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Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (Glucocorticoid-regulated inflammatory cyclooxygenase) (Gripghs) (Macrophage activation-associated marker protein P71/73) (PES-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2) (TIS10 protein)

 PGH2_MOUSE              Reviewed;         604 AA.
Q05769; Q543K3;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 188.
RecName: Full=Prostaglandin G/H synthase 2;
EC=1.14.99.1;
AltName: Full=Cyclooxygenase-2;
Short=COX-2;
AltName: Full=Glucocorticoid-regulated inflammatory cyclooxygenase;
AltName: Full=Gripghs;
AltName: Full=Macrophage activation-associated marker protein P71/73;
AltName: Full=PES-2;
AltName: Full=PHS II;
AltName: Full=Prostaglandin H2 synthase 2;
Short=PGH synthase 2;
Short=PGHS-2;
AltName: Full=Prostaglandin-endoperoxide synthase 2;
AltName: Full=TIS10 protein;
Flags: Precursor;
Name=Ptgs2; Synonyms=Cox-2, Cox2, Pghs-b, Tis10;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=SWR/J;
PubMed=1712772;
Kujubu D.A., Fletcher B.S., Varnum B.C., Lim R.W., Herschman H.R.;
"TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3
cells, encodes a novel prostaglandin synthase/cyclooxygenase
homologue.";
J. Biol. Chem. 266:12866-12872(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1339449;
Fletcher B.S., Kujubu D.A., Perrin D.M., Herschman H.R.;
"Structure of the mitogen-inducible TIS10 gene and demonstration that
the TIS10-encoded protein is a functional prostaglandin G/H
synthase.";
J. Biol. Chem. 267:4338-4344(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1419907;
Ryseck R.-P., Raynoschek C., Macdonald-Bravo H., Dorfman K.,
Mattei M.-G., Bravo R.;
"Identification of an immediate early gene, pghs-B, whose protein
product has prostaglandin synthase/cyclooxygenase activity.";
Cell Growth Differ. 3:443-450(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1594589; DOI=10.1073/pnas.89.11.4888;
O'Banion M.K., Winn V.D., Young D.A.;
"cDNA cloning and functional activity of a glucocorticoid-regulated
inflammatory cyclooxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 89:4888-4892(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Hippocampus, Mammary gland, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 281-360.
PubMed=1744122;
O'Banion M.K., Sadowski H.B., Winn V., Young D.A.;
"A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a
cyclooxygenase-related protein.";
J. Biol. Chem. 266:23261-23267(1991).
[8]
PARTIAL PROTEIN SEQUENCE.
PubMed=8482922;
Phillips T.A., Kujubu D.A., Mackay R.J., Herschman H.R., Russell S.W.,
Pace J.L.;
"The mouse macrophage activation-associated marker protein, p71/73, is
an inducible prostaglandin endoperoxide synthase (cyclooxygenase).";
J. Leukoc. Biol. 53:411-419(1993).
[9]
GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580, AND LACK OF
GLYCOSYLATION AT ASN-592.
PubMed=8349699;
Otto J.C., Dewitt D.L., Smith W.L.;
"N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and
their orientations in the endoplasmic reticulum.";
J. Biol. Chem. 268:18234-18242(1993).
[10]
FUNCTION IN INTESTINAL WOUND REPAIR, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=22465430; DOI=10.1053/j.gastro.2012.03.037;
Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.;
"Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic
mesenchymal stem cells in mice.";
Gastroenterology 143:110-121(2012).
[11]
REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
Smith W.L., DeWitt D.L., Garavito R.M.;
"Cyclooxygenases: structural, cellular, and molecular biology.";
Annu. Rev. Biochem. 69:145-182(2000).
[12]
REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
COLORECTAL CANCER.
PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
Sostres C., Gargallo C.J., Lanas A.;
"Aspirin, cyclooxygenase inhibition and colorectal cancer.";
World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH
(S)-FLURBIPROFEN; INDOMETHACIN; HEME AND
1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE,
COFACTOR, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
PubMed=8967954; DOI=10.1038/384644a0;
Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J.,
Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D.,
Seibert K., Isakson P.C., Stallings W.C.;
"Structural basis for selective inhibition of cyclooxygenase-2 by
anti-inflammatory agents.";
Nature 384:644-648(1996).
[14]
ERRATUM.
Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J.,
Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D.,
Seibert K., Isakson P.C., Stallings W.C.;
Nature 385:555-555(1997).
[15]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-569 IN COMPLEX WITH
ARACHIDONIC ACID, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
PubMed=10811226; DOI=10.1038/35011103;
Kiefer J.R., Pawlitz J.L., Moreland K.T., Stegeman R.A., Hood W.F.,
Gierse J.K., Stevens A.M., Goodwin D.C., Rowlinson S.W., Marnett L.J.,
Stallings W.C., Kurumbail R.G.;
"Structural insights into the stereochemistry of the cyclooxygenase
reaction.";
Nature 405:97-101(2000).
[16]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME AND
DICLOFENAC, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BONDS,
ENZYME REGULATION, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
PubMed=12925531; DOI=10.1074/jbc.M305481200;
Rowlinson S.W., Kiefer J.R., Prusakiewicz J.J., Pawlitz J.L.,
Kozak K.R., Kalgutkar A.S., Stallings W.C., Kurumbail R.G.,
Marnett L.J.;
"A novel mechanism of cyclooxygenase-2 inhibition involving
interactions with Ser-530 and Tyr-385.";
J. Biol. Chem. 278:45763-45769(2003).
[17]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-604 IN COMPLEX WITH HEME;
ACRYLIC ACID; ARACHIDONIC ACID AND DOCOSAHEXAENOIC ACID, CATALYTIC
ACTIVITY, ACTIVE SITE, SUBUNIT, COFACTOR, FUNCTION, DISULFIDE BONDS,
MUTAGENESIS OF LEU-517 AND ASN-580, AND GLYCOSYLATION AT ASN-53;
ASN-130; ASN-396 AND ASN-580.
PubMed=20463020; DOI=10.1074/jbc.M110.119867;
Vecchio A.J., Simmons D.M., Malkowski M.G.;
"Structural basis of fatty acid substrate binding to cyclooxygenase-
2.";
J. Biol. Chem. 285:22152-22163(2010).
[18]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 18-604 IN COMPLEXES WITH
HEME AND NAPROXEN ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-130 AND
ASN-396.
PubMed=20810665; DOI=10.1074/jbc.M110.162982;
Duggan K.C., Walters M.J., Musee J., Harp J.M., Kiefer J.R.,
Oates J.A., Marnett L.J.;
"Molecular basis for cyclooxygenase inhibition by the non-steroidal
anti-inflammatory drug naproxen.";
J. Biol. Chem. 285:34950-34959(2010).
[19]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-599 IN COMPLEX WITH HEME;
ACRYLIC ACID AND ARACHIDONIC ACID, FUNCTION, CATALYTIC ACTIVITY, AND
GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
PubMed=21489986; DOI=10.1074/jbc.M111.230367;
Vecchio A.J., Malkowski M.G.;
"The structural basis of endocannabinoid oxygenation by
cyclooxygenase-2.";
J. Biol. Chem. 286:20736-20745(2011).
-!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
committed step in prostanoid synthesis. Constitutively expressed
in some tissues in physiological conditions, such as the
endothelium, kidney and brain, and in pathological conditions,
such as in cancer. PTGS2 is responsible for production of
inflammatory prostaglandins. Up-regulation of PTGS2 is also
associated with increased cell adhesion, phenotypic changes,
resistance to apoptosis and tumor angiogenesis. In cancer cells,
PTGS2 is a key step in the production of prostaglandin E2 (PGE2),
which plays important roles in modulating motility, proliferation
and resistance to apoptosis. {ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665,
ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:22465430}.
