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Prostaglandin E synthase 2 (EC 5.3.99.3) (Membrane-associated prostaglandin E synthase-2) (mPGE synthase-2) (Microsomal prostaglandin E synthase 2) (mPGES-2) [Cleaved into: Prostaglandin E synthase 2 truncated form]

 PGES2_BOVIN             Reviewed;         372 AA.
Q66LN0; F1N1J6;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
20-JAN-2016, sequence version 3.
22-NOV-2017, entry version 86.
RecName: Full=Prostaglandin E synthase 2;
EC=5.3.99.3 {ECO:0000269|PubMed:10446427};
AltName: Full=Membrane-associated prostaglandin E synthase-2 {ECO:0000303|PubMed:10446427};
Short=mPGE synthase-2 {ECO:0000303|PubMed:10446427};
AltName: Full=Microsomal prostaglandin E synthase 2;
Short=mPGES-2;
Contains:
RecName: Full=Prostaglandin E synthase 2 truncated form;
Name=PTGES2; Synonyms=PGES2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hereford;
PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
"A whole-genome assembly of the domestic cow, Bos taurus.";
Genome Biol. 10:R42.01-R42.10(2009).
[2]
PROTEIN SEQUENCE OF 85-106.
PubMed=11866447; DOI=10.1006/bbrc.2002.6531;
Tanikawa N., Ohmiya Y., Ohkubo H., Hashimoto K., Kangawa K.,
Kojima M., Ito S., Watanabe K.;
"Identification and characterization of a novel type of membrane-
associated prostaglandin E synthase.";
Biochem. Biophys. Res. Commun. 291:884-889(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 135-191, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=15744024; DOI=10.1095/biolreprod.104.037036;
Parent J., Fortier M.A.;
"Expression and contribution of three different isoforms of
prostaglandin E synthase in the bovine endometrium.";
Biol. Reprod. 73:36-44(2005).
[4]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10446427; DOI=10.1016/S1388-1981(99)00084-0;
Watanabe K., Kurihara K., Suzuki T.;
"Purification and characterization of membrane-bound prostaglandin E
synthase from bovine heart.";
Biochim. Biophys. Acta 1439:406-414(1999).
-!- FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the
more stable prostaglandin E2 (PGE2).
{ECO:0000269|PubMed:10446427}.
-!- 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:0000269|PubMed:10446427}.
-!- ENZYME REGULATION: Isomerase activity is increased by sulfhydril
compounds. Dithiothreitol (DTT) is most effective, followed by
glutathione (GSH) and 2-mercaptoethanol.
{ECO:0000269|PubMed:10446427}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=24 uM for PGH2 {ECO:0000269|PubMed:10446427};
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
{ECO:0000269|PubMed:10446427}.
-!- SUBUNIT: May interact with CEBPB. Interacts with EXOSC10 (By
similarity). Homodimer. {ECO:0000250|UniProtKB:Q8BWM0,
ECO:0000250|UniProtKB:Q9H7Z7, ECO:0000269|PubMed:10446427}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000305|PubMed:10446427}; Single-pass membrane protein
{ECO:0000255}.
-!- 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: Detected in heart (at protein level)
(PubMed:10446427). Widely expressed. Expressed in heart > kidney >
muscle > testis > endometrium = ovary > myometrium = spleen =
lung. In endometrium, it is mainly expressed in luminal epithelial
cells followed by glandular epithelial cells, but expression is
also present in stromal cells at a lower level.
{ECO:0000269|PubMed:10446427, ECO:0000269|PubMed:15744024}.
-!- DEVELOPMENTAL STAGE: During the estrus cycle, it decreases from
the beginning of the cycle until days 13-15 and then increase
until ovulation (at protein level). {ECO:0000269|PubMed:15744024}.
-!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DAAA02032171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY692441; AAU04848.1; -; mRNA.
RefSeq; NP_001160026.1; NM_001166554.1.
UniGene; Bt.34207; -.
ProteinModelPortal; Q66LN0; -.
SMR; Q66LN0; -.
STRING; 9913.ENSBTAP00000021584; -.
PRIDE; Q66LN0; -.
Ensembl; ENSBTAT00000021584; ENSBTAP00000021584; ENSBTAG00000016218.
GeneID; 493639; -.
KEGG; bta:493639; -.
CTD; 80142; -.
GeneTree; ENSGT00390000000224; -.
InParanoid; Q66LN0; -.
KO; K05309; -.
OMA; WYLRVEK; -.
OrthoDB; EOG091G0AEH; -.
TreeFam; TF314304; -.
BRENDA; 5.3.99.3; 908.
Reactome; R-BTA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-BTA-6798695; Neutrophil degranulation.
UniPathway; UPA00662; -.
Proteomes; UP000009136; Chromosome 11.
Bgee; ENSBTAG00000016218; -.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IEA:Ensembl.
GO; GO:0009055; F:electron carrier 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; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0046903; P:secretion; IEA:Ensembl.
CDD; cd03197; GST_C_mPGES2; 1.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
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.
PROSITE; PS50405; GST_CTER; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus;
Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane;
Phosphoprotein; Prostaglandin biosynthesis; Prostaglandin metabolism;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 372 Prostaglandin E synthase 2.
/FTId=PRO_0000013125.
CHAIN 86 372 Prostaglandin E synthase 2 truncated
form.
/FTId=PRO_0000013126.
TOPO_DOM 1 54 Lumenal. {ECO:0000305}.
TRANSMEM 55 71 Helical. {ECO:0000255}.
TOPO_DOM 72 372 Cytoplasmic. {ECO:0000305}.
DOMAIN 87 190 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
DOMAIN 259 372 GST C-terminal.
REGION 161 162 Glutathione binding. {ECO:0000250}.
BINDING 145 145 Glutathione; via amide nitrogen and
carbonyl oxygen. {ECO:0000250}.
SITE 84 85 Cleavage. {ECO:0000250}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H7Z7}.
SEQUENCE 372 AA; 41738 MW; A87152D6CA33CD22 CRC64;
MAHAVRALWP HGRALAWRLG DRPALGLHAQ SRAGFTGAAG GSGPAATARK GGPRLLGAAA
LALGGALGLY HTARWHLRAQ DLRAERSATQ LSLSSRLQLT LYQYKTCPFC SKVRAFLDFH
ALPYQVVEVN PVRRAEIKFS SYRKVPIVMA QEGESLQQLN DSSVIISALK TYLVSGQPLA
DIITYYPPMK AVNDQGKEVT EFCNKYWLML DEKEAQRMYG GKEARTEEMK WRQWADDWLV
HLISPNVYRT PAEALASFDY IVKEGNFGTV EGAMAKYMGA AAMYFISKRL KRRHHLRDDV
REDLYEAANK WVAAVGKDRP FMGGQKPNLA DLAVYGVLRV MEGLEAFDDL MRHTHIQPWY
LRVEKAIAEA PQ


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