ID   PGDH_MOUSE              Reviewed;         269 AA.
AC   Q8VCC1; Q61106;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)];
DE            Short=15-PGDH;
DE            EC=1.1.1.141 {ECO:0000305|PubMed:8950170};
DE   AltName: Full=Eicosanoid/docosanoid dehydrogenase [NAD(+)];
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:P15428};
DE            EC=1.1.1.232 {ECO:0000250|UniProtKB:P15428};
DE   AltName: Full=Prostaglandin dehydrogenase 1;
GN   Name=Hpgd; Synonyms=Pgdh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Lung;
RX   PubMed=8950170; DOI=10.1016/s0167-4781(96)00123-6;
RA   Matsuo M., Ensor C.M., Tai H.H.;
RT   "Cloning and expression of the cDNA for mouse NAD(+)-dependent 15-
RT   hydroxyprostaglandin dehydrogenase.";
RL   Biochim. Biophys. Acta 1309:21-24(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=20448048; DOI=10.1074/jbc.m109.084426;
RA   Shiraya K., Hirata T., Hatano R., Nagamori S., Wiriyasermkul P.,
RA   Jutabha P., Matsubara M., Muto S., Tanaka H., Asano S., Anzai N., Endou H.,
RA   Yamada A., Sakurai H., Kanai Y.;
RT   "A novel transporter of SLC22 family specifically transports prostaglandins
RT   and co-localizes with 15-hydroxyprostaglandin dehydrogenase in renal
RT   proximal tubules.";
RL   J. Biol. Chem. 285:22141-22151(2010).
CC   -!- FUNCTION: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a
CC       broad array of hydroxylated polyunsaturated fatty acids (mainly
CC       eicosanoids and docosanoids, including prostaglandins, lipoxins and
CC       resolvins), yielding their corresponding keto (oxo) metabolites (By
CC       similarity) (PubMed:8950170). Decreases the levels of the pro-
CC       proliferative prostaglandins such as prostaglandin E2 (whose activity
CC       is increased in cancer because of an increase in the expression of
CC       cyclooxygenase 2) and generates oxo-fatty acid products that can
CC       profoundly influence cell function by abrogating pro-inflammatory
CC       cytokine expression. Converts resolvins E1, D1 and D2 to their oxo
CC       products, which represents a mode of resolvin inactivation. Resolvin E1
CC       plays important roles during the resolution phase of acute
CC       inflammation, while resolvins D1 and D2 have a unique role in obesity-
CC       induced adipose inflammation (By similarity).
CC       {ECO:0000250|UniProtKB:P15428, ECO:0000269|PubMed:8950170}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) +
CC         NADH; Xref=Rhea:RHEA:11876, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:606564;
CC         EC=1.1.1.141; Evidence={ECO:0000305|PubMed:8950170};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11877;
CC         Evidence={ECO:0000305|PubMed:8950170};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + NAD(+) = 15-
CC         oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:23260, ChEBI:CHEBI:15378, ChEBI:CHEBI:57409,
CC         ChEBI:CHEBI:57410, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.232; Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23261;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + NAD(+) = 11-
CC         oxo-(5Z,8Z,12E,14Z)-eicosatetraenoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:48640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78836, ChEBI:CHEBI:90697;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48641;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lipoxin A4 + NAD(+) = 15-oxo-(5S,6R)-dihydroxy-
CC         (7E,9E,11Z,13E)-eicosatetraenoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:41572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:67026, ChEBI:CHEBI:78311;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41573;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z)-eicosatrienoate + H(+) +
CC         NADH = (5S,6R,15S)-trihydroxy-(7E,9E,11Z)-eicosatrienoate + NAD(+);
CC         Xref=Rhea:RHEA:41596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78325, ChEBI:CHEBI:78329;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41597;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prostaglandin A1 = 15-oxo-prostaglandin A1 + H(+) +
CC         NADH; Xref=Rhea:RHEA:41263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57398,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:85072;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41264;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) +
CC         NADH; Xref=Rhea:RHEA:16477, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397,
CC         ChEBI:CHEBI:57401, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16478;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=14-hydroxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + NAD(+) =
CC         14-oxo-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:48952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:90866, ChEBI:CHEBI:90867;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48953;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + resolvin E1 = 18-oxo-resolvin E1 + H(+) + NADH;
CC         Xref=Rhea:RHEA:49244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:91000, ChEBI:CHEBI:91001;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49245;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + resolvin D1 = 8-oxoresolvin D1 + H(+) + NADH;
CC         Xref=Rhea:RHEA:50124, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132080;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50125;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + resolvin D1 = 17-oxoresolvin D1 + H(+) + NADH;
CC         Xref=Rhea:RHEA:50128, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132081;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50129;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + resolvin D2 = 7-oxoresolvin D2 + H(+) + NADH;
CC         Xref=Rhea:RHEA:53584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137497;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53585;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + resolvin D2 = 16-oxoresolvin D2 + H(+) + NADH;
CC         Xref=Rhea:RHEA:53588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137498;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53589;
CC         Evidence={ECO:0000250|UniProtKB:P15428};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in proximal convoluted tubules of the
CC       kidney, where it colocalizes with the prostaglandin transporter
CC       SLC22A22 (at protein level) (PubMed:20448048). Expressed in lung,
CC       intestine, stomach and liver (PubMed:8950170).