-!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
H(2) + A + H(2)O. {ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665,
ECO:0000269|PubMed:21489986}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:8967954};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:8967954};
-!- ENZYME REGULATION: Inhibited by the nonsteroidal anti-inflammatory
drugs aspirin, naproxen, diclofenac, meclofenamic acid,
indomethacin and their analogs. {ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20810665}.
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10811226,
ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020,
ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954}.
-!- INTERACTION:
Q9Z0J4:Nos1; NbExp=4; IntAct=EBI-298933, EBI-397596;
-!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
protein. Endoplasmic reticulum membrane; Peripheral membrane
protein.
-!- TISSUE SPECIFICITY: Following colon injury, expressed in the wound
bed mesenchyme during the first phase of repair, probably by
colonic mesenchymal stem cells (at protein level).
{ECO:0000269|PubMed:22465430}.
-!- DEVELOPMENTAL STAGE: During colonic wound repair, highly up-
regulated (more than 1600-fold) in the mesenchyme of the wound bed
2 days after injury as compared to uninjured mucosa. Further
increase in expression is observed at day 4 following injury
(close to 2200-fold). Down-regulated at day 6 (only 93-fold
increase as compared to uninjured mucosa).
{ECO:0000269|PubMed:22465430}.
-!- INDUCTION: By cytokines and mitogens.
-!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-
nitrosylation may take place on different Cys residues in addition
to Cys-526 (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mutant mice exhibit defects in colonic
mucosal wound repair. {ECO:0000269|PubMed:22465430}.
-!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2
is a 2 step reaction: a cyclooxygenase (COX) reaction which
converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase
reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The
cyclooxygenase reaction occurs in a hydrophobic channel in the
core of the enzyme. The peroxidase reaction occurs at a heme-
containing active site located near the protein surface. The
nonsteroidal anti-inflammatory drugs (NSAIDs) binding site
corresponds to the cyclooxygenase active site.
-!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is
mediated by 2 different isozymes: the constitutive PTGS1 and the
inducible PTGS2. PGHS1 is expressed constitutively and generally
produces prostanoids acutely in response to hormonal stimuli to
fine-tune physiological processes requiring instantaneous,
continuous regulation (e.g. hemostasis). PGHS2 is inducible and
typically produces prostanoids that mediate responses to
physiological stresses such as infection and inflammation.
-!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen.
Aspirin is able to produce an irreversible inactivation of the
enzyme through a serine acetylation. Inhibition of the PGHSs with
NSAIDs acutely reduces inflammation, pain, and fever, and long-
term use of these drugs reduces fatal thrombotic events, as well
as the development of colon cancer and Alzheimer's disease. PTGS2
is the principal isozyme responsible for production of
inflammatory prostaglandins. New generation PTGSs inhibitors
strive to be selective for PTGS2, to avoid side effects such as
gastrointestinal complications and ulceration.
-!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
{ECO:0000305}.
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EMBL; M64291; AAA39924.1; -; mRNA.
EMBL; M94967; AAA39918.1; -; mRNA.
EMBL; M82866; AAA40448.1; -; Genomic_DNA.
EMBL; M82862; AAA40448.1; JOINED; Genomic_DNA.
EMBL; M82863; AAA40448.1; JOINED; Genomic_DNA.
EMBL; M82864; AAA40448.1; JOINED; Genomic_DNA.
EMBL; M82865; AAA40448.1; JOINED; Genomic_DNA.
EMBL; M88242; AAA37740.1; -; mRNA.
EMBL; AK049923; BAC33986.1; -; mRNA.
EMBL; AK144956; BAE26154.1; -; mRNA.
EMBL; AK166221; BAE38639.1; -; mRNA.
EMBL; AK172161; BAE42855.1; -; mRNA.
EMBL; CH466520; EDL39487.1; -; Genomic_DNA.
