PTGES_MACFA
ID PTGES_MACFA Reviewed; 152 AA.
AC Q6PWL6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 glutathione S-transferase 1-like 1;
DE Short=MGST1-L1;
DE AltName: Full=Microsomal prostaglandin E synthase 1;
DE Short=MPGES-1;
GN Name=PTGES; Synonyms=MGST1L1;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Parent J., Chapdelaine P., Fortier M.A.;
RT "Molecular cloning of microsomal prostaglandin E synthase-1 and cytosolic
RT prostaglandin E synthase in macaque and distribution in female reproductive
RT tissues.";
RL Submitted (MAR-2004) 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; AY573809; AAS89037.1; -; mRNA.
DR RefSeq; XP_015291833.1; XM_015436347.1.
DR AlphaFoldDB; Q6PWL6; -.
DR SMR; Q6PWL6; -.
DR STRING; 9541.XP_005580707.1; -.
DR ChEMBL; CHEMBL4295610; -.
DR GeneID; 102125534; -.
DR KEGG; mcf:102125534; -.
DR CTD; 9536; -.
DR VEuPathDB; HostDB:ENSMFAG00000038160; -.
DR eggNOG; ENOG502RZBK; Eukaryota.
DR OMA; TIAQIPC; -.
DR OrthoDB; 1591261at2759; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000233100; Chromosome 15.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
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:0050220; F:prostaglandin-E synthase activity; ISS:UniProtKB.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
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..152
FT /note="Prostaglandin E synthase"
FT /id="PRO_0000217746"
FT TOPO_DOM 1..12
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 13..41
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TOPO_DOM 42..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 61..90
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TOPO_DOM 91..95
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 96..119
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TOPO_DOM 120..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT TRANSMEM 124..152
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 73..77
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 113
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 117
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT BINDING 126..130
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT SITE 49
FT /note="Essential for protaglandin-E synthase activity"
FT /evidence="ECO:0000250|UniProtKB:O14684"
FT SITE 126
FT /note="Essential for protaglandin-E synthase activity"
FT /evidence="ECO:0000250|UniProtKB:O14684"
SQ SEQUENCE 152 AA; 17116 MW; 5D50D2CCB6CA89F7 CRC64;
MPAHSLAMSS PALPAFLLCS TLLVIKMYVV AIITGQVRLR KKAFANPEDA LRHGGPQYCR
SDPDVERCLR AHRNDMETIY PFLFLGFVYS FLGPNPFVAW MHFLVFLLGR VVHTVAYLGK
LRAPIRSVTY TLAQLPCASM ALQILWEAAR HL
