PGES2_HUMAN
ID PGES2_HUMAN Reviewed; 377 AA.
AC Q9H7Z7; Q53EW9; Q5SYV6; Q96GI0; Q96GL2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Prostaglandin E synthase 2;
DE EC=5.3.99.3 {ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783, ECO:0000269|PubMed:18198127};
DE AltName: Full=Membrane-associated prostaglandin E synthase-2 {ECO:0000303|PubMed:12804604};
DE Short=mPGE synthase-2 {ECO:0000303|PubMed:12804604};
DE AltName: Full=Microsomal prostaglandin E synthase 2;
DE Short=mPGES-2;
DE AltName: Full=Prostaglandin-H(2) E-isomerase;
DE Contains:
DE RecName: Full=Prostaglandin E synthase 2 truncated form;
GN Name=PTGES2; Synonyms=C9orf15, PGES2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11866447; DOI=10.1006/bbrc.2002.6531;
RA Tanikawa N., Ohmiya Y., Ohkubo H., Hashimoto K., Kangawa K., Kojima M.,
RA Ito S., Watanabe K.;
RT "Identification and characterization of a novel type of membrane-associated
RT prostaglandin E synthase.";
RL Biochem. Biophys. Res. Commun. 291:884-889(2002).
RN [6]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-110 AND CYS-113, ACTIVITY
RP REGULATION, AND FUNCTION.
RX PubMed=12804604; DOI=10.1016/s0006-291x(03)01025-8;
RA Watanabe K., Ohkubo H., Niwa H., Tanikawa N., Koda N., Ito S., Ohmiya Y.;
RT "Essential 110Cys in active site of membrane-associated prostaglandin E
RT synthase-2.";
RL Biochem. Biophys. Res. Commun. 306:577-581(2003).
RN [7]
RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=12835322; DOI=10.1074/jbc.m305108200;
RA Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T.,
RA Ohmiya Y., Watanabe K., Kudo I.;
RT "Cellular prostaglandin E2 production by membrane-bound prostaglandin E
RT synthase-2 via both cyclooxygenases-1 and -2.";
RL J. Biol. Chem. 278:37937-37947(2003).
RN [8]
RP INTERACTION WITH EXOSC10.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [9]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-110.
RX PubMed=17585783; DOI=10.1021/bi700605m;
RA Yamada T., Takusagawa F.;
RT "PGH2 degradation pathway catalyzed by GSH-heme complex bound microsomal
RT prostaglandin E2 synthase type 2: the first example of a dual-function
RT enzyme.";
RL Biochemistry 46:8414-8424(2007).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND CAUTION.
RX PubMed=18198127; DOI=10.1016/j.bbrc.2008.01.029;
RA Watanabe K., Ito S., Yamamoto S.;
RT "Studies on membrane-associated prostaglandin E synthase-2 with reference
RT to production of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT).";
RL Biochem. Biophys. Res. Commun. 367:782-786(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more
CC stable prostaglandin E2 (PGE2) (in vitro) (PubMed:12804604,
CC PubMed:18198127, PubMed:17585783). The biological function and the GSH-
CC dependent property of PTGES2 is still under debate (PubMed:18198127,
CC PubMed:17585783). In vivo, PTGES2 could form a complex with GSH and
CC heme and 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 (PubMed:17585783) (By similarity). {ECO:0000250|UniProtKB:Q9N0A4,
CC ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783,
CC ECO:0000269|PubMed:18198127}.
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:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783,
CC ECO:0000269|PubMed:18198127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC Evidence={ECO:0000305|PubMed:12804604};
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:0000269|PubMed:17585783};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48645;
CC Evidence={ECO:0000305|PubMed:17585783};
CC -!- ACTIVITY REGULATION: Isomerase activity is increased by sulfhydril
CC compounds. Dithiothreitol (DTT) is most effective, followed by
CC dihydrolipoic acid, glutathione (GSH) and 2-mercaptoethanol.
CC {ECO:0000269|PubMed:12804604}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 uM for PGH2 (for the GSH-heme complex-bound enzyme)
CC {ECO:0000269|PubMed:17585783};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC -!- SUBUNIT: Homodimer. May interact with CEBPB (By similarity). Interacts
CC with EXOSC10. {ECO:0000250|UniProtKB:Q66LN0,
CC ECO:0000250|UniProtKB:Q8BWM0, ECO:0000269|PubMed:15231747}.
