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Database: UniProt
Entry: A0A0B2VY83_TOXCA
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ID   A0A0B2VY83_TOXCA        Unreviewed;       335 AA.
AC   A0A0B2VY83;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Prostaglandin E synthase 2 {ECO:0000256|ARBA:ARBA00019474};
DE            EC=5.3.99.3 {ECO:0000256|ARBA:ARBA00012203};
DE   AltName: Full=Microsomal prostaglandin E synthase 2 {ECO:0000256|ARBA:ARBA00031041};
GN   Name=Ptges2 {ECO:0000313|EMBL:KHN86389.1};
GN   ORFNames=Tcan_13608 {ECO:0000313|EMBL:KHN86389.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN86389.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN86389.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN86389.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-
CC         heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644,
CC         ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274;
CC         Evidence={ECO:0000256|ARBA:ARBA00023930};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48645;
CC         Evidence={ECO:0000256|ARBA:ARBA00023930};
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:ARBA00023931};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC         Evidence={ECO:0000256|ARBA:ARBA00023931};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004702}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409}.
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:KHN86389.1}.
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DR   EMBL; JPKZ01000627; KHN86389.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VY83; -.
DR   STRING; 6265.A0A0B2VY83; -.
DR   OMA; DYCLTEG; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:InterPro.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03197; GST_C_mPGES2; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 6.20.200.30; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR034334; PGES2.
DR   InterPro; IPR034335; PGES2_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12782; MICROSOMAL PROSTAGLANDIN E SYNTHASE-2; 1.
DR   PANTHER; PTHR12782:SF5; PROSTAGLANDIN E SYNTHASE 2; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDG01182; Prostaglandin_E_synthase_like; 1.
DR   SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW   Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..335
FT                   /note="Prostaglandin E synthase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002096390"
FT   DOMAIN          51..129
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
SQ   SEQUENCE   335 AA;  38873 MW;  B5275EE85F79E9CB CRC64;
     MALLWTRSAL FGGSVAVHLT ESSEKADKAW NVDQATQKRE LVASDVDKTL LNLRLYQYQT
     CPFCCKVRTF LDYYGFQYEL VEVNPITKTQ LRFSPNYKKV PILVAGGDIV LTESSLIVSV
     LSTFLHRTNR SLNDVVQFYP EIKSIDPKTK KELLLCPNKY YIMLEDTKLS DEQIQNSREE
     REWREWVDEH FIHLISPNVY RTWSESLATF RWFSEVGQWH DAFSPWERYL AVYAGAAVMF
     FVSKRLKKRH NIVDERTALM DACEQWMSAL GDRPFLGGRQ PNLADLALYG AMNSFYGCAA
     FAELLERTRI GVWFERMRSA VESRAGSSLM RSRCR
//
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