CCDS; CCDS15353.1; -.
PIR; A49010; A49010.
RefSeq; NP_035328.2; NM_011198.4.
UniGene; Mm.292547; -.
PDB; 1CVU; X-ray; 2.40 A; A/B=18-569.
PDB; 1CX2; X-ray; 3.00 A; A/B/C/D=18-604.
PDB; 1DCX; Model; -; A/B=18-569.
PDB; 1DD0; Model; -; A/B=18-569.
PDB; 1DDX; X-ray; 3.00 A; A/B/C/D=18-569.
PDB; 1PXX; X-ray; 2.90 A; A/B/C/D=1-604.
PDB; 3HS5; X-ray; 2.10 A; A/B=20-604.
PDB; 3HS6; X-ray; 2.40 A; A/B=20-604.
PDB; 3HS7; X-ray; 2.65 A; A/B=20-604.
PDB; 3KRK; X-ray; 2.40 A; A/B=20-604.
PDB; 3LN0; X-ray; 2.20 A; A/B/C/D=18-604.
PDB; 3LN1; X-ray; 2.40 A; A/B/C/D=18-604.
PDB; 3MDL; X-ray; 2.20 A; A/B=20-599.
PDB; 3MQE; X-ray; 2.80 A; A/B/C/D=18-604.
PDB; 3NT1; X-ray; 1.73 A; A/B=18-604.
PDB; 3NTB; X-ray; 2.27 A; A/B/C/D=18-604.
PDB; 3NTG; X-ray; 2.19 A; A/B/C/D=18-569.
PDB; 3OLT; X-ray; 2.45 A; A/B=20-604.
PDB; 3OLU; X-ray; 2.35 A; A/B=20-604.
PDB; 3PGH; X-ray; 2.50 A; A/B/C/D=18-604.
PDB; 3Q7D; X-ray; 2.40 A; A/B=18-604.
PDB; 3QH0; X-ray; 2.10 A; A/B=1-604.
PDB; 3QMO; X-ray; 3.00 A; A/B=1-604.
PDB; 3RR3; X-ray; 2.84 A; A/B/C/D=18-577.
PDB; 3TZI; X-ray; 2.15 A; A/B=20-604.
PDB; 4COX; X-ray; 2.90 A; A/B/C/D=18-604.
PDB; 4E1G; X-ray; 2.10 A; A/B=1-604.
PDB; 4FM5; X-ray; 2.81 A; A/B/C/D=1-604.
PDB; 4M10; X-ray; 2.01 A; A/B/C/D=18-604.
PDB; 4M11; X-ray; 2.45 A; A/B/C/D=18-569.
PDB; 4OTJ; X-ray; 2.11 A; A/B/C/D=18-604.
PDB; 4OTY; X-ray; 2.35 A; A/B=18-604.
PDB; 4PH9; X-ray; 1.81 A; A/B=20-568.
PDB; 4RRW; X-ray; 2.57 A; A/B/C/D=18-604.
PDB; 4RRX; X-ray; 2.78 A; A/B=18-604.
PDB; 4RRY; X-ray; 2.43 A; A/B/C/D=18-604.
PDB; 4RRZ; X-ray; 2.57 A; A/B/C/D=18-604.
PDB; 4RS0; X-ray; 2.81 A; A=18-604.
PDB; 4RUT; X-ray; 2.16 A; A/B/C/D=18-604.
PDB; 4Z0L; X-ray; 2.29 A; A/B/C/D=18-604.
PDB; 5COX; X-ray; 3.00 A; A/B/C/D=18-604.
PDB; 5FDQ; X-ray; 1.90 A; A/B=20-604.
PDB; 5JVY; X-ray; 2.36 A; A/B=20-568.
PDB; 5JVZ; X-ray; 2.62 A; A/B=20-569.
PDB; 5JW1; X-ray; 2.82 A; A/B=20-569.
