. DR PDB; 3NT1; X-ray; 1.73 A; A/B=18-604. DR PDB; 3NTB; X-ray; 2.27 A; A/B/C/D=18-604. DR PDB; 3NTG; X-ray; 2.19 A; A/B/C/D=18-569. DR PDB; 3OLT; X-ray; 2.45 A; A/B=20-604. DR PDB; 3OLU; X-ray; 2.35 A; A/B=20-604. DR PDB; 3PGH; X-ray; 2.50 A; A/B/C/D=18-604. DR PDB; 3Q7D; X-ray; 2.40 A; A/B=18-604. DR PDB; 3QH0; X-ray; 2.10 A; A/B=1-604. DR PDB; 3QMO; X-ray; 3.00 A; A/B=1-604. DR PDB; 3RR3; X-ray; 2.84 A; A/B/C/D=18-577. DR PDB; 3TZI; X-ray; 2.15 A; A/B=20-604. DR PDB; 4COX; X-ray; 2.90 A; A/B/C/D=18-604. DR PDB; 4E1G; X-ray; 2.10 A; A/B=1-604. DR PDB; 4FM5; X-ray; 2.81 A; A/B/C/D=1-604. DR PDB; 4M10; X-ray; 2.01 A; A/B/C/D=18-604. DR PDB; 4M11; X-ray; 2.45 A; A/B/C/D=18-569. DR PDB; 4OTJ; X-ray; 2.11 A; A/B/C/D=18-604. DR PDB; 4OTY; X-ray; 2.35 A; A/B=18-604. DR PDB; 4PH9; X-ray; 1.81 A; A/B=20-568. DR PDB; 4RRW; X-ray; 2.57 A; A/B/C/D=18-604. DR PDB; 4RRX; X-ray; 2.78 A; A/B=18-604. DR PDB; 4RRY; X-ray; 2.43 A; A/B/C/D=18-604. DR PDB; 4RRZ; X-ray; 2.57 A; A/B/C/D=18-604. DR PDB; 4RS0; X-ray; 2.81 A; A=18-604. DR PDB; 4RUT; X-ray; 2.16 A; A/B/C/D=18-604. DR PDB; 4Z0L; X-ray; 2.29 A; A/B/C/D=18-604. DR PDB; 5COX; X-ray; 3.00 A; A/B/C/D=18-604. DR PDB; 5FDQ; X-ray; 1.90 A; A/B=20-604. DR PDB; 5JVY; X-ray; 2.36 A; A/B=20-568. DR PDB; 5JVZ; X-ray; 2.62 A; A/B=20-569. DR PDB; 5JW1; X-ray; 2.82 A; A/B=20-569. DR PDB; 5W58; X-ray; 2.27 A; A=18-604. DR PDB; 6BL3; X-ray; 2.22 A; A/B/C/D=18-604. DR PDB; 6BL4; X-ray; 2.22 A; A/B/C/D=18-604. DR PDB; 6COX; X-ray; 2.80 A; A/B=18-604. DR PDB; 6OFY; X-ray; 2.20 A; A/B=20-568. DR PDB; 6V3R; X-ray; 2.66 A; A/B/C/D=18-604. DR PDB; 8ET0; X-ray; 2.15 A; A/B=18-604. DR PDBsum; 1CVU; -. DR PDBsum; 1CX2; -. DR PDBsum; 1DDX; -. DR PDBsum; 1PXX; -. DR PDBsum; 3HS5; -. DR PDBsum; 3HS6; -. DR PDBsum; 3HS7; -. DR PDBsum; 3KRK; -. DR PDBsum; 3LN0; -. DR PDBsum; 3LN1; -. DR PDBsum; 3MDL; -. DR PDBsum; 3MQE; -. DR PDBsum; 3NT1; -. DR PDBsum; 3NTB; -. DR PDBsum; 3NTG; -. DR PDBsum; 3OLT; -. DR PDBsum; 3OLU; -. DR PDBsum; 3PGH; -. DR PDBsum; 3Q7D; -. DR PDBsum; 3QH0; -. DR PDBsum; 3QMO; -. DR PDBsum; 3RR3; -. DR PDBsum; 3TZI; -. DR PDBsum; 4COX; -. DR PDBsum; 4E1G; -. DR PDBsum; 4FM5; -. DR PDBsum; 4M10; -. DR PDBsum; 4M11; -. DR PDBsum; 4OTJ; -. DR PDBsum; 4OTY; -. DR PDBsum; 4PH9; -. DR PDBsum; 4RRW; -. DR PDBsum; 4RRX; -. DR PDBsum; 4RRY; -. DR PDBsum; 4RRZ; -. DR PDBsum; 4RS0; -. DR PDBsum; 4RUT; -. DR PDBsum; 4Z0L; -. DR PDBsum; 5COX; -. DR PDBsum; 5FDQ; -. DR PDBsum; 5JVY; -. DR PDBsum; 5JVZ; -. DR PDBsum; 5JW1; -. DR PDBsum; 5W58; -. DR PDBsum; 6BL3; -. DR PDBsum; 6BL4; -. DR PDBsum; 6COX; -. DR PDBsum; 6OFY; -. DR PDBsum; 6V3R; -. DR PDBsum; 8ET0; -. DR AlphaFoldDB; Q05769; -. DR SMR; Q05769; -. DR BioGRID; 202463; 7. DR DIP; DIP-31082N; -. DR IntAct; Q05769; 3. DR MINT; Q05769; -. DR STRING; 10090.ENSMUSP00000035065; -. DR BindingDB; Q05769; -. DR ChEMBL; CHEMBL4321; -. DR DrugCentral; Q05769; -. DR GuidetoPHARMACOLOGY; 1376; -. DR SwissLipids; SLP:000001129; -. DR PeroxiBase; 3360; MmPGHS02. DR GlyConnect; 514; 7 N-Linked glycans (5 sites). DR GlyCosmos; Q05769; 4 sites, 13 glycans. DR GlyGen; Q05769; 4 sites, 12 N-linked glycans (4 sites). DR iPTMnet; Q05769; -. DR PhosphoSitePlus; Q05769; -. DR SwissPalm; Q05769; -. DR PaxDb; 10090-ENSMUSP00000035065; -. DR PeptideAtlas; Q05769; -. DR ProteomicsDB; 301805; -. DR Pumba; Q05769; -. DR Antibodypedia; 776; 1258 antibodies from 49 providers. DR DNASU; 19225; -. DR Ensembl; ENSMUST00000035065.9; ENSMUSP00000035065.8; ENSMUSG00000032487.9. DR GeneID; 19225; -. DR KEGG; mmu:19225; -. DR UCSC; uc007cxv.1; mouse. DR AGR; MGI:97798; -. DR CTD; 5743; -. DR MGI; MGI:97798; Ptgs2. DR VEuPathDB; HostDB:ENSMUSG00000032487; -. DR eggNOG; KOG2408; Eukaryota. DR GeneTree; ENSGT00390000010743; -. DR HOGENOM; CLU_022428_0_0_1; -. DR InParanoid; Q05769; -. DR OMA; NVHYGYK; -. DR OrthoDB; 1086441at2759; -. DR PhylomeDB; Q05769; -. DR TreeFam; TF329675; -. DR BRENDA; 1.14.99.1; 3474. DR Reactome; R-MMU-197264; Nicotinamide salvaging. DR Reactome; R-MMU-2142770; Synthesis of 15-eicosatetraenoic acid derivatives. DR Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR Reactome; R-MMU-9018677; Biosynthesis of DHA-derived SPMs. DR Reactome; R-MMU-9018679; Biosynthesis of EPA-derived SPMs. DR Reactome; R-MMU-9025094; Biosynthesis of DPAn-3 SPMs. DR Reactome; R-MMU-9027604; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives. DR UniPathway; UPA00662; -. DR BioGRID-ORCS; 19225; 4 hits in 78 CRISPR screens. DR ChiTaRS; mt-Co2; mouse. DR EvolutionaryTrace; Q05769; -. DR PRO; PR:Q05769; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q05769; Protein. DR Bgee; ENSMUSG00000032487; Expressed in granulocyte and 112 other cell types or tissues. DR ExpressionAtlas; Q05769; baseline and differential. DR GO; GO:0005901; C:caveola; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB. DR GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. 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; ISO:MGI. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0001525; P:angiogenesis; ISO:MGI. DR GO; GO:0030282; P:bone mineralization; ISO:MGI. DR GO; GO:0050873; P:brown fat cell differentiation; IMP:BHF-UCL. DR GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl. DR GO; GO:0071498; P:cellular response to fluid shear stress; IDA:MGI. DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IMP:CAFA. DR GO; GO:0019371; P:cyclooxygenase pathway; IDA:UniProtKB. DR GO; GO:0046697; P:decidualization; IMP:MGI. DR GO; GO:0007566; P:embryo implantation; IMP:MGI. DR GO; GO:0042633; P:hair cycle; IEA:Ensembl. DR GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB. DR GO; GO:0007612; P:learning; ISO:MGI. DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISO:MGI. DR GO; GO:0007613; P:memory; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CAFA. DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:MGI. DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:CAFA. DR GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IMP:CAFA. DR GO; GO:0045986; P:negative regulation of smooth muscle contraction; ISO:MGI. DR GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; ISO:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:BHF-UCL. DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0031622; P:positive regulation of fever generation; IDA:BHF-UCL. DR GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISO:MGI. