TEBP_BOVIN
ID TEBP_BOVIN Reviewed; 160 AA.
AC Q3ZBF7; Q66LN1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Endometrium;
RX PubMed=15744024; DOI=10.1095/biolreprod.104.037036;
RA Parent J., Fortier M.A.;
RT "Expression and contribution of three different isoforms of prostaglandin E
RT synthase in the bovine endometrium.";
RL Biol. Reprod. 73:36-44(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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:0000269|PubMed:15744024}.
CC -!- TISSUE SPECIFICITY: Detected in testis and ovary, at lower levels in
CC endometrium, myometrium, kidney and lung, and only faintly in spleen,
CC heart and muscle (at protein level). Expressed at high levels in
CC glandular and luminal epithelial cells of the endometrium, but also
CC detected in stromal cells (at protein level).
CC {ECO:0000269|PubMed:15744024}.
CC -!- INDUCTION: Expression declines progressively during the estrous cycle;
CC it is higher at the beginning (days 1-9) and then follows a progressive
CC decline to reach its lowest point at the follicular phase of the cycle
CC (days 19-21). {ECO:0000269|PubMed:15744024}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR EMBL; AY692440; AAU04847.1; -; mRNA.
DR EMBL; BC103350; AAI03351.1; -; mRNA.
DR RefSeq; NP_001007807.2; NM_001007806.2.
DR AlphaFoldDB; Q3ZBF7; -.
DR BMRB; Q3ZBF7; -.
DR SMR; Q3ZBF7; -.
DR STRING; 9913.ENSBTAP00000023908; -.
DR PaxDb; Q3ZBF7; -.
DR PRIDE; Q3ZBF7; -.
DR GeneID; 493638; -.
DR KEGG; bta:493638; -.
DR CTD; 10728; -.
DR eggNOG; KOG3158; Eukaryota.
DR HOGENOM; CLU_078883_1_2_1; -.
DR InParanoid; Q3ZBF7; -.
DR OrthoDB; 1461729at2759; -.
DR TreeFam; TF315077; -.
DR BRENDA; 5.3.99.3; 908.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IBA:GO_Central.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
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_0000288778"
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"
FT CONFLICT 12..13
FT /note="RD -> GG (in Ref. 1; AAU04847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 18697 MW; 23538BB9D7AFD73F CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
