LOCUS       NP_001124461             160 aa            linear   ROD 03-APR-2024
DEFINITION  prostaglandin E synthase 3 [Rattus norvegicus].
ACCESSION   NP_001124461
VERSION     NP_001124461.1
DBSOURCE    REFSEQ: accession NM_001130989.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Woodford,M.R., Sager,R.A., Marris,E., Dunn,D.M., Blanden,A.R.,
            Murphy,R.L., Rensing,N., Shapiro,O., Panaretou,B., Prodromou,C.,
            Loh,S.N., Gutmann,D.H., Bourboulia,D., Bratslavsky,G., Wong,M. and
            Mollapour,M.
  TITLE     Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates
            folding of kinase and non-kinase clients
  JOURNAL   EMBO J 36 (24), 3650-3665 (2017)
   PUBMED   29127155
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Nakatani,Y., Miyazaki,Y. and Hara,S.
  TITLE     Cytosolic Prostaglandin E Synthase Is Involved in c-Fos Expression
            in Rat Fibroblastic 3Y1 Cells
  JOURNAL   Biol Pharm Bull 40 (11), 1963-1967 (2017)
   PUBMED   29093345
  REMARK    GeneRIF: Study in cultured rat fibroblasts suggests that cPGES/p23
            is involved in the activation of ERK to promote c-Fos expression.
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Majed,B.H. and Khalil,R.A.
  TITLE     Molecular mechanisms regulating the vascular prostacyclin pathways
            and their adaptation during pregnancy and in the newborn
  JOURNAL   Pharmacol Rev 64 (3), 540-582 (2012)
   PUBMED   22679221
  REMARK    Review article
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Yang,J. and Fuller,P.J.
  TITLE     Interactions of the mineralocorticoid receptor--within and without
  JOURNAL   Mol Cell Endocrinol 350 (2), 196-205 (2012)
   PUBMED   21784126
  REMARK    Review article
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Hirata,T. and Narumiya,S.
  TITLE     Prostanoids as regulators of innate and adaptive immunity
  JOURNAL   Adv Immunol 116, 143-174 (2012)
   PUBMED   23063076
  REMARK    Review article
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Weaver,A.J., Sullivan,W.P., Felts,S.J., Owen,B.A. and Toft,D.O.
  TITLE     Crystal structure and activity of human p23, a heat shock protein
            90 co-chaperone
  JOURNAL   J Biol Chem 275 (30), 23045-23052 (2000)
   PUBMED   10811660
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Weikl,T., Abelmann,K. and Buchner,J.
  TITLE     An unstructured C-terminal region of the Hsp90 co-chaperone p23 is
            important for its chaperone function
  JOURNAL   J Mol Biol 293 (3), 685-691 (1999)
   PUBMED   10543959
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Holt,S.E., Aisner,D.L., Baur,J., Tesmer,V.M., Dy,M., Ouellette,M.,
            Trager,J.B., Morin,G.B., Toft,D.O., Shay,J.W., Wright,W.E. and
            White,M.A.
  TITLE     Functional requirement of p23 and Hsp90 in telomerase complexes
  JOURNAL   Genes Dev 13 (7), 817-826 (1999)
   PUBMED   10197982
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Whitesell,L., Sutphin,P.D., Pulcini,E.J., Martinez,J.D. and
            Cook,P.H.
  TITLE     The physical association of multiple molecular chaperone proteins
            with mutant p53 is altered by geldanamycin, an hsp90-binding agent
  JOURNAL   Mol Cell Biol 18 (3), 1517-1524 (1998)
   PUBMED   9488468
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Czar,M.J., Welsh,M.J. and Pratt,W.B.
  TITLE     Immunofluorescence localization of the 90-kDa heat-shock protein to
            cytoskeleton
  JOURNAL   Eur J Cell Biol 70 (4), 322-330 (1996)
   PUBMED   8864660
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166579.1, DY308945.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..160
                     /product="prostaglandin E synthase 3"
                     /EC_number="5.3.99.3"
                     /note="cPGES; hsp90 co-chaperone; telomerase-binding
                     protein p23; progesterone receptor complex p23; cytosolic
                     prostaglandin E2 synthase; prostaglandin E synthase 3
                     (cytosolic)"
                     /calculated_mol_wt=18590
     Region          3..109
                     /region_name="p23"
                     /note="p23 binds heat shock protein (Hsp)90 and
                     participates in the folding of a number of Hsp90 clients,
                     including the progesterone receptor. p23 also has a
                     passive chaperoning activity and in addition may
                     participate in prostaglandin synthesis; cd00237"
                     /db_xref="CDD:107218"
     Site            order(8,53,87..90,99,103,106)
                     /site_type="other"
                     /note="putative Hsp90 binding site [polypeptide binding]"
                     /db_xref="CDD:107218"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q15185; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15185; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Site            order(56,58,88,91..93)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107218"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15185; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q7; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Region          118..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P83868.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15185; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Site            142..143
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-7.
                     /evidence=ECO:0000250|UniProtKB:Q15185; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P83868.2)"
     Region          157..160
                     /region_name="PXLE motif.
                     /evidence=ECO:0000250|UniProtKB:Q15185"
                     /note="propagated from UniProtKB/Swiss-Prot (P83868.2)"
     CDS             1..160
                     /gene="Ptges3"
                     /gene_synonym="RGD1561913"
                     /coded_by="NM_001130989.2:293..775"
                     /db_xref="GeneID:362809"
                     /db_xref="RGD:1561913"
ORIGIN      
        1 mqpasakwyd rrdyvfiefc vedskdvnvn fekskltfsc lggsdnfkhl neidlfhcid
       61 pndskhkrtd rsilcclrkg esgqswprlt keraklnwls vdfnnwkdwe ddsdedmsnf
      121 drfsemmdhm ggdedvdlpe vdgadddsqd sddekmpdle
//
