ID  P35354;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Nucleus inner membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Nucleus outer membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000269|PubMed:9545330}.
DR  UNIPROT: P35354;
DR  UNIPROT: A8K802;
DR  UNIPROT: Q16876;
DR  PDB: 5F19;
DR  PDB: 5F1A;
DR  PDB: 5IKQ;
DR  PDB: 5IKR;
DR  PDB: 5IKT;
DR  PDB: 5IKV;
DR  PDB: 5KIR;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DR  OMIM: 600262;
DR  DisGeNET: 5743;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response (PubMed:7947975, PubMed:7592599, PubMed:9261177, PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:11939906, PubMed:19540099). The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes (PubMed:7947975, PubMed:7592599, PubMed:9261177, PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593). This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (PubMed:7947975, PubMed:7592599, PubMed:9261177, PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593). Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3- series prostaglandins (PubMed:11939906, PubMed:19540099). In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids (PubMed:27642067). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response (PubMed:22942274). Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols (PubMed:11034610, PubMed:11192938, PubMed:9048568, PubMed:9261177). Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation (PubMed:12391014). Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D- series resolvins (RvDs) (PubMed:12391014). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2 (PubMed:21206090). In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13- series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection (PubMed:26236990). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (PubMed:22068350, PubMed:26282205). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:Q05769, ECO:0000269|PubMed:11034610, ECO:0000269|PubMed:11192938, ECO:0000269|PubMed:11939906, ECO:0000269|PubMed:12391014, ECO:0000269|PubMed:16373578, ECO:0000269|PubMed:21206090, ECO:0000269|PubMed:22068350, ECO:0000269|PubMed:22942274, ECO:0000269|PubMed:26236990, ECO:0000269|PubMed:26282205, ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27642067, ECO:0000269|PubMed:7592599, ECO:0000269|PubMed:7947975, ECO:0000269|PubMed:9048568, ECO:0000269|PubMed:9261177, ECO:0000303|PubMed:19540099}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9WMX2; IntAct: EBI-9083640; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.35
DE  Interaction: O14936; IntAct: EBI-21252062; Score: 0.37
DE  Interaction: Q9H0V9; IntAct: EBI-21845712; Score: 0.35
DE  Interaction: P35354; IntAct: EBI-15578876; Score: 0.40
DE  Interaction: P04439; IntAct: EBI-20910216; Score: 0.40
DE  Interaction: Q86V38; IntAct: EBI-25846357; Score: 0.56
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0043005;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0032991;
GO  GO:0019899;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0016702;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0042803;
GO  GO:0007568;
GO  GO:0001525;
GO  GO:0030282;
GO  GO:0050873;
GO  GO:0071318;
GO  GO:0071498;
GO  GO:0034605;
GO  GO:0071456;
GO  GO:0071284;
GO  GO:0071260;
GO  GO:0071471;
GO  GO:0034644;
GO  GO:0019371;
GO  GO:0046697;
GO  GO:0007566;
GO  GO:0042633;
GO  GO:0006954;
GO  GO:0007612;
GO  GO:0035633;
GO  GO:0007613;
GO  GO:0051926;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043154;
GO  GO:1902219;
GO  GO:0045986;
GO  GO:0032227;
GO  GO:0030728;
GO  GO:0043065;
GO  GO:0090336;
GO  GO:0090050;
GO  GO:0031622;
GO  GO:0090271;
GO  GO:0045429;
GO  GO:0033138;
GO  GO:0090362;
GO  GO:0031394;
GO  GO:0042307;
GO  GO:0048661;
GO  GO:0045987;
GO  GO:0031915;
GO  GO:0051968;
GO  GO:0071636;
GO  GO:0010575;
GO  GO:0045907;
GO  GO:0001516;
GO  GO:0032310;
GO  GO:0008217;
GO  GO:0050727;
GO  GO:0150077;
GO  GO:1990776;
GO  GO:0032355;
GO  GO:0070542;
GO  GO:0009750;
GO  GO:0051384;
GO  GO:0032496;
GO  GO:0010226;
GO  GO:0010042;
GO  GO:0009624;
GO  GO:0006979;
GO  GO:0034612;
GO  GO:0033280;
GO  GO:0009410;
GO  GO:0019233;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTH
SQ  FKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDS
SQ  NEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKY
SQ  QIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSIL
SQ  LEHGITQFVESFTRQIAGRVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEAL
SQ  YGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGFQIINTASIQSLICNNVKG
SQ  CPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKERSTEL
//