ID A0A2Y9L0G4_ENHLU Unreviewed; 148 AA.
AC A0A2Y9L0G4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 Name=LOC111160212 {ECO:0000313|RefSeq:XP_022378828.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022378828.1};
RN [1] {ECO:0000313|RefSeq:XP_022378828.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022378828.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_022378828.1; XM_022523120.1.
DR AlphaFoldDB; A0A2Y9L0G4; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000248482; Unplaced.
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 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:UP000248482}.
FT DOMAIN 1..90
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 116..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 148 AA; 17257 MW; 72AB26522A32F6C1 CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRVD FNNWKDWEDD SDEDMSNFDR FSEMMNNMGG
DEDVDLPEVD GADDDSQDSD DEKMPDLE
//