PDB; 6COX; X-ray; 2.80 A; A/B=18-604.
PDBsum; 1CVU; -.
PDBsum; 1CX2; -.
PDBsum; 1DCX; -.
PDBsum; 1DD0; -.
PDBsum; 1DDX; -.
PDBsum; 1PXX; -.
PDBsum; 3HS5; -.
PDBsum; 3HS6; -.
PDBsum; 3HS7; -.
PDBsum; 3KRK; -.
PDBsum; 3LN0; -.
PDBsum; 3LN1; -.
PDBsum; 3MDL; -.
PDBsum; 3MQE; -.
PDBsum; 3NT1; -.
PDBsum; 3NTB; -.
PDBsum; 3NTG; -.
PDBsum; 3OLT; -.
PDBsum; 3OLU; -.
PDBsum; 3PGH; -.
PDBsum; 3Q7D; -.
PDBsum; 3QH0; -.
PDBsum; 3QMO; -.
PDBsum; 3RR3; -.
PDBsum; 3TZI; -.
PDBsum; 4COX; -.
PDBsum; 4E1G; -.
PDBsum; 4FM5; -.
PDBsum; 4M10; -.
PDBsum; 4M11; -.
PDBsum; 4OTJ; -.
PDBsum; 4OTY; -.
PDBsum; 4PH9; -.
PDBsum; 4RRW; -.
PDBsum; 4RRX; -.
PDBsum; 4RRY; -.
PDBsum; 4RRZ; -.
PDBsum; 4RS0; -.
PDBsum; 4RUT; -.
PDBsum; 4Z0L; -.
PDBsum; 5COX; -.
PDBsum; 5FDQ; -.
PDBsum; 5JVY; -.
PDBsum; 5JVZ; -.
PDBsum; 5JW1; -.
PDBsum; 6COX; -.
ProteinModelPortal; Q05769; -.
SMR; Q05769; -.
BioGrid; 202463; 6.
DIP; DIP-31082N; -.
IntAct; Q05769; 2.
STRING; 10090.ENSMUSP00000035065; -.
BindingDB; Q05769; -.
ChEMBL; CHEMBL4321; -.
SwissLipids; SLP:000001129; -.
PeroxiBase; 3360; MmPGHS02.
iPTMnet; Q05769; -.
PhosphoSitePlus; Q05769; -.
UniCarbKB; Q05769; -.
PaxDb; Q05769; -.
PeptideAtlas; Q05769; -.
PRIDE; Q05769; -.
Ensembl; ENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.
GeneID; 19225; -.
KEGG; mmu:19225; -.
UCSC; uc007cxv.1; mouse.
CTD; 5743; -.
MGI; MGI:97798; Ptgs2.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00390000010743; -.
HOGENOM; HOG000013149; -.
HOVERGEN; HBG000366; -.
InParanoid; Q05769; -.
KO; K11987; -.
OMA; CNNVKGC; -.
OrthoDB; EOG091G03CD; -.
PhylomeDB; Q05769; -.
TreeFam; TF329675; -.
BRENDA; 1.14.99.1; 3474.
Reactome; R-MMU-197264; Nicotinamide salvaging.
Reactome; R-MMU-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
UniPathway; UPA00662; -.
EvolutionaryTrace; Q05769; -.
PRO; PR:Q05769; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000032487; -.
CleanEx; MM_PTGS2; -.
ExpressionAtlas; Q05769; baseline and differential.
Genevisible; Q05769; MM.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:Ensembl.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0030282; P:bone mineralization; ISO:MGI.
GO; GO:0050873; P:brown fat cell differentiation; IMP:BHF-UCL.
GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; IDA:MGI.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IMP:CAFA.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0019371; P:cyclooxygenase pathway; IDA:UniProtKB.
GO; GO:0046697; P:decidualization; IMP:MGI.
GO; GO:0007566; P:embryo implantation; IMP:MGI.
