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PGH2_CAVPO
ID   PGH2_CAVPO              Reviewed;         604 AA.
AC   P70682;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Prostaglandin G/H synthase 2;
DE            EC=1.14.99.1;
DE   AltName: Full=Cyclooxygenase-2;
DE            Short=COX-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   Flags: Precursor;
GN   Name=PTGS2; Synonyms=COX2;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley; TISSUE=Uterus;
RX   PubMed=8977409; DOI=10.1210/endo.138.1.4889;
RA   Bracken K.E., Elger W., Jantke I., Nanninga A., Gellersen B.;
RT   "Cloning of guinea pig cyclooxygenase-2 and 15-hydroxyprostaglandin
RT   dehydrogenase complementary deoxyribonucleic acids: steroid-modulated gene
RT   expression correlates to prostaglandin F2 alpha secretion in cultured
RT   endometrial cells.";
RL   Endocrinology 138:237-247(1997).
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. The
CC       cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the
CC       hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase
CC       activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor
CC       of all 2-series prostaglandins and thromboxanes. This complex
CC       transformation is initiated by abstraction of hydrogen at carbon 13
CC       (with S-stereochemistry), followed by insertion of molecular O2 to form
CC       the endoperoxide bridge between carbon 9 and 11 that defines
CC       prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase
CC       activity) yields a hydroperoxy group in PGG2 that is then reduced to
CC       PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation
CC       and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and
CC       eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the
CC       precursors of 1- and 3-series prostaglandins. In an alternative pathway
CC       of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to
CC       prostanoid lysophopholipids, which are then hydrolyzed by intracellular
CC       phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl
CC       glycerol yielding the glyceryl ester of PGH2, a process that can
CC       contribute to pain response. Generates lipid mediators from n-3 and n-6
CC       polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism.
CC       Oxygenates PUFAs to hydroperoxy compounds and then reduces them to
CC       corresponding alcohols. Plays a role in the generation of resolution
CC       phase interaction products (resolvins) during both sterile and
CC       infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3))
CC       to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a
CC       component of the biosynthetic pathway of E-series resolvins (RvEs),
CC       converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that
CC       is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-
CC       RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA,
CC       C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs)
CC       shown to activate macrophage phagocytosis during bacterial infection.
CC       In activated leukocytes, contributes to oxygenation of
CC       hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-
CC       diHETE). {ECO:0000250|UniProtKB:P35354}.
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:0000250|UniProtKB:P35354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729;
CC         Evidence={ECO:0000250|UniProtKB:P35354};
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:0000250|UniProtKB:P35354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597;
CC         Evidence={ECO:0000250|UniProtKB:P35354};
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:0000250|UniProtKB:P35354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601;
CC         Evidence={ECO:0000250|UniProtKB:P35354};
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:0000250|UniProtKB:P35354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45289;
CC         Evidence={ECO:0000250|UniProtKB:P35354};
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:0000250|UniProtKB:P35354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45293;
CC         Evidence={ECO:0000250|UniProtKB:P35354};
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:0000250|UniProtKB:Q05769};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:Q05769};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000250|UniProtKB:P35354}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q05769}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane
CC       {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane
CC       {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of
CC       the endoplasmic reticulum and nuclear envelope.
CC       {ECO:0000250|UniProtKB:P35354}.
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   -!- 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; Y07896; CAA69204.1; -; mRNA.
DR   RefSeq; NP_001166478.1; NM_001173007.1.
DR   AlphaFoldDB; P70682; -.
DR   SMR; P70682; -.
DR   STRING; 10141.ENSCPOP00000001794; -.
DR   BindingDB; P70682; -.
DR   ChEMBL; CHEMBL4523261; -.
DR   PeroxiBase; 4137; CpoPGHS02.
DR   GeneID; 100135607; -.
DR   KEGG; cpoc:100135607; -.
DR   CTD; 5743; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   InParanoid; P70682; -.
DR   OrthoDB; 324380at2759; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR   GO; GO:0005640; C:nuclear outer membrane; ISS:UniProtKB.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; ISS:UniProtKB.
DR   GO; GO:0019371; P:cyclooxygenase pathway; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0150077; P:regulation of neuroinflammatory response; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Dioxygenase; Disulfide bond; Endoplasmic reticulum;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Glycoprotein; Heme; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; Microsome;
KW   Nucleus; Oxidoreductase; Peroxidase; Prostaglandin biosynthesis;
KW   Prostaglandin metabolism; Reference proteome; S-nitrosylation; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..604
FT                   /note="Prostaglandin G/H synthase 2"
FT                   /id="PRO_0000023873"
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   ACT_SITE        371
FT                   /note="For cyclooxygenase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
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:0000255|PROSITE-ProRule:PRU00298"
FT   SITE            516
FT                   /note="Aspirin-acetylated serine"
FT                   /evidence="ECO:0000250|UniProtKB:P35354"
FT   MOD_RES         526
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P35354"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        21..32
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
FT   DISULFID        22..145
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
FT   DISULFID        26..42
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
FT   DISULFID        44..54
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
FT   DISULFID        555..561
FT                   /evidence="ECO:0000250|UniProtKB:Q05769"
SQ   SEQUENCE   604 AA;  68883 MW;  DA22AED46ABBFBC5 CRC64;
     MLARALLLCA ALALGQAANP CCSNPCQNRG ECLSVGFDRY KCDCTRTGYY GENCTTPEFL
     TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRNAIMI YVLTSRSHLI DSPPTYNAHY
     GYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGKKELPDS NEVLEKVLLR RKFIPDPQGT
     NMMFAFFAQH FTHQFFKSDQ KRGPAFTTGL AHGVDLSHIY GETLDRQHKL RLFKDGKMKY
     QIIDGEMYPP TVKETQVEMM YPPYIPEHAR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
     VLKQEHPEWD DERLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ
     NRIASEFNTL YHWHPLLPDT FQIDDQVYNF QQFLYNNSIL VEHGLTQFVE SFTKQIAGRV
     AGGRNVPLAV QRVAKASIEH SRKMKYQSLN EYRKRFLMKP YTSFEELTGE KEMAAGLEAL
     YGDIDAMELY PALLVEKPRP DAIFGETMVE MGAPFSLKGL MGNPICSPHY WKPSTFGGEV
     GFQIVNTASI QSLICNNVKG CPVTAFNLPD PQLAKTVTIN ASASHSRLED LSPTVLLKGR
     STEL
 
 
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