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Database: UniProt
Entry: A0A2K6PSX1_RHIRO
LinkDB: A0A2K6PSX1_RHIRO
Original site: A0A2K6PSX1_RHIRO 
ID   A0A2K6PSX1_RHIRO        Unreviewed;       164 AA.
AC   A0A2K6PSX1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000019629.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000019629.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K6PSX1; -.
DR   STRING; 61622.ENSRROP00000019629; -.
DR   Ensembl; ENSRROT00000043802.1; ENSRROP00000019629.1; ENSRROG00000033807.1.
DR   GeneTree; ENSGT00940000154256; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000233200; 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   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:UP000233200}.
FT   DOMAIN          2..91
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
SQ   SEQUENCE   164 AA;  19507 MW;  B1FCF0E11187230F CRC64;
     MVQPASAKWY DRRDYVFIEF CVEDSKDVNV NFEKSKLTFS CLGGSDNFKH LNEIDLFHCI
     DPNDSKHKRT DRSILCCLRK GESGQSWPRL TKERAKLNWL SVDFNNWKDW EDDSDEDMSN
     FDRFSEDSQD SDDESKYIKS MFTQRYFASK TKLKIEMLTS FEKK
//
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