CC -!- INTERACTION:
CC Q9H7Z7; Q5VU69: C1orf189; NbExp=3; IntAct=EBI-681645, EBI-10247920;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12835322}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Prostaglandin E synthase 2 truncated form]:
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:12835322}.
CC Note=Synthesized as a Golgi membrane-bound protein, which is further
CC cleaved into the predominant soluble truncated form. The truncated form
CC is cytoplasmic and is enriched in the perinuclear region.
CC {ECO:0000269|PubMed:12835322}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the heart, including
CC apex, inter-ventricular septum, both atria and ventricles, but not in
CC the aorta. Also expressed in fetal heart. Detected in various regions
CC of the brain: cerebellum; occipital, frontal and parietal lobes. Also
CC expressed in the lymph nodes, skeletal muscle, kidney and trachea, but
CC not in the thymus or lung. Overexpressed in colorectal cancer.
CC {ECO:0000269|PubMed:11866447}.
CC -!- PTM: Synthesized as a Golgi membrane-associated protein, and the
CC proteolytic removal of the N-terminal hydrophobic domain leads to the
CC formation of a mature cytosolic enzyme. {ECO:0000269|PubMed:12835322}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC -!- CAUTION: It is not known if heme and GST are required for prostaglandin
CC synthase activity. The protein copurifies with heme and GST when DTT is
CC omitted during the purification procedure. The GSH-heme complex-bound
CC enzyme has been proposed to act as a lyase and catalyze the degradation
CC of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-
CC heptadecatrienoic acid (HHT) and malondialdehyde (MDA). According to
CC PubMed:18198127, boiling the enzyme leads to loss of prostaglandin
CC synthase activity, but does not eliminate the lyase activity. Besides,
CC free heme can catalyze the formation of 12L-hydroxy-5,8,10-
CC heptadecatrienoic acid (HHT) (PubMed:18198127). A more recent study
CC demonstrates the GSH-dependent property of PTGES2, DTT dissociates the
CC bound heme to produce active PGE2 synthase in vitro (By similarity).
CC PTGES2 can only catalyzes PGE2 synthesis in the free state as an
CC enzyme, while in vivo it forms a complex with heme and does not
CC participate in PGE2 synthesis (By similarity). In agreement with this
CC study, the in vivo evidence from PTGES2 deficient mice do not show that
CC this protein is responsible for the PGE2 production under basal or
CC pathophysiological conditions (By similarity).
CC {ECO:0000250|UniProtKB:Q8BWM0, ECO:0000250|UniProtKB:Q9N0A4,
CC ECO:0000269|PubMed:18198127, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK024100; BAB14826.1; -; mRNA.
DR EMBL; AK223520; BAD97240.1; -; mRNA.
DR EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009397; AAH09397.2; -; mRNA.
DR EMBL; BC009456; AAH09456.1; -; mRNA.
DR EMBL; BC011613; AAH11613.1; -; mRNA.
DR CCDS; CCDS6891.1; -.
DR RefSeq; NP_001243264.1; NM_001256335.1.
DR RefSeq; NP_079348.1; NM_025072.6.
DR RefSeq; NP_945176.1; NM_198938.2.
DR AlphaFoldDB; Q9H7Z7; -.
DR SMR; Q9H7Z7; -.
DR BioGRID; 123135; 89.
DR IntAct; Q9H7Z7; 28.
DR MINT; Q9H7Z7; -.
DR STRING; 9606.ENSP00000345341; -.
DR BindingDB; Q9H7Z7; -.
DR ChEMBL; CHEMBL4411; -.
DR GuidetoPHARMACOLOGY; 1378; -.
DR SwissLipids; SLP:000001095; -.
DR GlyGen; Q9H7Z7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H7Z7; -.
DR PhosphoSitePlus; Q9H7Z7; -.
DR SwissPalm; Q9H7Z7; -.
DR BioMuta; PTGES2; -.
DR DMDM; 73921741; -.
DR EPD; Q9H7Z7; -.
DR jPOST; Q9H7Z7; -.
DR MassIVE; Q9H7Z7; -.
DR MaxQB; Q9H7Z7; -.
DR PaxDb; Q9H7Z7; -.
DR PeptideAtlas; Q9H7Z7; -.
DR PRIDE; Q9H7Z7; -.
DR ProteomicsDB; 81164; -.
DR TopDownProteomics; Q9H7Z7; -.
DR Antibodypedia; 17330; 328 antibodies from 34 providers.
DR DNASU; 80142; -.
DR Ensembl; ENST00000338961.11; ENSP00000345341.6; ENSG00000148334.16.
