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 03-AUG-2022, entry version 129.
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.ENSSSCP00000023451; -.
DR SwissLipids; SLP:000000733; -.
DR PeptideAtlas; Q29073; -.
DR PRIDE; Q29073; -.
DR Ensembl; ENSSSCT00005017036; ENSSSCP00005010141; ENSSSCG00005011097.
DR Ensembl; ENSSSCT00005017053; ENSSSCP00005010153; ENSSSCG00005011097.
DR Ensembl; ENSSSCT00005017071; ENSSSCP00005010169; ENSSSCG00005011097.
DR Ensembl; ENSSSCT00005017093; ENSSSCP00005010183; ENSSSCG00005011097.
DR Ensembl; ENSSSCT00005017113; ENSSSCP00005010196; ENSSSCG00005011097.
DR Ensembl; ENSSSCT00035022658; ENSSSCP00035008340; ENSSSCG00035017612.
DR Ensembl; ENSSSCT00070044298; ENSSSCP00070037326; ENSSSCG00070022262.
DR Ensembl; ENSSSCT00070044304; ENSSSCP00070037331; ENSSSCG00070022262.
DR Ensembl; ENSSSCT00070044312; ENSSSCP00070037338; ENSSSCG00070022262.
DR Ensembl; ENSSSCT00070044338; ENSSSCP00070037361; ENSSSCG00070022262.
DR Ensembl; ENSSSCT00070044343; ENSSSCP00070037366; ENSSSCG00070022262.
DR GeneID; 397678; -.
DR KEGG; ssc:397678; -.
DR CTD; 22949; -.
DR eggNOG; KOG1196; Eukaryota.
DR InParanoid; Q29073; -.
DR BRENDA; 1.3.1.48; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 1.
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 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 PANTHER; PTHR43205; PTHR43205; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02825; B4_12hDH; 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
