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Prostaglandin E synthase 2 (EC 5.3.99.3) (GATE-binding factor 1) (GBF-1) (Microsomal prostaglandin E synthase 2) (mPGES-2) [Cleaved into: Prostaglandin E synthase 2 truncated form]

 PGES2_MOUSE             Reviewed;         384 AA.
Q8BWM0; A2ASQ2; Q99J30;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
20-DEC-2017, entry version 128.
RecName: Full=Prostaglandin E synthase 2;
EC=5.3.99.3 {ECO:0000250|UniProtKB:Q9H7Z7};
AltName: Full=GATE-binding factor 1 {ECO:0000303|PubMed:12050152};
Short=GBF-1 {ECO:0000303|PubMed:12050152};
AltName: Full=Microsomal prostaglandin E synthase 2;
Short=mPGES-2;
Contains:
RecName: Full=Prostaglandin E synthase 2 truncated form;
Name=Ptges2; Synonyms=Gbf1, Pges2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, POSSIBLE SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=12050152; DOI=10.1074/jbc.M202679200;
Hu J., Meng Q., Roy S.K., Raha A., Hu J., Zhang J., Hashimoto K.,
Kalvakolanu D.V.;
"A novel transactivating factor that regulates interferon-gamma-
dependent gene expression.";
J. Biol. Chem. 277:30253-30263(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=12835322; DOI=10.1074/jbc.M305108200;
Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T.,
Ohmiya Y., Watanabe K., Kudo I.;
"Cellular prostaglandin E2 production by membrane-bound prostaglandin
E synthase-2 via both cyclooxygenases-1 and -2.";
J. Biol. Chem. 278:37937-37947(2003).
[7]
INDUCTION.
PubMed=15584915; DOI=10.1111/j.1471-4159.2004.02829.x;
Bosetti F., Langenbach R., Weerasinghe G.R.;
"Prostaglandin E2 and microsomal prostaglandin E synthase-2 expression
are decreased in the cyclooxygenase-2-deficient mouse brain despite
compensatory induction of cyclooxygenase-1 and Ca2+-dependent
phospholipase A2.";
J. Neurochem. 91:1389-1397(2004).
[8]
INTERACTION WITH CEBPB.
PubMed=15879117; DOI=10.4049/jimmunol.174.10.6203;
Meng Q., Raha A., Roy S., Hu J., Kalvakolanu D.V.;
"IFN-gamma-stimulated transcriptional activation by IFN-gamma-
activated transcriptional element-binding factor 1 occurs via an
inducible interaction with CAAAT/enhancer-binding protein-beta.";
J. Immunol. 174:6203-6211(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the
more stable prostaglandin E2 (PGE2) (By similarity). May also have
transactivation activity toward IFN-gamma (IFNG), possibly via an
interaction with CEBPB; however, the relevance of transcription
activation activity remains unclear.
{ECO:0000250|UniProtKB:Q9H7Z7, ECO:0000303|PubMed:12050152}.
-!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-
hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-
dihydroxy-9-oxoprosta-5,13-dienoate.
{ECO:0000250|UniProtKB:Q9H7Z7}.
-!- ENZYME REGULATION: Isomerase activity is increased by sulfhydril
compounds. Dithiothreitol (DTT) is most effective, followed by
glutathione (GSH) and 2-mercaptoethanol.
{ECO:0000250|UniProtKB:Q66LN0}.
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
-!- SUBUNIT: Homodimer. Interacts with EXOSC10 (By similarity). May
interact with CEBPB. {ECO:0000250|UniProtKB:Q66LN0,
ECO:0000250|UniProtKB:Q9H7Z7, ECO:0000269|PubMed:15879117}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:Q9H7Z7}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q9H7Z7}. Nucleus
{ECO:0000269|PubMed:12050152}. Note=According to PubMed:12050152,
some fraction may be nuclear. {ECO:0000269|PubMed:12050152}.
-!- SUBCELLULAR LOCATION: Prostaglandin E synthase 2 truncated form:
Cytoplasm {ECO:0000250|UniProtKB:Q9H7Z7}. Note=Synthesized as a
Golgi membrane-bound protein, which is further cleaved into the
predominant soluble truncated form.
{ECO:0000250|UniProtKB:Q9H7Z7}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
liver, colon and lung. {ECO:0000269|PubMed:12050152,
ECO:0000269|PubMed:12835322}.
-!- INDUCTION: Constitutively expressed. Not induced during tissue
inflammation. Down-regulated in the absence of Ptges.
{ECO:0000269|PubMed:12835322, ECO:0000269|PubMed:15584915}.
