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Database: UniProt
Entry: G7PII7_MACFA
LinkDB: G7PII7_MACFA
Original site: G7PII7_MACFA 
ID   G7PII7_MACFA            Unreviewed;       153 AA.
AC   G7PII7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=EGM_03395 {ECO:0000313|EMBL:EHH66410.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1] {ECO:0000313|EMBL:EHH66410.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CE-4 {ECO:0000313|EMBL:EHH66410.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
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   EMBL; CM001286; EHH66410.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7PII7; -.
DR   SMR; G7PII7; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000009130; Chromosome 11.
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}.
FT   DOMAIN          1..89
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          123..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..153
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHH66410.1"
FT   NON_TER         153
FT                   /evidence="ECO:0000313|EMBL:EHH66410.1"
SQ   SEQUENCE   153 AA;  17852 MW;  4E1FC254DAAF8F9B CRC64;
     QPASAKWYDR RDYVFIEFCV EDSKDVNVNF EKSKLTFSCL GGSDNFKHLN EIDLFHCIDP
     NDSKHKRTDR SILCCLRKGE SGQSWPRLTK ERAKLNWLSV DFNNWKDWED DSDEDMSNFD
     RFSEMMNNMG GDEDVDLPEV DGADDDSQDS DDE
//
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