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:CAFA. DR GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; ISO:MGI. DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:CAFA. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI. DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISO:MGI. DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI. DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:MGI. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI. DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI. DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB. DR GO; GO:0032310; P:prostaglandin secretion; IMP:MGI. DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI. DR GO; GO:0150077; P:regulation of neuroinflammatory response; IDA:UniProtKB. DR GO; GO:1990776; P:response to angiotensin; IEA:Ensembl. DR GO; GO:0034097; P:response to cytokine; ISO:MGI. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl. DR GO; GO:0009750; P:response to fructose; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI. DR GO; GO:0010042; P:response to manganese ion; IEA:Ensembl. DR GO; GO:0009624; P:response to nematode; IMP:MGI. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. 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:SF8; PROSTAGLANDIN G_H SYNTHASE 2; 1. DR Pfam; PF03098; An_peroxidase; 1. DR Pfam; PF00008; EGF; 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; Q05769; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Dioxygenase; Direct protein sequencing; KW Disulfide bond; Endoplasmic reticulum; Fatty acid biosynthesis; KW Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis; KW Lipid metabolism; Membrane; Metal-binding; Microsome; Nucleus; KW Oxidoreductase; Peroxidase; Prostaglandin biosynthesis; KW Prostaglandin metabolism; Reference proteome; S-nitrosylation; Signal. FT SIGNAL 1..17 FT CHAIN 18..604 FT /note="Prostaglandin G/H synthase 2" FT /id="PRO_0000023876" FT DOMAIN 18..55 FT /note="EGF-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT ACT_SITE 193 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, FT ECO:0000269|PubMed:20463020" FT ACT_SITE 371 FT /note="For cyclooxygenase activity" FT /evidence="ECO:0000269|PubMed:20463020" FT BINDING 106 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20463020, FT ECO:0007744|PDB:3KRK" FT BINDING 341 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20463020, FT ECO:0007744|PDB:3KRK" FT BINDING 374 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:0000269|PubMed:12925531, FT ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, FT ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, FT ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, FT ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, FT ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, FT ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, FT ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, FT ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, FT ECO:0007744|PDB:6COX" FT SITE 516 FT /note="Aspirin-acetylated serine" FT SITE 592 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:8349699" FT MOD_RES 526 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P35354" FT MOD_RES 565 FT /note="O-acetylserine; by SPHK1" FT /evidence="ECO:0000269|PubMed:29662056" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, FT ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, FT ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, FT ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, FT ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, FT ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, FT ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, FT ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, FT ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, FT ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, FT ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, FT ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, FT ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, FT ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, FT ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, FT ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, FT ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, FT ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, FT ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, FT ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, FT ECO:0007744|PDB:6COX" FT /id="CAR_000222" FT CARBOHYD 130 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, FT ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, FT ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, FT ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, FT ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, FT ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, FT ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, FT ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, FT ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, FT ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, FT ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, FT ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, FT ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, FT ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, FT ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, FT ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, FT ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, FT ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, FT ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, FT ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, FT ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, FT ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, FT ECO:0007744|PDB:6COX" FT /id="CAR_000223" FT CARBOHYD 396 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, FT ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, FT ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, FT ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, FT ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, FT ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, FT ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, FT ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, FT ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, FT ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, FT ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, FT ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, FT ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, FT ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, FT ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, FT ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, FT ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, FT ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, FT ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, FT ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, FT ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, FT ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX" FT /id="CAR_000224" FT CARBOHYD 580 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:8349699" FT /id="CAR_000225" FT DISULFID 21..32 FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, FT ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, FT ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, FT ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, FT ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, FT ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, FT ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, FT ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, FT ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, FT ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, FT ECO:0007744|PDB:3Q7D, ECO:0007744|PDB:3QH0, FT ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3RR3, FT ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, FT ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, FT ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, FT ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, FT ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, FT ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, FT ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, FT ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, FT ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, FT ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, FT ECO:0007744|PDB:5JW1, ECO:0007744|PDB:5W58, FT ECO:0007744|PDB:6COX" FT DISULFID 22..145 FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, FT ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, FT ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, FT ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, FT ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, FT ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, FT ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, FT ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, FT ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, FT ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, FT ECO:0007744|PDB:3Q7D, ECO:0007744|PDB:3QH0, FT ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3RR3, FT ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, FT ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, FT ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, FT ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, FT ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, FT ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, FT ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, FT ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, FT ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, FT ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, FT ECO:0007744|PDB:5JW1, ECO:0007744|PDB:5W58, FT ECO:0007744|PDB:6COX" FT DISULFID 26..42 FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, FT ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, FT ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, FT ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, FT ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, FT ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, FT ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, FT ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, FT ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, FT ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, FT ECO:0007744|PDB:3Q7D, ECO:0007744|PDB:3QH0, FT ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3RR3, FT ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, FT ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, FT ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, FT ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, FT ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, FT ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, FT ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, FT ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, FT ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, FT ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, FT ECO:0007744|PDB:5JW1, ECO:0007744|PDB:5W58, FT ECO:0007744|PDB:6COX" FT DISULFID 44..54 FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, FT ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, FT ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, FT ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, FT ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, FT ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, FT ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, FT ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, FT ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, FT ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, FT ECO:0007744|PDB:3Q7D, ECO:0007744|PDB:3QH0, FT ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3RR3, FT ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, FT ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, FT ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, FT ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, FT ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, FT ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, FT ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, FT ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, FT ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, FT ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, FT ECO:0007744|PDB:5JW1, ECO:0007744|PDB:5W58, FT ECO:0007744|PDB:6COX" FT DISULFID 555..561 FT /evidence="ECO:0000269|PubMed:10811226, FT ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, FT ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, FT ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, FT ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, FT ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, FT ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, FT ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, FT ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, FT ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, FT ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, FT ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, FT ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, FT ECO:0007744|PDB:3Q7D, ECO:0007744|PDB:3QH0, FT ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3RR3, FT ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, FT ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, FT ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, FT ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, FT ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, FT ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, FT ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, FT ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, FT ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, FT ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, FT ECO:0007744|PDB:5JW1, ECO:0007744|PDB:5W58, FT ECO:0007744|PDB:6COX" FT MUTAGEN 374 FT /note="H->Y: Impairs peroxidase and cyclooxygenase FT activities toward 2-arachidonoyl glycerol." FT /evidence="ECO:0000269|PubMed:22942274" FT MUTAGEN 517 FT /note="L->A,F,P,T: Slightly reduced activity." FT /evidence="ECO:0000269|PubMed:20463020" FT MUTAGEN 565 FT /note="S->A: Decreases acetylation by SPHK1." FT /evidence="ECO:0000269|PubMed:29662056" FT MUTAGEN 580 FT /note="N->A: Loss of glycosylation site." FT /evidence="ECO:0000269|PubMed:20463020" FT CONFLICT 98 FT /note="I -> T (in Ref. 1; AAA39924)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="A -> R (in Ref. 3; AAA39918)" FT /evidence="ECO:0000305" FT CONFLICT 301 FT /note="I -> L (in Ref. 7; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 585 FT /note="H -> R (in Ref. 3; AAA39918)" FT /evidence="ECO:0000305" FT TURN 20..23 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:6COX" FT STRAND 31..36 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:3NT1" FT TURN 51..54 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 59..67 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 71..78 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 82..89 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 92..107 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:5JW1" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:4RRX" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 125..129 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:1DDX" FT STRAND 135..138 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:1DDX" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 160..167 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 182..192 FT /evidence="ECO:0007829|PDB:3NT1" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:3NT1" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:4PH9" FT HELIX 217..220 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 224..230 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:6COX" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:3NT1" FT TURN 276..279 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 282..305 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 311..332 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 334..339 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 349..352 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 365..370 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 379..383 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 398..414 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 420..424 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 431..443 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 449..455 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 464..468 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 472..481 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 484..486 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 489..495 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 503..505 FT /evidence="ECO:0007829|PDB:4PH9" FT HELIX 506..521 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 524..526 FT /evidence="ECO:0007829|PDB:3NT1" FT TURN 528..530 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 533..536 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 539..546 FT /evidence="ECO:0007829|PDB:3NT1" FT HELIX 550..557 FT /evidence="ECO:0007829|PDB:3NT1" FT STRAND 558..560 FT /evidence="ECO:0007829|PDB:3Q7D" SQ SEQUENCE 604 AA; 69013 MW; DFE1658295C92064 CRC64; MLFRAVLLCA ALGLSQAANP CCSNPCQNRG ECMSTGFDQY KCDCTRTGFY GENCTTPEFL TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRSLIMK YVLTSRSYLI DSPPTYNVHY GYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGNKELPDS KEVLEKVLLR REFIPDPQGS NMMFAFFAQH FTHQFFKTDH KRGPGFTRGL GHGVDLNHIY GETLDRQHKL RLFKDGKLKY QVIGGEVYPP TVKDTQVEMI YPPHIPENLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD ILKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ NRIASEFNTL YHWHPLLPDT FNIEDQEYSF KQFLYNNSIL LEHGLTQFVE SFTRQIAGRV AGGRNVPIAV QAVAKASIDQ SREMKYQSLN EYRKRFSLKP YTSFEELTGE KEMAAELKAL YSDIDVMELY PALLVEKPRP DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV GFKIINTASI QSLICNNVKG CPFTSFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR STEL //