TEBP_MACFA
ID TEBP_MACFA Reviewed; 160 AA.
AC Q6PWL5; Q5DI75;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16303602; DOI=10.1016/j.prostaglandins.2005.02.005;
RA Parent J., Chapdelaine P., Fortier M.A.;
RT "Molecular cloning and tissue distribution of microsomal-1 and cytosolic
RT prostaglandin E synthases in macaque.";
RL Prostaglandins Other Lipid Mediat. 78:27-37(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-124, AND TISSUE SPECIFICITY.
RX PubMed=15774546; DOI=10.1093/humrep/deh784;
RA Duffy D.M., Seachord C.L., Dozier B.L.;
RT "Microsomal prostaglandin E synthase-1 (mPGES-1) is the primary form of
RT PGES expressed by the primate periovulatory follicle.";
RL Hum. Reprod. 20:1485-1492(2005).
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 -!- TISSUE SPECIFICITY: Detected in granulosa cells of periovulatory
CC follicles. Detected at high levels in lung, and at lower levels in
CC endometrium, ovary, myometrium, oviduct and liver (at protein level).
CC Detected in endometrium, myometrium, oviduct and ovary, and at low
CC levels in liver and lung. {ECO:0000269|PubMed:15774546,
CC ECO:0000269|PubMed:16303602}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR EMBL; AY573810; AAS89038.1; -; mRNA.
DR EMBL; AY805116; AAW83054.1; -; mRNA.
DR RefSeq; NP_001270588.1; NM_001283659.1.
DR AlphaFoldDB; Q6PWL5; -.
DR BMRB; Q6PWL5; -.
DR SMR; Q6PWL5; -.
DR STRING; 9541.XP_005571313.1; -.
DR Ensembl; ENSMFAT00000083615; ENSMFAP00000053375; ENSMFAG00000045371.
DR GeneID; 102140495; -.
DR CTD; 10728; -.
DR VEuPathDB; HostDB:ENSMFAG00000045371; -.
DR eggNOG; KOG3158; Eukaryota.
DR GeneTree; ENSGT00940000154256; -.
DR OMA; DDYANNF; -.
DR BRENDA; 5.3.99.3; 1793.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000045371; Expressed in lung and 13 other tissues.
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 1: Evidence at protein 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_0000288779"
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