-!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AK050616; BAC34345.1; -; mRNA.
EMBL; AL928669; CAM22503.1; -; Genomic_DNA.
EMBL; CH466542; EDL08547.1; -; Genomic_DNA.
EMBL; BC004846; AAH04846.1; -; mRNA.
CCDS; CCDS15914.1; -.
RefSeq; NP_598544.2; NM_133783.2.
UniGene; Mm.28048; -.
ProteinModelPortal; Q8BWM0; -.
SMR; Q8BWM0; -.
BioGrid; 220557; 1.
IntAct; Q8BWM0; 1.
MINT; MINT-4113056; -.
STRING; 10090.ENSMUSP00000028162; -.
iPTMnet; Q8BWM0; -.
PhosphoSitePlus; Q8BWM0; -.
SwissPalm; Q8BWM0; -.
EPD; Q8BWM0; -.
MaxQB; Q8BWM0; -.
PaxDb; Q8BWM0; -.
PeptideAtlas; Q8BWM0; -.
PRIDE; Q8BWM0; -.
Ensembl; ENSMUST00000028162; ENSMUSP00000028162; ENSMUSG00000026820.
GeneID; 96979; -.
KEGG; mmu:96979; -.
UCSC; uc008jfm.2; mouse.
CTD; 80142; -.
MGI; MGI:1917592; Ptges2.
eggNOG; KOG3029; Eukaryota.
eggNOG; ENOG410XS2X; LUCA.
GeneTree; ENSGT00390000000224; -.
HOGENOM; HOG000231901; -.
HOVERGEN; HBG069136; -.
InParanoid; Q8BWM0; -.
KO; K05309; -.
OMA; WYLRVEK; -.
OrthoDB; EOG091G0AEH; -.
TreeFam; TF314304; -.
Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-MMU-6798695; Neutrophil degranulation.
UniPathway; UPA00662; -.
PRO; PR:Q8BWM0; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026820; -.
CleanEx; MM_PTGES2; -.
ExpressionAtlas; Q8BWM0; baseline and differential.
Genevisible; Q8BWM0; MM.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:UniProtKB-EC.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0046903; P:secretion; IDA:MGI.
CDD; cd03197; GST_C_mPGES2; 1.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR034334; PGES2.
InterPro; IPR034335; PGES2_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF13417; GST_N_3; 1.
SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00195; GLUTAREDOXIN_1; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Fatty acid biosynthesis;
Fatty acid metabolism; Golgi apparatus; Isomerase; Lipid biosynthesis;
Lipid metabolism; Membrane; Nucleus; Prostaglandin biosynthesis;
Prostaglandin metabolism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 384 Prostaglandin E synthase 2.
/FTId=PRO_0000013131.
CHAIN 87 384 Prostaglandin E synthase 2 truncated
form. {ECO:0000250}.
/FTId=PRO_0000013132.
TOPO_DOM 1 56 Lumenal. {ECO:0000255}.
TRANSMEM 57 73 Helical. {ECO:0000255}.
TOPO_DOM 74 384 Cytoplasmic. {ECO:0000255}.
DOMAIN 89 192 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
DOMAIN 262 376 GST C-terminal.
REGION 163 164 Glutathione binding. {ECO:0000250}.
BINDING 147 147 Glutathione; via amide nitrogen and
carbonyl oxygen. {ECO:0000250}.
SITE 86 87 Cleavage. {ECO:0000250}.
CONFLICT 210 210 L -> P (in Ref. 5; AAH04846).
{ECO:0000305}.
SEQUENCE 384 AA; 43324 MW; 5A737A01466582CA CRC64;
MAQAARLSWV LVSSRCALTE GLLTRPWQPL SAQSRAGFTR VAAGSRGAAV RKGSPRLLGA
AALALGGALG LYHTVRWHQR SQDLRAERSA AQLPLSNSLQ LTLYQYKTCP FCSKVRAFLD
FHSLPYQVVE VNPVRRTEIK FSSYRKVPIL VAQEGDSLQQ LNDSSVIISA LKTYLVSGQP
LEEVITYYPP MKAMNDQGKE VTEFCNKYWL MLDEKEAQQM YGGKEARTEE MKWRQWADDW
LVHLISPNVY RTPAEALASF DYIVREGKFG AVEAAMAKYV GAAAMYLISK RLKSRHHLQD
DVRVDLYEAA NKWVTAVGKD RPFMGGQKPN LADLAVYGVL RVMEGLEAFD DLMRHSHIQP
WYLRMERAIE EAPSVHHVNP SCKD


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