CC       {ECO:0000269|PubMed:20448048, ECO:0000269|PubMed:8950170}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB41825.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U44389; AAB41825.1; ALT_FRAME; mRNA.
DR   EMBL; AK146038; BAE26850.1; -; mRNA.
DR   EMBL; BC021157; AAH21157.1; -; mRNA.
DR   CCDS; CCDS40341.1; -.
DR   RefSeq; NP_032304.2; NM_008278.2.
DR   AlphaFoldDB; Q8VCC1; -.
DR   SMR; Q8VCC1; -.
DR   BioGRID; 200406; 2.
DR   STRING; 10090.ENSMUSP00000034026; -.
DR   BindingDB; Q8VCC1; -.
DR   iPTMnet; Q8VCC1; -.
DR   PhosphoSitePlus; Q8VCC1; -.
DR   jPOST; Q8VCC1; -.
DR   MaxQB; Q8VCC1; -.
DR   PaxDb; 10090-ENSMUSP00000034026; -.
DR   PeptideAtlas; Q8VCC1; -.
DR   ProteomicsDB; 288131; -.
DR   Antibodypedia; 1511; 644 antibodies from 38 providers.
DR   DNASU; 15446; -.
DR   Ensembl; ENSMUST00000034026.10; ENSMUSP00000034026.9; ENSMUSG00000031613.10.
DR   GeneID; 15446; -.
DR   KEGG; mmu:15446; -.
DR   UCSC; uc009lso.1; mouse.
DR   AGR; MGI:108085; -.
DR   CTD; 3248; -.
DR   MGI; MGI:108085; Hpgd.
DR   VEuPathDB; HostDB:ENSMUSG00000031613; -.
DR   eggNOG; KOG4169; Eukaryota.
DR   GeneTree; ENSGT00940000154593; -.
DR   HOGENOM; CLU_010194_2_16_1; -.
DR   InParanoid; Q8VCC1; -.
DR   OMA; FCDPLTM; -.
DR   OrthoDB; 2082185at2759; -.
DR   PhylomeDB; Q8VCC1; -.
DR   TreeFam; TF324093; -.
DR   Reactome; R-MMU-2142700; Synthesis of Lipoxins (LX).
DR   Reactome; R-MMU-9018676; Biosynthesis of D-series resolvins.
DR   Reactome; R-MMU-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR   SABIO-RK; Q8VCC1; -.
DR   BioGRID-ORCS; 15446; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Hpgd; mouse.
DR   PRO; PR:Q8VCC1; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8VCC1; Protein.
DR   Bgee; ENSMUSG00000031613; Expressed in right lung lobe and 205 other cell types or tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0016404; F:15-hydroxyprostaglandin dehydrogenase (NAD+) activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISO:MGI.
DR   GO; GO:0004957; F:prostaglandin E receptor activity; ISS:UniProtKB.
DR   GO; GO:0097070; P:ductus arteriosus closure; IMP:UniProtKB.
DR   GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0030728; P:ovulation; ISS:UniProtKB.
DR   GO; GO:0007567; P:parturition; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR   GO; GO:1905828; P:regulation of prostaglandin catabolic process; ISS:UniProtKB.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd05323; ADH_SDR_c_like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44229; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   PANTHER; PTHR44229:SF4; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   Genevisible; Q8VCC1; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Fatty acid metabolism; Lipid metabolism; NAD; Oxidoreductase;
KW   Prostaglandin metabolism; Reference proteome; Tumor suppressor.
FT   CHAIN           1..269
FT                   /note="15-hydroxyprostaglandin dehydrogenase [NAD(+)]"
FT                   /id="PRO_0000253626"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..37
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..65
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        113
FT                   /note="S -> G (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="A -> S (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="E -> G (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="T -> A (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="N -> D (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="A -> P (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="T -> S (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="K -> E (in Ref. 1; AAB41825)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   269 AA;  29181 MW;  10E879A7E31A8E34 CRC64;
     MHVNGKVALV TGAAQGIGKA FAEALLLHGA KVALVDWNLE AGVKCKAALD EQFEPQKTLF
     VQCDVADQKQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW EQTLQINLVS VISGTYLGLD
     YMSKQNGGEG GIIINMSSLA GLMPVAQQPV YCASKHGIIG FTRSAAMAAN LMKSGVRLNV
     ICPGFVDTPI LESIEKEENM GQYIEYKDQI KAMMKFYGVL HPSTIANGLI NLIEDDALNG
     AIMKITASKG IHFQDYDISP LLVKAPLTS
//