PGH2_MOUSE
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 03-AUG-2022, entry version 216.
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; 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). 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:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020,
CC ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986,
CC ECO:0000269|PubMed:22942274, 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 (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + 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 -!- 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}.
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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 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 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 GlyGen; Q05769; 4 sites, 12 N-linked glycans (4 sites).
DR iPTMnet; Q05769; -.
DR PhosphoSitePlus; Q05769; -.
DR SwissPalm; Q05769; -.
DR PaxDb; Q05769; -.
DR PeptideAtlas; Q05769; -.
DR PRIDE; Q05769; -.
DR ProteomicsDB; 301805; -.
DR Antibodypedia; 776; 1028 antibodies from 49 providers.
DR DNASU; 19225; -.
DR Ensembl; ENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.
DR GeneID; 19225; -.
DR KEGG; mmu:19225; -.
DR UCSC; uc007cxv.1; mouse.
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; 324380at2759; -.
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 73 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 111 other tissues.
DR ExpressionAtlas; Q05769; baseline and differential.
DR Genevisible; Q05769; MM.
DR GO; GO:0005901; C:caveola; ISO:MGI.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0007568; P:aging; IEA:Ensembl.
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:0034644; P:cellular response to UV; IEA:Ensembl.
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:0006954; P:inflammatory response; ISO:MGI.
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:0030728; P:ovulation; 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:0010942; P:positive regulation of cell death; ISO:MGI.
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:0010226; P:response to lithium ion; IEA:Ensembl.
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 GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR029576; COX-2.
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:SF8; PTHR11903:SF8; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR Pfam; PF00008; EGF; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
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
