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Database: UniProt
Entry: PTGR1_PIG
LinkDB: PTGR1_PIG
Original site: PTGR1_PIG 
ID   PTGR1_PIG               Reviewed;         329 AA.
AC   Q29073; O62642;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 135.
DE   RecName: Full=Prostaglandin reductase 1;
DE            Short=PRG-1;
DE   AltName: Full=15-oxoprostaglandin 13-reductase {ECO:0000303|PubMed:9461497};
DE            EC=1.3.1.48 {ECO:0000269|PubMed:9461497};
DE   AltName: Full=Dithiolethione-inducible gene 1 protein {ECO:0000250|UniProtKB:P97584};
DE            Short=D3T-inducible gene 1 protein {ECO:0000250|UniProtKB:P97584};
DE            Short=DIG-1 {ECO:0000250|UniProtKB:P97584};
DE   AltName: Full=Leukotriene B4 12-hydroxydehydrogenase {ECO:0000303|PubMed:8576264};
DE   AltName: Full=NAD(P)H-dependent alkenal/one oxidoreductase;
DE            EC=1.3.1.74 {ECO:0000250|UniProtKB:Q14914};
GN   Name=PTGR1; Synonyms=LTB4DH;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP   ACTIVITY, AND MUTAGENESIS OF ALA-149; ALA-150; GLY-152; GLY-155; GLY-159
RP   AND GLY-166.
RC   TISSUE=Kidney;
RX   PubMed=8576264; DOI=10.1074/jbc.271.5.2844;
RA   Yokomizo T., Ogawa Y., Uozumi N., Kume K., Izumi T., Shimizu T.;
RT   "cDNA cloning, expression, and mutagenesis study of leukotriene B4 12-
RT   hydroxydehydrogenase.";
RL   J. Biol. Chem. 271:2844-2850(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Lung;
RX   PubMed=9461497; DOI=10.1042/bj3300103;
RA   Ensor C.M., Zhang H., Tai H.-H.;
RT   "Purification, cDNA cloning and expression of 15-oxoprostaglandin 13-
RT   reductase from pig lung.";
RL   Biochem. J. 330:103-108(1998).
RN   [3]
RP   CHARACTERIZATION, PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   TISSUE=Kidney;
RX   PubMed=8394361; DOI=10.1016/s0021-9258(17)46820-7;
RA   Yokomizo T., Izumi T., Takahashi T., Kasama T., Kobayashi Y., Sato F.,
RA   Taketani Y., Shimizu T.;
RT   "Enzymatic inactivation of leukotriene B4 by a novel enzyme found in the
RT   porcine kidney. Purification and properties of leukotriene B4 12-
RT   hydroxydehydrogenase.";
RL   J. Biol. Chem. 268:18128-18135(1993).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10837478; DOI=10.1074/jbc.m002863200;
RA   Clish C.B., Levy B.D., Chiang N., Tai H.-H., Serhan C.N.;
RT   "Oxidoreductases in lipoxin A4 metabolic inactivation: a novel role for 15-
RT   onoprostaglandin 13-reductase/leukotriene B4 12-hydroxydehydrogenase in
RT   inflammation.";
RL   J. Biol. Chem. 275:25372-25380(2000).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=11688989; DOI=10.1006/bbrc.2001.5841;
RA   Clish C.B., Sun Y.P., Serhan C.N.;
RT   "Identification of dual cyclooxygenase-eicosanoid oxidoreductase
RT   inhibitors: NSAIDs that inhibit PG-LX reductase/LTB(4) dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 288:868-874(2001).
CC   -!- FUNCTION: NAD(P)H-dependent oxidoreductase involved in metabolic
CC       inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins
CC       (PG), leukotrienes (LT) and lipoxins (LX) (PubMed:8576264,
CC       PubMed:9461497, PubMed:10837478, PubMed:11688989). Preferentially uses
CC       NADPH over NADH as cofactor (PubMed:9461497). Catalyzes with high
CC       efficiency the reduction of the 13,14 double bond of 15-oxoPGs,
CC       including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-
CC       alpha (PubMed:9461497, PubMed:11688989). Catalyzes with lower
CC       efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its
CC       derivatives, converting them into biologically less active 12-oxo-LTB4
CC       metabolites (PubMed:8576264, PubMed:8394361). Reduces 15-oxo-LXA4 to
CC       13,14 dihydro-15-oxo-LXA4 and may promote neutrophil recruitment at the
CC       inflammatory site (PubMed:10837478, PubMed:11688989). Plays a role in
CC       metabolic detoxification of alkenals and ketones. Reduces alpha,beta-
CC       unsaturated alkenals and ketones, particularly those with medium-chain
CC       length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-
CC       2-one (By similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic
CC       lipid constituent of oxidized low-density lipoprotein particles (By
CC       similarity). {ECO:0000250|UniProtKB:P97584,
CC       ECO:0000250|UniProtKB:Q14914, ECO:0000269|PubMed:10837478,
CC       ECO:0000269|PubMed:11688989, ECO:0000269|PubMed:8394361,
CC       ECO:0000269|PubMed:8576264, ECO:0000269|PubMed:9461497}.
