ID A0A7J7Z8G9_MYOMY Unreviewed; 160 AA.
AC A0A7J7Z8G9;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE RecName: Full=Prostaglandin E synthase 3 {ECO:0000256|ARBA:ARBA00040552, ECO:0000256|RuleBase:RU369032};
DE Short=cPGES {ECO:0000256|RuleBase:RU369032};
DE EC=5.3.99.3 {ECO:0000256|ARBA:ARBA00012203, ECO:0000256|RuleBase:RU369032};
DE AltName: Full=Cytosolic prostaglandin E2 synthase {ECO:0000256|ARBA:ARBA00042997, ECO:0000256|RuleBase:RU369032};
GN ORFNames=mMyoMyo1_016002 {ECO:0000313|EMBL:KAF6370236.1};
OS Myotis myotis (Greater mouse-eared bat) (Vespertilio myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6370236.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6370236.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6370236.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6370236.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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:0000256|ARBA:ARBA00045393}.
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:0000256|ARBA:ARBA00000609,
CC ECO:0000256|RuleBase:RU369032};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004702, ECO:0000256|RuleBase:RU369032}.
CC -!- SUBUNIT: Forms a complex with HSP70, HSP90 and other chaperones.
CC {ECO:0000256|RuleBase:RU369032}.
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:0000256|ARBA:ARBA00046445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU369032}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733, ECO:0000256|RuleBase:RU369032}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6370236.1}.
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DR EMBL; JABWUV010000003; KAF6370236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J7Z8G9; -.
DR SMR; A0A7J7Z8G9; -.
DR VEuPathDB; HostDB:GeneID_118650202; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000527355; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:TreeGrafter.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:TreeGrafter.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006457; P:protein folding; IEA:TreeGrafter.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; IEA:TreeGrafter.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IEA:TreeGrafter.
DR CDD; cd00237; p23; 1.
DR FunFam; 2.60.40.790:FF:000003; prostaglandin E synthase 3; 1.
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:SF3; PROSTAGLANDIN E SYNTHASE 3; 1.
DR PANTHER; PTHR22932; TELOMERASE-BINDING PROTEIN P23 HSP90 CO-CHAPERONE; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|RuleBase:RU369032};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369032};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU369032};
KW Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585,
KW ECO:0000256|RuleBase:RU369032};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Reference proteome {ECO:0000313|Proteomes:UP000527355}.
FT DOMAIN 1..90
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 124..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 160 AA; 18697 MW; 23538BB9D7AFD73F CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
//
