PTGR2_PONAB
ID PTGR2_PONAB Reviewed; 351 AA.
AC Q5R806;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Prostaglandin reductase 2;
DE Short=PRG-2;
DE EC=1.3.1.48;
DE AltName: Full=15-oxoprostaglandin 13-reductase;
GN Name=PTGR2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on
CC 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha
CC with highest activity towards 15-keto-PGE2. Overexpression represses
CC transcriptional activity of PPARG and inhibits adipocyte
CC differentiation. {ECO:0000250|UniProtKB:Q8VDQ1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NAD(+) = 15-
CC oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-
CC oxoprostaglandin E2 + H(+) + NADPH; Xref=Rhea:RHEA:11912,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin
CC F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374,
CC ChEBI:CHEBI:133409; Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-
CC oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:133408;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-
CC oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:79072, ChEBI:CHEBI:133411;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH92104.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR859950; CAH92104.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q5R806; -.
DR SMR; Q5R806; -.
DR STRING; 9601.ENSPPYP00000006793; -.
DR eggNOG; KOG1196; Eukaryota.
DR InParanoid; Q5R806; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036132; F:13-prostaglandin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR CDD; cd08293; PTGR2; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR037399; PTGR2.
DR PANTHER; PTHR43205; PTHR43205; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipid metabolism; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..351
FT /note="Prostaglandin reductase 2"
FT /id="PRO_0000218072"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165..168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 253..259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 287..289
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 288..290
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 38479 MW; A0BF58632E0CE7D8 CRC64;
MIVQRVVLNS RPGKNGNPVA ENFRMEEVYL PDNINEGQVQ VRTLYLSVDP YMRCRMNEDT
GTDYITPWQL SQVVDGGGIG IIEESKHTNL TKGDFVTSFY WPWQTKVILD GNSLEKVDPQ
LVDGHLSYFL GAIGMPGLTS LIGIQEKGHI TAGSNKTMVV SGAAGACGSV AGQIGHLLGC
SRVVGICGTH EKCVLLTSEL GFDAAINYKK DNVAEQLRES CPAGVDVYFD NVGGNISDTV
ISQMNENSHI ILCGQISQYN KDVPYPPPLS PAIEAIQKER NITRERFLVL NYRDKFEPGI
LQLSQWFKEG KLKIKETVIN GLENMGAAFQ SMMTGGNIGK QIVCISEEIS L