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:0000269|PubMed:9461497};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586;
CC         Evidence={ECO:0000305|PubMed:9461497};
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:0000269|PubMed:9461497};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC         Evidence={ECO:0000305|PubMed:9461497};
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:0000269|PubMed:11688989, ECO:0000269|PubMed:9461497};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC         Evidence={ECO:0000305|PubMed:11688989, ECO:0000305|PubMed:9461497};
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:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
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:0000269|PubMed:9461497};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590;
CC         Evidence={ECO:0000305|PubMed:9461497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) +
CC         NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309;
CC         Evidence={ECO:0000269|PubMed:8394361, ECO:0000269|PubMed:8576264};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609;
CC         Evidence={ECO:0000305|PubMed:8394361, ECO:0000305|PubMed:8576264};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy-
CC         leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:133346;
CC         Evidence={ECO:0000269|PubMed:8394361};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209;
CC         Evidence={ECO:0000305|PubMed:8394361};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy-
CC         (6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974;
CC         Evidence={ECO:0000269|PubMed:8394361};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205;
CC         Evidence={ECO:0000305|PubMed:8394361};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate +
CC         NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate +
CC         H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974,
CC         ChEBI:CHEBI:133975; Evidence={ECO:0000269|PubMed:8394361};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213;
CC         Evidence={ECO:0000305|PubMed:8394361};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z,13E)-eicosatetraenoate +
CC         H(+) + NADH = 15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z)-eicosatrienoate +
CC         NAD(+); Xref=Rhea:RHEA:41592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78311, ChEBI:CHEBI:78325;
CC         Evidence={ECO:0000269|PubMed:10837478, ECO:0000269|PubMed:11688989};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41593;
CC         Evidence={ECO:0000305|PubMed:10837478, ECO:0000305|PubMed:11688989};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) +
CC         NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112;
CC         Evidence={ECO:0000250|UniProtKB:P97584};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738;
CC         Evidence={ECO:0000250|UniProtKB:P97584};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH;
CC         Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH;
CC         Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618;
CC         Evidence={ECO:0000250|UniProtKB:Q14914};
CC   -!- ACTIVITY REGULATION: Down-regulated by nonsteroidal anti-inflammatory
CC       drugs diclofenac, indomethacin and niflumic acid.
CC       {ECO:0000269|PubMed:11688989}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.7 uM for 15-oxo-PGE1 {ECO:0000269|PubMed:9461497};
CC         KM=19 uM for 15-oxo-PGE2 {ECO:0000269|PubMed:9461497};
CC         KM=10 uM for LTB4 {ECO:0000269|PubMed:9461497};
CC         KM=153 uM for NADH {ECO:0000269|PubMed:9461497};
CC         KM=15 uM for NADPH {ECO:0000269|PubMed:9461497};
CC         KM=8 uM for LTB4 {ECO:0000269|PubMed:8394361};
CC         KM=14 uM for 6-trans-LTB4 {ECO:0000269|PubMed:8394361};
CC         KM=1.5 uM for NADP(+) {ECO:0000269|PubMed:8394361};
CC         Vmax=2470 nmol/min/mg enzyme with 15-keto-PGE1 as substrate
CC         {ECO:0000269|PubMed:9461497};
CC         Vmax=847 nmol/min/mg enzyme with 15-keto-PGE2 as substrate
CC         {ECO:0000269|PubMed:9461497};
CC         Vmax=7.0 nmol/min/mg enzyme with LTB4 as substrate
CC         {ECO:0000269|PubMed:9461497};
CC         Vmax=2352 nmol/min/mg enzyme with NADH as substrate
CC         {ECO:0000269|PubMed:9461497};
CC         Vmax=729 nmol/min/mg enzyme with NADPH as substrate
CC         {ECO:0000269|PubMed:9461497};
CC         Vmax=8.0 nmol/min/mg enzyme with LTB4 as substrate
CC         {ECO:0000269|PubMed:8394361};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:8394361};
CC   -!- SUBUNIT: Monomer or homodimer. {ECO:0000250|UniProtKB:Q9EQZ5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8394361}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously distributed in various tissues and
CC       leukocytes, the kidney and liver had the highest enzyme activities.
CC   -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC       {ECO:0000305}.
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DR   EMBL; D49386; BAA08381.1; -; mRNA.
DR   EMBL; U87622; AAC39170.1; -; mRNA.
DR   PIR; A47421; A47421.
DR   RefSeq; NP_999550.1; NM_214385.1.
DR   AlphaFoldDB; Q29073; -.
DR   SMR; Q29073; -.
DR   STRING; 9823.ENSSSCP00000039006; -.
DR   SwissLipids; SLP:000000733; -.
DR   PaxDb; 9823-ENSSSCP00000023451; -.
DR   PeptideAtlas; Q29073; -.
DR   Ensembl; ENSSSCT00005017036.1; ENSSSCP00005010141.1; ENSSSCG00005011097.1.