DR GeneID; 80142; -.
DR KEGG; hsa:80142; -.
DR MANE-Select; ENST00000338961.11; ENSP00000345341.6; NM_025072.7; NP_079348.1.
DR UCSC; uc004bti.4; human.
DR CTD; 80142; -.
DR DisGeNET; 80142; -.
DR GeneCards; PTGES2; -.
DR HGNC; HGNC:17822; PTGES2.
DR HPA; ENSG00000148334; Tissue enhanced (skeletal).
DR MIM; 608152; gene.
DR neXtProt; NX_Q9H7Z7; -.
DR OpenTargets; ENSG00000148334; -.
DR PharmGKB; PA33949; -.
DR VEuPathDB; HostDB:ENSG00000148334; -.
DR eggNOG; KOG3029; Eukaryota.
DR GeneTree; ENSGT00390000000224; -.
DR HOGENOM; CLU_011226_0_0_1; -.
DR InParanoid; Q9H7Z7; -.
DR OMA; LWTGGCA; -.
DR OrthoDB; 1042777at2759; -.
DR PhylomeDB; Q9H7Z7; -.
DR TreeFam; TF314304; -.
DR BioCyc; MetaCyc:HS07514-MON; -.
DR BRENDA; 5.3.99.3; 2681.
DR PathwayCommons; Q9H7Z7; -.
DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9H7Z7; -.
DR UniPathway; UPA00662; -.
DR BioGRID-ORCS; 80142; 18 hits in 1088 CRISPR screens.
DR ChiTaRS; PTGES2; human.
DR GeneWiki; PTGES2; -.
DR GenomeRNAi; 80142; -.
DR Pharos; Q9H7Z7; Tchem.
DR PRO; PR:Q9H7Z7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H7Z7; protein.
DR Bgee; ENSG00000148334; Expressed in apex of heart and 186 other tissues.
DR ExpressionAtlas; Q9H7Z7; baseline and differential.
DR Genevisible; Q9H7Z7; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036134; F:12-hydroxyheptadecatrienoic acid synthase activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IDA:FlyBase.
DR GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0046903; P:secretion; IEA:Ensembl.
DR CDD; cd03197; GST_C_mPGES2; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR034334; PGES2.
DR InterPro; IPR034335; PGES2_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus;
KW Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Phosphoprotein;
KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..377
FT /note="Prostaglandin E synthase 2"
FT /id="PRO_0000013127"
FT CHAIN 88..377
FT /note="Prostaglandin E synthase 2 truncated form"
FT /evidence="ECO:0000250|UniProtKB:Q66LN0"
FT /id="PRO_0000013128"
FT TOPO_DOM 1..57
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 90..193
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DOMAIN 263..377
FT /note="GST C-terminal"
FT BINDING 148
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9N0A4"
FT BINDING 164..165
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9N0A4"
FT SITE 87..88
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q66LN0"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 298
FT /note="R -> H (in dbSNP:rs13283456)"
FT /id="VAR_049494"
FT MUTAGEN 110
FT /note="C->S: Loss of prostaglandin-E synthase activity. Can
FT bind glutathione-heme and exhibits PGH2 degradation
FT activity."
FT /evidence="ECO:0000269|PubMed:12804604,
FT ECO:0000269|PubMed:17585783"
FT MUTAGEN 113
FT /note="C->S: Slightly decreased prostaglandin-E synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:12804604"
FT CONFLICT 319
FT /note="G -> S (in Ref. 2; BAD97240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 41943 MW; 82F2DF867BB8337C CRC64;
MDPAARVVRA LWPGGCALAW RLGGRPQPLL PTQSRAGFAG AAGGPSPVAA ARKGSPRLLG
AAALALGGAL GLYHTARWHL RAQDLHAERS AAQLSLSSRL QLTLYQYKTC PFCSKVRAFL
DFHALPYQVV EVNPVRRAEI KFSSYRKVPI LVAQEGESSQ QLNDSSVIIS ALKTYLVSGQ
PLEEIITYYP AMKAVNEQGK EVTEFGNKYW LMLNEKEAQQ VYGGKEARTE EMKWRQWADD
WLVHLISPNV YRTPTEALAS FDYIVREGKF GAVEGAVAKY MGAAAMYLIS KRLKSRHRLQ
DNVREDLYEA ADKWVAAVGK DRPFMGGQKP NLADLAVYGV LRVMEGLDAF DDLMQHTHIQ
PWYLRVERAI TEASPAH
