ID  P35355;
PN  Prostaglandin G/H synthase 2;
GN  Ptgs2;
OS  10116;
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:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: P35355;
DR  UNIPROT: Q64379;
DR  UNIPROT: Q925V4;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
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. 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. 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. 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. 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. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. 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. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). 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. 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. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE) (By similarity). 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:P35354, ECO:0000250|UniProtKB:Q05769}.
DE  Reference Proteome: Yes;
DE  Interaction: P49286; IntAct: EBI-11578730; Score: 0.00
GO  GO:0005737;
GO  GO:0005789;
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:0043066;
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:0010942;
GO  GO:0090050;
GO  GO:0008284;
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:0042127;
GO  GO:0150077;
GO  GO:1990776;
GO  GO:0034097;
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:0014070;
GO  GO:0010033;
GO  GO:0010243;
GO  GO:0006979;
GO  GO:0009314;
GO  GO:0034612;
GO  GO:0033280;
GO  GO:0009410;
GO  GO:0019233;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLFRAVLLCAALALSHAANPCCSNPCQNRGECMSIGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTH
SQ  FKGVWNIVNNIPFLRNSIMRYVLTSRSHLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDS
SQ  KEVLEKVLLRREFIPDPQGTNMMFAFFAQHFTHQFFKTDQKRGPGFTRGLGHGVDLNHVYGETLDRQHKLRLFQDGKLKY
SQ  QVIGGEVYPPTVKDTQVDMIYPPHVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWDDERLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFNIEDQEYTFKQFLYNNSIL
SQ  LEHGLAHFVESFTRQIAGRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEELTGEKEMAAELKAL
SQ  YHDIDAMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFGGEVGFRIINTASIQSLICNNVKG
SQ  CPFASFNVQDPQPTKTATINASASHSRLDDINPTVLIKRRSTEL
//