TEBP_RAT
ID TEBP_RAT Reviewed; 160 AA.
AC P83868;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Prostaglandin E synthase 3;
DE EC=5.3.99.3 {ECO:0000269|PubMed:10922363};
DE AltName: Full=Cytosolic prostaglandin E2 synthase;
DE Short=cPGES;
DE AltName: Full=Hsp90 co-chaperone;
DE AltName: Full=Progesterone receptor complex p23;
DE AltName: Full=Telomerase-binding protein p23;
GN Name=Ptges3 {ECO:0000250|UniProtKB:Q15185};
GN Synonyms=Tebp {ECO:0000250|UniProtKB:Q15185};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG The MGC Project Team;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-20; 33-42 AND 53-62, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION, AND PATHWAY.
RC STRAIN=Wistar {ECO:0000269|PubMed:10922363};
RC TISSUE=Brain {ECO:0000269|PubMed:10922363};
RX PubMed=10922363; DOI=10.1074/jbc.m003504200;
RA Tanioka T., Nakatani Y., Semmyo N., Murakami M., Kudo I.;
RT "Molecular identification of cytosolic prostaglandin E2 synthase that is
RT functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2
RT biosynthesis.";
RL J. Biol. Chem. 275:32775-32782(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND SER-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cytosolic prostaglandin synthase that catalyzes the
CC oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin
CC E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to
CC genomic response elements in a hormone-dependent manner and disrupts
CC receptor-mediated transcriptional activation, by promoting disassembly
CC of transcriptional regulatory complexes. Facilitates HIF alpha proteins
CC hydroxylation via interaction with EGLN1/PHD2, leading to recruit
CC EGLN1/PHD2 to the HSP90 pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q15185, ECO:0000269|PubMed:10922363}.
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:10922363};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000269|PubMed:10922363}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2. Binds to the progesterone receptor. Interacts with
CC TERT; the interaction, together with HSP90AA1, is required for correct
CC assembly and stabilization of the telomerase holoenzyme complex.
CC Interacts (via PXLE motif) with EGLN1/PHD2, recruiting EGLN1/PHD2 to
CC the HSP90 pathway to facilitate HIF alpha proteins hydroxylation.
CC Interacts with HSP90AA1, FLCN, FNIP1 and FNIP2.
CC {ECO:0000250|UniProtKB:Q15185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis.
CC {ECO:0000269|PubMed:10922363}.
CC -!- INDUCTION: In brain, by LPS. {ECO:0000269|PubMed:10922363}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CK475788; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CK475788; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001124461.1; NM_001130989.1.
DR AlphaFoldDB; P83868; -.
DR BMRB; P83868; -.
DR SMR; P83868; -.
DR BioGRID; 263737; 1.
DR STRING; 10116.ENSRNOP00000003787; -.
DR iPTMnet; P83868; -.
DR PhosphoSitePlus; P83868; -.
DR SwissPalm; P83868; -.
DR jPOST; P83868; -.
DR PaxDb; P83868; -.
DR PRIDE; P83868; -.
DR GeneID; 362809; -.
DR KEGG; rno:362809; -.
DR UCSC; RGD:1561913; rat.
DR CTD; 10728; -.
DR RGD; 1561913; Ptges3.
DR VEuPathDB; HostDB:ENSRNOG00000002642; -.
DR eggNOG; KOG3158; Eukaryota.
DR HOGENOM; CLU_078883_1_2_1; -.
DR InParanoid; P83868; -.
DR OMA; DDYANNF; -.
DR OrthoDB; 1461729at2759; -.
DR PhylomeDB; P83868; -.
DR TreeFam; TF315077; -.
DR Reactome; R-RNO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-3371511; HSF1 activation.
DR Reactome; R-RNO-3371568; Attenuation phase.
DR Reactome; R-RNO-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-RNO-8939211; ESR-mediated signaling.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR SABIO-RK; P83868; -.
DR UniPathway; UPA00662; -.
DR ChiTaRS; Ptges3; rat.
DR PRO; PR:P83868; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000002642; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P83868; baseline and differential.
DR Genevisible; P83868; RN.
DR GO; GO:0005884; C:actin filament; IDA:RGD.
DR GO; GO:0101031; C:chaperone complex; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:RGD.
DR GO; GO:0002039; F:p53 binding; IDA:RGD.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IDA:RGD.
DR GO; GO:0003720; F:telomerase activity; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:RGD.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:RGD.
DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISO:RGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; ISO:RGD.
DR GO; GO:0060430; P:lung saccule development; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:RGD.
DR GO; GO:0006693; P:prostaglandin metabolic process; IMP:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; ISO:RGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISO:RGD.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932; PTHR22932; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Isomerase; Isopeptide bond; Lipid biosynthesis;
KW Lipid metabolism; Phosphoprotein; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome; Ubl conjugation.
FT CHAIN 1..160
FT /note="Prostaglandin E synthase 3"
FT /id="PRO_0000291382"
FT DOMAIN 1..90
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 118..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..160
FT /note="PXLE motif"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT COMPBIAS 119..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0Q7"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT CONFLICT 2
FT /note="Q -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="T -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 18721 MW; 7702CB59D7AFD739 CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMDHM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
