ID Q2TJZ7_PIG Unreviewed; 153 AA.
AC Q2TJZ7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Prostaglandin E synthase {ECO:0000256|ARBA:ARBA00039926};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE EC=5.3.99.3 {ECO:0000256|ARBA:ARBA00012203};
DE AltName: Full=Glutathione peroxidase PTGES {ECO:0000256|ARBA:ARBA00042173};
DE AltName: Full=Glutathione transferase PTGES {ECO:0000256|ARBA:ARBA00042011};
DE AltName: Full=Microsomal prostaglandin E synthase 1 {ECO:0000256|ARBA:ARBA00041613};
GN Name=PTGES {ECO:0000313|Ensembl:ENSSSCP00000006094.2,
GN ECO:0000313|VGNC:VGNC:91950};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAX52523.1};
RN [1] {ECO:0000313|EMBL:AAX52523.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Uterus {ECO:0000313|EMBL:AAX52523.1};
RX PubMed=16223862; DOI=10.1210/en.2005-0880;
RA Waclawik A., Rivero-Muller A., Blitek A., Kaczmarek M.M., Brokken L.J.,
RA Watanabe K., Rahman N.A., Ziecik A.J.;
RT "Molecular cloning and spatiotemporal expression of prostaglandin F
RT synthase and microsomal prostaglandin E synthase-1 in porcine
RT endometrium.";
RL Endocrinology 147:210-221(2006).
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000006094.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000006094.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000006094.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036848};
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:0000256|ARBA:ARBA00036805};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53325;
CC Evidence={ECO:0000256|ARBA:ARBA00036805};
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:0000256|ARBA:ARBA00036040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64365;
CC Evidence={ECO:0000256|ARBA:ARBA00036040};
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:0000256|ARBA:ARBA00023931};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC Evidence={ECO:0000256|ARBA:ARBA00023931};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000256|ARBA:ARBA00001955};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004702}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the MAPEG family.
CC {ECO:0000256|ARBA:ARBA00010459}.
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DR EMBL; AY857634; AAX52523.1; -; mRNA.
DR RefSeq; NP_001033720.1; NM_001038631.1.
DR STRING; 9823.ENSSSCP00000006094; -.
DR ChEMBL; CHEMBL5152; -.
DR PaxDb; 9823-ENSSSCP00000006094; -.
DR Ensembl; ENSSSCT00000006255.4; ENSSSCP00000006094.2; ENSSSCG00000005688.4.
DR GeneID; 654407; -.
DR KEGG; ssc:654407; -.
DR CTD; 9536; -.
DR VGNC; VGNC:91950; PTGES.
DR eggNOG; ENOG502RZBK; Eukaryota.
DR GeneTree; ENSGT00390000011980; -.
DR HOGENOM; CLU_105467_1_1_1; -.
DR OMA; TIAQIPC; -.
DR OrthoDB; 5347993at2759; -.
DR TreeFam; TF105327; -.
DR BRENDA; 5.3.99.3; 6170.
DR Reactome; R-SSC-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000005688; Expressed in ovary and 41 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IEA:Ensembl.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004667; F:prostaglandin-D synthase activity; IEA:Ensembl.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IBA:GO_Central.
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; IMP:AgBase.
DR GO; GO:0031620; P:regulation of fever generation; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR InterPro; IPR040162; MGST1-like.
DR PANTHER; PTHR10689; MICROSOMAL GLUTATHIONE S-TRANSFERASE 1; 1.
DR PANTHER; PTHR10689:SF9; PROSTAGLANDIN E SYNTHASE; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAX52523.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q2TJZ7};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 153 AA; 17339 MW; F4E33F8FE3E78619 CRC64;
MPPPSLEMVS GQVLPAFLLC STLLVIKMYV VAIITGQVRL RKKAFANPED AQRHGGLQYC
RSDPDVERCL RAHRNDMETI YPFLFLGLVY SFLGPDPFVA WMHFLIFFLG RMVHTIAYLG
KLRAPTRSLA YTLAQLPCAS MALQIVWEAA RHL
//
