PTGR2_BOVIN
ID PTGR2_BOVIN Reviewed; 351 AA.
AC Q32L99;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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}.
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DR EMBL; BC109688; AAI09689.1; -; mRNA.
DR RefSeq; NP_001068717.1; NM_001075249.2.
DR RefSeq; XP_005212001.1; XM_005211944.1.
DR RefSeq; XP_015328711.1; XM_015473225.1.
DR RefSeq; XP_015328712.1; XM_015473226.1.
DR AlphaFoldDB; Q32L99; -.
DR SMR; Q32L99; -.
DR STRING; 9913.ENSBTAP00000004878; -.
DR PaxDb; Q32L99; -.
DR PeptideAtlas; Q32L99; -.
DR PRIDE; Q32L99; -.
DR Ensembl; ENSBTAT00000004878; ENSBTAP00000004878; ENSBTAG00000003747.
DR GeneID; 506263; -.
DR KEGG; bta:506263; -.
DR CTD; 145482; -.
DR VEuPathDB; HostDB:ENSBTAG00000003747; -.
DR eggNOG; KOG1196; Eukaryota.
DR GeneTree; ENSGT00940000156793; -.
DR HOGENOM; CLU_026673_29_2_1; -.
DR InParanoid; Q32L99; -.
DR OMA; ECPKGVD; -.
DR OrthoDB; 884151at2759; -.
DR TreeFam; TF324201; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000003747; Expressed in caput epididymis and 107 other tissues.
DR ExpressionAtlas; Q32L99; baseline.
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; 1.
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_0000285789"
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; 38400 MW; 6BC981F3DDA5A9B8 CRC64;
MIVQRVVLNS RPGKNGHPVA ENFRVEEVNL PDCVNEGQVQ VRTLYLSVDP YMRCRMNEDT
GSDYITPWQL SQVVDGGGVG IIEESKHTNF MKGDFVTSFY WPWQTKVILD GNILEKVDPQ
LVDGHLSYFL GAIGMPGLTS LIGVQEKGHI TAGSNQTMVV SGAAGACGSL AGQIGRLLGC
SRVVGICGTP EKCLFLTSEL GFDAAINYKE GNVAEQLHKL CPAGVDVYFD NVGGDISDTV
ISQMNQNSHI ILCGQISQYN KDVPYPPPLP PAIEAIQKER NITRERFLVL NYKDKFEFGI
LQLSQWFKEG KLKIKETMIN GLENMGAAFQ SMMTGGNIGK QIVCISGDTS L
