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PTGES_HORSE
ID   PTGES_HORSE             Reviewed;         153 AA.
AC   Q8HZJ2;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Prostaglandin E synthase;
DE            EC=5.3.99.3 {ECO:0000250|UniProtKB:O14684};
DE   AltName: Full=Glutathione peroxidase PTGES;
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:O14684};
DE   AltName: Full=Glutathione transferase PTGES;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:O14684};
DE   AltName: Full=Microsomal prostaglandin E synthase 1;
DE            Short=MPGES-1;
GN   Name=PTGES;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sirois J., Bouchard N., Filion F.;
RT   "Characterization of equine prostaglandin E synthase.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated
CC       prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the
CC       glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2
CC       (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli
CC       (By similarity). Plays a key role in inflammation response, fever and
CC       pain (By similarity). Catalyzes also the oxidoreduction of
CC       endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-
CC       hydroperoxy-PGE2. In addition, displays low glutathione transferase and
CC       glutathione-dependent peroxidase activities, toward 1-chloro-2,4-
CC       dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE),
CC       respectively (By similarity). {ECO:0000250|UniProtKB:O14684,
CC       ECO:0000250|UniProtKB:Q9JM51}.
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:0000250|UniProtKB:O14684};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC         Evidence={ECO:0000250|UniProtKB:O14684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin E2;
CC         Xref=Rhea:RHEA:53324, ChEBI:CHEBI:85166, ChEBI:CHEBI:137172;
CC         Evidence={ECO:0000250|UniProtKB:O14684};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53325;
CC         Evidence={ECO:0000250|UniProtKB:O14684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin G2 = (15S)-15-hydroperoxy-prostaglandin E2;
CC         Xref=Rhea:RHEA:64364, ChEBI:CHEBI:82629, ChEBI:CHEBI:152564;
CC         Evidence={ECO:0000250|UniProtKB:O14684};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64365;
CC         Evidence={ECO:0000250|UniProtKB:O14684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC         S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC         Evidence={ECO:0000250|UniProtKB:O14684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2
CC         glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:O14684};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC         Evidence={ECO:0000250|UniProtKB:O14684};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000250|UniProtKB:O14684}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:O14684}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O14684}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm,
CC       perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes
CC       with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment.
CC       {ECO:0000250|UniProtKB:O14684}.
CC   -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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DR   EMBL; AY057096; AAL18255.1; -; mRNA.
DR   RefSeq; NP_001075404.1; NM_001081935.1.
DR   RefSeq; XP_014591354.1; XM_014735868.1.
DR   RefSeq; XP_014591355.1; XM_014735869.1.
DR   AlphaFoldDB; Q8HZJ2; -.
DR   SMR; Q8HZJ2; -.
DR   STRING; 9796.ENSECAP00000001029; -.
DR   PaxDb; Q8HZJ2; -.
DR   PRIDE; Q8HZJ2; -.
DR   Ensembl; ENSECAT00000001327; ENSECAP00000001029; ENSECAG00000000943.
DR   GeneID; 100034143; -.
DR   KEGG; ecb:100034143; -.
DR   CTD; 9536; -.
DR   VGNC; VGNC:21990; PTGES.
DR   GeneTree; ENSGT00390000011980; -.
DR   InParanoid; Q8HZJ2; -.
DR   OrthoDB; 1591261at2759; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000002281; Chromosome 25.
DR   Bgee; ENSECAG00000000943; Expressed in chorionic villus and 20 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0004667; F:prostaglandin-D synthase activity; IEA:Ensembl.
DR   GO; GO:0050220; F:prostaglandin-E synthase activity; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0031620; P:regulation of fever generation; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR   Gene3D; 1.20.120.550; -; 1.
DR   InterPro; IPR023352; MAPEG-like_dom_sf.
DR   InterPro; IPR001129; Membr-assoc_MAPEG.
DR   InterPro; IPR040162; MGST1-like.
DR   PANTHER; PTHR10689; PTHR10689; 1.
DR   Pfam; PF01124; MAPEG; 1.
DR   SUPFAM; SSF161084; SSF161084; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..153
FT                   /note="Prostaglandin E synthase"
FT                   /id="PRO_0000217744"
FT   TOPO_DOM        1..13
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   TRANSMEM        14..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   TOPO_DOM        43..61
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   TRANSMEM        62..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   TOPO_DOM        92..96
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   TRANSMEM        97..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   TOPO_DOM        121..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   TRANSMEM        125..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   BINDING         39
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   BINDING         74..78
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   BINDING         114
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   BINDING         118
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   BINDING         127..131
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   SITE            50
FT                   /note="Essential for protaglandin-E synthase activity"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
FT   SITE            127
FT                   /note="Essential for protaglandin-E synthase activity"
FT                   /evidence="ECO:0000250|UniProtKB:O14684"
SQ   SEQUENCE   153 AA;  17172 MW;  41D409620B7233AB CRC64;
     MPPPSLAMVS GQALPAFLLC STLLVIKMYA VAVITGQVRL RKKAFANPED ALRHGGLQFH
     RDDQDVERCL RAHRNDMETI YPFLFLGLVY SFLGPDPFVA QMHFLVFFLG RMVHTVAYLG
     KLRAPTRSLA YTVAQLPCAS MALQIVWEAA RHL
 
 
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