GO; GO:0042633; P:hair cycle; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB.
GO; GO:0007612; P:learning; IEA:Ensembl.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CAFA.
GO; GO:0097756; P:negative regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:CAFA.
GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IMP:CAFA.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0030728; P:ovulation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:BHF-UCL.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
GO; GO:0031622; P:positive regulation of fever generation; IDA:BHF-UCL.
GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IEA:Ensembl.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:CAFA.
GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; IEA:Ensembl.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:CAFA.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IEA:Ensembl.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0009750; P:response to fructose; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR029576; COX-2.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR037120; Haem_peroxidase_sf.
PANTHER; PTHR11903:SF8; PTHR11903:SF8; 1.
Pfam; PF03098; An_peroxidase; 1.
Pfam; PF00008; EGF; 1.
PRINTS; PR00457; ANPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Dioxygenase;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Fatty acid biosynthesis; Fatty acid metabolism; Glycoprotein; Heme;
Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
Microsome; Oxidoreductase; Peroxidase; Prostaglandin biosynthesis;
Prostaglandin metabolism; Reference proteome; S-nitrosylation; Signal.
SIGNAL 1 17
CHAIN 18 604 Prostaglandin G/H synthase 2.
/FTId=PRO_0000023876.
DOMAIN 18 55 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298,
ECO:0000269|PubMed:20463020}.
ACT_SITE 371 371 For cyclooxygenase activity.
{ECO:0000269|PubMed:20463020}.
METAL 374 374 Iron (heme axial ligand).
BINDING 106 106 Substrate.
BINDING 341 341 Substrate.
BINDING 371 371 Substrate.
SITE 516 516 Aspirin-acetylated serine.
SITE 592 592 Not glycosylated.
{ECO:0000269|PubMed:8349699}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10811226,
ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20463020,
ECO:0000269|PubMed:20810665,
ECO:0000269|PubMed:21489986,
ECO:0000269|PubMed:8349699,
ECO:0000269|PubMed:8967954}.
/FTId=CAR_000222.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10811226,
ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20463020,
ECO:0000269|PubMed:20810665,
ECO:0000269|PubMed:21489986,
ECO:0000269|PubMed:8349699,
ECO:0000269|PubMed:8967954}.
/FTId=CAR_000223.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10811226,
ECO:0000269|PubMed:12925531,
ECO:0000269|PubMed:20463020,
ECO:0000269|PubMed:20810665,
ECO:0000269|PubMed:21489986,
ECO:0000269|PubMed:8349699,
ECO:0000269|PubMed:8967954}.
/FTId=CAR_000224.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20463020,
ECO:0000269|PubMed:8349699}.
/FTId=CAR_000225.
DISULFID 21 32
DISULFID 22 145
DISULFID 26 42
DISULFID 44 54
DISULFID 555 561
MUTAGEN 517 517 L->A,F,P,T: Slightly reduced activity.
{ECO:0000269|PubMed:20463020}.
MUTAGEN 580 580 N->A: Loss of glycosylation site.
{ECO:0000269|PubMed:20463020}.
CONFLICT 98 98 I -> T (in Ref. 1; AAA39924).
{ECO:0000305}.
CONFLICT 142 142 A -> R (in Ref. 3; AAA39918).
{ECO:0000305}.
CONFLICT 301 301 I -> L (in Ref. 7; no nucleotide entry).
{ECO:0000305}.
CONFLICT 585 585 H -> R (in Ref. 3; AAA39918).
{ECO:0000305}.
TURN 20 23 {ECO:0000244|PDB:3NT1}.
HELIX 27 29 {ECO:0000244|PDB:6COX}.
STRAND 31 36 {ECO:0000244|PDB:3NT1}.
STRAND 39 43 {ECO:0000244|PDB:3NT1}.
STRAND 47 50 {ECO:0000244|PDB:3NT1}.
TURN 51 54 {ECO:0000244|PDB:3NT1}.
