Ptgs2
entrez
19225
canonical
uniprot
Q05769
canonical
ensembl
ENSMUSG00000032487
resolver
ensp
ENSMUSP00000035065
resolver
enst
ENSMUST00000035065
resolver
genesymbol
Ptgs2
resolver
genesymbol_syn
Cox-2
resolver
genesymbol_syn
Cox2
resolver
genesymbol_syn
Pghs-b
resolver
genesymbol_syn
Tis10
resolver
uniprot
Q543K3
resolver
uniprot_entry
PGH2_MOUSE
resolver
uniprot_sec
Q543K3
resolver
activity_regulation
ACTIVITY 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}.
uniprot
proteins
amino_acid_sequence
MLFRAVLLCAALGLSQAANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLNHIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIAGRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFNVQDPQPTKTATINASASHSRLDDINPTVLIKRRSTEL
uniprot
proteins
ec_number
1.14.99.1
uniprot
proteins
function
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:12925531, PubMed:20463020, PubMed:20810665, PubMed:21489986, PubMed:22942274). 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 (PubMed:12925531, PubMed:20463020, PubMed:20810665, PubMed:21489986, PubMed:22942274). 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 (By similarity). In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophospholipids to prostanoid lysophospholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids (By similarity). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response (By similarity). 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 (By similarity). 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 (By similarity). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (By similarity). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (PubMed:29662056). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:P79208, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:22942274, ECO:0000269|PubMed:29662056}.
uniprot
proteins
mass_dalton
69013
uniprot
proteins
mutagenesis
MUTAGEN 374; /note="H->Y: Impairs peroxidase and cyclooxygenase activities toward 2-arachidonoyl glycerol."; /evidence="ECO:0000269|PubMed:22942274"; MUTAGEN 517; /note="L->A,F,P,T: Slightly reduced activity."; /evidence="ECO:0000269|PubMed:20463020"; MUTAGEN 565; /note="S->A: Decreases acetylation by SPHK1."; /evidence="ECO:0000269|PubMed:29662056"; MUTAGEN 580; /note="N->A: Loss of glycosylation site."; /evidence="ECO:0000269|PubMed:20463020
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986}.
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526. {ECO:0000250|UniProtKB:P35354}.; PTM: Acetylated at Ser-565 by SPHK1. During neuroinflammation, acetylation by SPHK1 promotes neuronal secretion of specialized preresolving mediators (SPMs), especially 15-R-lipoxin A4, which results in an increase of phagocytic microglia. {ECO:0000269|PubMed:29662056}.
uniprot
proteins
protein_family
Prostaglandin G/H synthase family
uniprot
proteins
pubmed
10811226
uniprot
proteins
pubmed
10966456
uniprot
proteins
pubmed
12244105
uniprot
proteins
pubmed
12925531
uniprot
proteins
pubmed
1339449
uniprot
proteins
pubmed
1419907
uniprot
proteins
pubmed
1594589
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1712772
uniprot
proteins
pubmed
1744122
uniprot
proteins
pubmed
20463020
uniprot
proteins
pubmed
20810665
uniprot
proteins
pubmed
21467029
uniprot
proteins
pubmed
21489986
uniprot
proteins
pubmed
22465430
uniprot
proteins
pubmed
22942274
uniprot
proteins
pubmed
24605250
uniprot
proteins
pubmed
29662056
uniprot
proteins
pubmed
8349699
uniprot
proteins
pubmed
8482922
uniprot
proteins
pubmed
8967954
uniprot
proteins
pubmed
9545330
uniprot
proteins
sequence_length
604
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Nucleus inner membrane {ECO:0000305|PubMed:9545330}; Peripheral membrane protein. Nucleus outer membrane {ECO:0000305|PubMed:9545330}; Peripheral membrane protein. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
uniprot
proteins