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Database: UniProt
Entry: A0A5N3XYE4_MUNRE
LinkDB: A0A5N3XYE4_MUNRE
Original site: A0A5N3XYE4_MUNRE 
ID   A0A5N3XYE4_MUNRE        Unreviewed;       159 AA.
AC   A0A5N3XYE4;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   24-JAN-2024, entry version 12.
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};
DE   Flags: Fragment;
GN   ORFNames=FD755_009776 {ECO:0000313|EMBL:KAB0378198.1};
OS   Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Muntiacinae; Muntiacus.
OX   NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0378198.1, ECO:0000313|Proteomes:UP000326062};
RN   [1] {ECO:0000313|EMBL:KAB0378198.1, ECO:0000313|Proteomes:UP000326062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0378198.1};
RC   TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0378198.1};
RA   Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT   "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL   Submitted (JUN-2019) 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.
CC       {ECO:0000256|RuleBase:RU369032}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {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:KAB0378198.1}.
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DR   EMBL; VCEB01000004; KAB0378198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N3XYE4; -.
DR   SMR; A0A5N3XYE4; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000326062; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00237; p23; 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:UP000326062}.
FT   DOMAIN          1..89
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          123..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..159
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KAB0378198.1"
SQ   SEQUENCE   159 AA;  18566 MW;  DC064BB027CF4E1F CRC64;
     QPASAKWYDR RDYVFIEFCV EDSKDVNVNF EKSKLTFSCL GGSDNFKHLN EIDLFHCIDP
     NDSKHKRTDR SILCCLRKGE SGQSWPRLTK ERAKLNWLSV DFNNWKDWED DSDEDMSNFD
     RFSEMMNNMG GDEDVDLPEV DGADDDSQDS DDEKMPDLE
//
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