TEBP_PONAB
ID TEBP_PONAB Reviewed; 160 AA.
AC Q5NVM4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Prostaglandin E synthase 3;
DE EC=5.3.99.3 {ECO:0000250|UniProtKB:Q15185};
DE AltName: Full=Cytosolic prostaglandin E2 synthase;
DE Short=cPGES;
GN Name=PTGES3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytosolic prostaglandin synthase that catalyzes the
CC oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin
CC E2 (PGE2). Molecular chaperone that localizes to genomic response
CC elements in a hormone-dependent manner and disrupts receptor-mediated
CC transcriptional activation, by promoting disassembly of transcriptional
CC regulatory complexes. Facilitates HIF alpha proteins hydroxylation via
CC interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90
CC pathway. {ECO:0000250|UniProtKB:Q15185}.
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:0000250|UniProtKB:Q15185};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000250|UniProtKB:Q15185}.
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 -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR EMBL; CR925997; CAI29639.1; -; mRNA.
DR RefSeq; NP_001127087.1; NM_001133615.1.
DR AlphaFoldDB; Q5NVM4; -.
DR BMRB; Q5NVM4; -.
DR SMR; Q5NVM4; -.
DR STRING; 9601.ENSPPYP00000005319; -.
DR Ensembl; ENSPPYT00000005528; ENSPPYP00000005319; ENSPPYG00000004669.
DR GeneID; 100174118; -.
DR KEGG; pon:100174118; -.
DR CTD; 10728; -.
DR eggNOG; KOG3158; Eukaryota.
DR GeneTree; ENSGT00940000154256; -.
DR HOGENOM; CLU_078883_1_2_1; -.
DR InParanoid; Q5NVM4; -.
DR OMA; DDYANNF; -.
DR OrthoDB; 1461729at2759; -.
DR TreeFam; TF315077; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Isomerase; Isopeptide bond; Lipid biosynthesis; Lipid metabolism;
KW Phosphoprotein; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..160
FT /note="Prostaglandin E synthase 3"
FT /id="PRO_0000288780"
FT DOMAIN 1..90
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 124..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 135..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:0000250|UniProtKB:Q15185"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15185"
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"
SQ SEQUENCE 160 AA; 18697 MW; 23538BB9D7AFD73F CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
