ID C1BYL6_ESOLU Unreviewed; 159 AA.
AC C1BYL6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Prostaglandin E synthase 3 {ECO:0000256|ARBA:ARBA00040552};
DE EC=5.3.99.3 {ECO:0000256|ARBA:ARBA00012203};
DE AltName: Full=Cytosolic prostaglandin E2 synthase {ECO:0000256|ARBA:ARBA00042997};
GN Name=TEBP {ECO:0000313|EMBL:ACO14119.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|EMBL:ACO14119.1};
RN [1] {ECO:0000313|EMBL:ACO14119.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Head kidney {ECO:0000313|EMBL:ACO14119.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [2] {ECO:0000313|EMBL:ACO14119.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Head kidney {ECO:0000313|EMBL:ACO14119.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., Jantzen S., Cooper G., Davidson W.S., Koop B.F.;
RT "Esox lucius ESTs and full-length cDNAs.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004702}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733}.
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DR EMBL; BT079695; ACO14119.1; -; mRNA.
DR AlphaFoldDB; C1BYL6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501}.
FT DOMAIN 1..90
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 126..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 159 AA; 18527 MW; 54ACBE96C2C3FAAA CRC64;
MHPATAKWYD RRDSVYIEFC VADSKDVKIN FEKAKFVFSY LGGIDQVKHE NEVDLFEAID
QNESMHKRTD RSVLCCLRKA EPGKAWPRLT KEKAKLTWLS VDFNNWKDWE DDSDEELGNF
DRFSEMMNNM GGEDDLPDLD VADDDESADS DDEKMPDLE
//
