ID PGES2_DANRE Reviewed; 377 AA.
AC Q7ZUC7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Prostaglandin E synthase 2;
DE EC=5.3.99.3 {ECO:0000250|UniProtKB:Q66LN0};
DE AltName: Full=Microsomal prostaglandin E synthase 2;
DE Short=mPGES-2;
GN Name=ptges2; Synonyms=pges2, ptgesl;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more
CC stable prostaglandin E2 (PGE2) (in vitro). The biological function and
CC the GSH-dependent property of PTGES2 is still under debate (By
CC similarity). In vivo, PTGES2 could form a complex with GSH and heme and
CC would not participate in PGE2 synthesis but would catalyze the
CC degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-
CC 5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA)
CC (By similarity). {ECO:0000250|UniProtKB:Q9H7Z7,
CC ECO:0000250|UniProtKB:Q9N0A4}.
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:Q66LN0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC Evidence={ECO:0000250|UniProtKB:Q66LN0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-
CC heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274;
CC Evidence={ECO:0000250|UniProtKB:Q66LN0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48645;
CC Evidence={ECO:0000250|UniProtKB:Q66LN0};
CC -!- ACTIVITY REGULATION: Isomerase activity is increased by sulfhydril
CC compounds. Dithiothreitol (DTT) is most effective, followed by
CC glutathione (GSH) and 2-mercaptoethanol.
CC {ECO:0000250|UniProtKB:Q66LN0}.
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000250|UniProtKB:Q66LN0}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q66LN0}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9H7Z7}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9H7Z7}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; BC049325; AAH49325.1; -; mRNA.
DR RefSeq; NP_956574.1; NM_200280.1.
DR AlphaFoldDB; Q7ZUC7; -.
DR SMR; Q7ZUC7; -.
DR STRING; 7955.ENSDARP00000111602; -.
DR PaxDb; 7955-ENSDARP00000111602; -.
DR PeptideAtlas; Q7ZUC7; -.
DR GeneID; 799964; -.
DR KEGG; dre:799964; -.
DR AGR; ZFIN:ZDB-GENE-040426-1063; -.
DR CTD; 799964; -.
DR ZFIN; ZDB-GENE-040426-1063; ptgesl.
DR eggNOG; KOG3029; Eukaryota.
DR InParanoid; Q7ZUC7; -.
DR OrthoDB; 1226at2759; -.
DR Reactome; R-DRE-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR UniPathway; UPA00662; -.
DR PRO; PR:Q7ZUC7; -.
DR Proteomes; UP000000437; Alternate scaffold 8.
DR Proteomes; UP000000437; Chromosome 8.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0036134; F:12-hydroxyheptadecatrienoic acid synthase activity; IEA:RHEA.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IBA:GO_Central.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03197; GST_C_mPGES2; 1.
DR CDD; cd03040; GST_N_mPGES2; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 6.20.200.30; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR034334; PGES2.
DR InterPro; IPR034335; PGES2_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12782; MICROSOMAL PROSTAGLANDIN E SYNTHASE-2; 1.
DR PANTHER; PTHR12782:SF5; PROSTAGLANDIN E SYNTHASE 2; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDG01182; Prostaglandin_E_synthase_like; 1.
DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..377
FT /note="Prostaglandin E synthase 2"
FT /id="PRO_0000186045"
FT TOPO_DOM 1..65
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 105..182
FT /note="GST N-terminal"
FT DOMAIN 266..377
FT /note="GST C-terminal"
FT BINDING 153
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9N0A4"
FT BINDING 166..167
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9N0A4"
SQ SEQUENCE 377 AA; 42792 MW; 9152364D898BF74B CRC64;
MAAACTRTLG KVGRLVLDTP TCRFTNTAAF VPRTSMRCQG RAYGTGSSGF KSRLLLAAPV
RGSGRVLGCA FLLGGGFGLY QTIKLTLQHH LAEKESDASD LDTDLKLTLY QYKTCPFCSK
VRAFLDYHRL PYEIVEVNPV MRQEIKWSTY RKVPILMVNG TVQLNDSSVI ISALKTYISS
KDKKISEILA CYPEMKSKND RGKDVIEFGN KYWVMVHDAD ADQLYPGKDS RKEEIKWRTW
ADDWLVHLIS PNVYRTPTEA LASFDYIVRE GKFGSFEGFF AKYFGAAAMW IISKRLKYKH
NLQADVRQDL YKAVNDWVAA IGKNKQFMGG DEPNLADLAV FGVLRVMEGL QSFDDMMEHT
KVKKWYSRMQ KATQHVS
//