DR   Ensembl; ENSSSCT00005017053.1; ENSSSCP00005010153.1; ENSSSCG00005011097.1.
DR   Ensembl; ENSSSCT00005017071.1; ENSSSCP00005010169.1; ENSSSCG00005011097.1.
DR   Ensembl; ENSSSCT00005017093.1; ENSSSCP00005010183.1; ENSSSCG00005011097.1.
DR   Ensembl; ENSSSCT00005017113.1; ENSSSCP00005010196.1; ENSSSCG00005011097.1.
DR   Ensembl; ENSSSCT00035022658.1; ENSSSCP00035008340.1; ENSSSCG00035017612.1.
DR   Ensembl; ENSSSCT00070044298.1; ENSSSCP00070037326.1; ENSSSCG00070022262.1.
DR   Ensembl; ENSSSCT00070044304.1; ENSSSCP00070037331.1; ENSSSCG00070022262.1.
DR   Ensembl; ENSSSCT00070044312.1; ENSSSCP00070037338.1; ENSSSCG00070022262.1.
DR   Ensembl; ENSSSCT00070044338.1; ENSSSCP00070037361.1; ENSSSCG00070022262.1.
DR   Ensembl; ENSSSCT00070044343.1; ENSSSCP00070037366.1; ENSSSCG00070022262.1.
DR   GeneID; 397678; -.
DR   KEGG; ssc:397678; -.
DR   CTD; 22949; -.
DR   eggNOG; KOG1196; Eukaryota.
DR   InParanoid; Q29073; -.
DR   OrthoDB; 179761at2759; -.
DR   BRENDA; 1.3.1.48; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 1.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0036185; F:13-lipoxin reductase activity; IDA:UniProtKB.
DR   GO; GO:0036132; F:13-prostaglandin reductase activity; IDA:UniProtKB.
DR   GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IBA:GO_Central.
DR   GO; GO:0035798; F:2-alkenal reductase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0097257; F:leukotriene B4 12-hydroxy dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0036102; P:leukotriene B4 metabolic process; IDA:UniProtKB.
DR   GO; GO:2001302; P:lipoxin A4 metabolic process; IDA:UniProtKB.
DR   GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR   CDD; cd08294; leukotriene_B4_DH_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR020843; PKS_ER.
DR   InterPro; IPR014190; PTGR1.
DR   NCBIfam; TIGR02825; B4_12hDH; 1.
DR   PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR   PANTHER; PTHR43205:SF7; PROSTAGLANDIN REDUCTASE 1; 1.
DR   Pfam; PF16884; ADH_N_2; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Fatty acid metabolism;
KW   Hydroxylation; Lipid metabolism; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW   Prostaglandin metabolism; Reference proteome.
FT   CHAIN           1..329
FT                   /note="Prostaglandin reductase 1"
FT                   /id="PRO_0000218067"
FT   BINDING         152..155
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   BINDING         178
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   BINDING         193
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   BINDING         217
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   BINDING         239..245
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   BINDING         270..272
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   BINDING         321
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   MOD_RES         178
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q14914"
FT   MOD_RES         178
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91YR9"
FT   MUTAGEN         149
FT                   /note="A->E: Reduces activity by 90%."
FT                   /evidence="ECO:0000269|PubMed:8576264"
FT   MUTAGEN         149
FT                   /note="A->V: Reduces activity by half."
FT                   /evidence="ECO:0000269|PubMed:8576264"
FT   MUTAGEN         150
FT                   /note="A->V: No effect."
FT                   /evidence="ECO:0000269|PubMed:8576264"
FT   MUTAGEN         152
FT                   /note="G->V: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8576264"
FT   MUTAGEN         155
FT                   /note="G->V: Reduces activity by 99%."
FT                   /evidence="ECO:0000269|PubMed:8576264"
FT   MUTAGEN         159
FT                   /note="G->V: Reduces activity by 60%."
FT                   /evidence="ECO:0000269|PubMed:8576264"
FT   MUTAGEN         166
FT                   /note="G->V: Reduces activity by 99%."
FT                   /evidence="ECO:0000269|PubMed:8576264"
FT   CONFLICT        118
FT                   /note="T -> A (in Ref. 2; AAC39170)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  35762 MW;  D8893061A7EFBEEA CRC64;
     MVRAKSWTLK KHFVGYPTPS NFELKTVELP PLKNGEVLLE ALFLTVDPYM RIAARKLKEG
     DMMMGEQVAR VIESKNAAFP TGTIVVALLG WTTHSISDGK NLERLLAEWP DTLPLSLTLG
     TVGMPGLTAY FGLLDICGLK GGETVMVNAA AGAVGSVVGQ IAKLKGCKVV GAAGSDEKVA
     CLKKYGFDVA FNYKTIESLE ETLKKASPEG YDCYFDNVGG EFSNAVTSQM KKFGRIAICG
     AISTYNRTGP PPPGPPPEVV IYNELCFQGF IVTRWQGEVR QKALRDLLKW VSEGKIQYHE
     HITEGFENMP AAFMGMLKGE NLGKAIVKA
//
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