HELIX 59 67 {ECO:0000244|PDB:3NT1}.
HELIX 71 78 {ECO:0000244|PDB:3NT1}.
HELIX 82 89 {ECO:0000244|PDB:3NT1}.
HELIX 92 107 {ECO:0000244|PDB:3NT1}.
STRAND 108 110 {ECO:0000244|PDB:5JW1}.
STRAND 116 119 {ECO:0000244|PDB:4RRX}.
STRAND 120 122 {ECO:0000244|PDB:3NT1}.
HELIX 125 129 {ECO:0000244|PDB:3NT1}.
STRAND 131 133 {ECO:0000244|PDB:1DDX}.
STRAND 135 138 {ECO:0000244|PDB:3NT1}.
STRAND 145 147 {ECO:0000244|PDB:1DDX}.
STRAND 150 153 {ECO:0000244|PDB:3NT1}.
HELIX 160 167 {ECO:0000244|PDB:3NT1}.
HELIX 182 192 {ECO:0000244|PDB:3NT1}.
TURN 193 195 {ECO:0000244|PDB:3NT1}.
TURN 200 202 {ECO:0000244|PDB:3NT1}.
STRAND 206 208 {ECO:0000244|PDB:3NT1}.
STRAND 213 215 {ECO:0000244|PDB:4PH9}.
HELIX 217 220 {ECO:0000244|PDB:3NT1}.
HELIX 224 230 {ECO:0000244|PDB:3NT1}.
STRAND 241 243 {ECO:0000244|PDB:3NT1}.
STRAND 246 248 {ECO:0000244|PDB:3NT1}.
HELIX 252 255 {ECO:0000244|PDB:3NT1}.
STRAND 263 265 {ECO:0000244|PDB:6COX}.
HELIX 267 269 {ECO:0000244|PDB:3NT1}.
TURN 276 279 {ECO:0000244|PDB:3NT1}.
HELIX 282 305 {ECO:0000244|PDB:3NT1}.
HELIX 311 332 {ECO:0000244|PDB:3NT1}.
HELIX 334 339 {ECO:0000244|PDB:3NT1}.
HELIX 349 352 {ECO:0000244|PDB:3NT1}.
HELIX 365 370 {ECO:0000244|PDB:3NT1}.
HELIX 374 376 {ECO:0000244|PDB:3NT1}.
STRAND 379 383 {ECO:0000244|PDB:3NT1}.
STRAND 386 388 {ECO:0000244|PDB:3NT1}.
HELIX 390 393 {ECO:0000244|PDB:3NT1}.
HELIX 398 414 {ECO:0000244|PDB:3NT1}.
STRAND 420 424 {ECO:0000244|PDB:3NT1}.
HELIX 428 430 {ECO:0000244|PDB:3NT1}.
HELIX 431 443 {ECO:0000244|PDB:3NT1}.
HELIX 449 455 {ECO:0000244|PDB:3NT1}.
HELIX 464 468 {ECO:0000244|PDB:3NT1}.
STRAND 469 471 {ECO:0000244|PDB:3NT1}.
HELIX 472 481 {ECO:0000244|PDB:3NT1}.
HELIX 484 486 {ECO:0000244|PDB:3NT1}.
HELIX 489 495 {ECO:0000244|PDB:3NT1}.
STRAND 503 505 {ECO:0000244|PDB:4PH9}.
HELIX 506 521 {ECO:0000244|PDB:3NT1}.
HELIX 524 526 {ECO:0000244|PDB:3NT1}.
TURN 528 530 {ECO:0000244|PDB:3NT1}.
HELIX 533 536 {ECO:0000244|PDB:3NT1}.
HELIX 539 546 {ECO:0000244|PDB:3NT1}.
HELIX 550 557 {ECO:0000244|PDB:3NT1}.
STRAND 558 560 {ECO:0000244|PDB:3Q7D}.
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


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