PTGES_CANLF
ID PTGES_CANLF Reviewed; 153 AA.
AC A0SYQ0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Prostaglandin E synthase;
DE EC=5.3.99.3 {ECO:0000250|UniProtKB:O14684};
DE AltName: Full=Glutathione peroxidase PTGES;
DE EC=1.11.1.- {ECO:0000250|UniProtKB:O14684};
DE AltName: Full=Glutathione transferase PTGES;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:O14684};
DE AltName: Full=Microsomal prostaglandin E synthase 1;
DE Short=MPGES-1;
GN Name=PTGES; Synonyms=PGES;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kowalewski M.P., Hoffmann B.;
RT "Molecular cloning and characterization of prostaglandin E synthase (PGES)
RT in canine corpus luteum.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated
CC prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the
CC glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2
CC (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli
CC (By similarity). Plays a key role in inflammation response, fever and
CC pain (By similarity). Catalyzes also the oxidoreduction of
CC endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-
CC hydroperoxy-PGE2. In addition, displays low glutathione transferase and
CC glutathione-dependent peroxidase activities, toward 1-chloro-2,4-
CC dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE),
CC respectively (By similarity). {ECO:0000250|UniProtKB:O14684,
CC ECO:0000250|UniProtKB:Q9JM51}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin E2;
CC Xref=Rhea:RHEA:53324, ChEBI:CHEBI:85166, ChEBI:CHEBI:137172;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53325;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin G2 = (15S)-15-hydroperoxy-prostaglandin E2;
CC Xref=Rhea:RHEA:64364, ChEBI:CHEBI:82629, ChEBI:CHEBI:152564;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64365;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2
CC glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:O14684};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000250|UniProtKB:O14684};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000250|UniProtKB:O14684}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:O14684}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O14684}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm,
CC perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes
CC with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment.
CC {ECO:0000250|UniProtKB:O14684}.
CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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DR EMBL; EF063141; ABK59963.1; -; mRNA.
DR RefSeq; NP_001116326.1; NM_001122854.1.
DR AlphaFoldDB; A0SYQ0; -.
DR SMR; A0SYQ0; -.
DR STRING; 9612.ENSCAFP00000040771; -.
DR BindingDB; A0SYQ0; -.
DR ChEMBL; CHEMBL3341581; -.
DR PaxDb; A0SYQ0; -.
DR PRIDE; A0SYQ0; -.
DR Ensembl; ENSCAFT00030013175; ENSCAFP00030011517; ENSCAFG00030007173.
DR Ensembl; ENSCAFT00040011106; ENSCAFP00040009614; ENSCAFG00040005943.
DR Ensembl; ENSCAFT00845041265; ENSCAFP00845032348; ENSCAFG00845023377.
DR GeneID; 480698; -.
DR KEGG; cfa:480698; -.
DR CTD; 9536; -.
DR VEuPathDB; HostDB:ENSCAFG00845023377; -.
DR eggNOG; ENOG502RZBK; Eukaryota.
DR GeneTree; ENSGT00390000011980; -.
DR HOGENOM; CLU_105467_1_1_1; -.
DR InParanoid; A0SYQ0; -.
DR OMA; TIAQIPC; -.
DR OrthoDB; 1591261at2759; -.
DR TreeFam; TF105327; -.
DR Reactome; R-CFA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR UniPathway; UPA00662; -.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000030838; Expressed in placenta and 49 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0004667; F:prostaglandin-D synthase activity; IEA:Ensembl.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0031620; P:regulation of fever generation; IEA:Ensembl.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR Gene3D; 1.20.120.550; -; 1.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR InterPro; IPR040162; MGST1-like.
DR PANTHER; PTHR10689; PTHR10689; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; SSF161084; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..153
FT /note="Prostaglandin E synthase"
FT /id="PRO_0000289555"
FT TOPO_DOM 1..13
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 14..42
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TOPO_DOM 43..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 62..91
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TOPO_DOM 92..96
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 97..120
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TOPO_DOM 121..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 125..153
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 74..78
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 114
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 118
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 127..131
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT SITE 50
FT /note="Essential for protaglandin-E synthase activity"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT SITE 127
FT /note="Essential for protaglandin-E synthase activity"
FT /evidence="ECO:0000250|UniProtKB:O14684"
SQ SEQUENCE 153 AA; 17129 MW; 5D6759341590F24E CRC64;
MPPPVLALVS GQALPAFLLC STLLVIKMYV VAVITGQVRL RKKAFANPED ALRHGGLQYC
RSDQDVDRCL RAHRNDMETI YPFLFLGFVY SFLGPDPFIA QMHFLVFFLG RMVHTVAYLG
KLRAPTRSLA YTVAQLPCAS MALQIVWEAA CHL
