PGDH_HUMAN
ID PGDH_HUMAN Reviewed; 266 AA.
AC P15428; B4DTA4; B4DU74; B4DV57; D3DP43; E7EV11; O00749; Q06F08; Q12998;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)] {ECO:0000305};
DE Short=15-PGDH;
DE EC=1.1.1.141 {ECO:0000269|PubMed:15044627, ECO:0000269|PubMed:15574495, ECO:0000269|PubMed:16757471, ECO:0000269|PubMed:16828555, ECO:0000269|PubMed:25586183, ECO:0000269|PubMed:8086429};
DE AltName: Full=Eicosanoid/docosanoid dehydrogenase [NAD(+)];
DE EC=1.1.1.- {ECO:0000269|PubMed:10837478, ECO:0000269|PubMed:16757471, ECO:0000269|PubMed:21916491, ECO:0000269|PubMed:22844113, ECO:0000269|PubMed:25586183, ECO:0000269|PubMed:8086429};
DE EC=1.1.1.232 {ECO:0000269|PubMed:21916491};
DE AltName: Full=Prostaglandin dehydrogenase 1;
DE AltName: Full=Short chain dehydrogenase/reductase family 36C member 1;
GN Name=HPGD {ECO:0000312|HGNC:HGNC:5154}; Synonyms=PGDH1, SDR36C1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=2337593; DOI=10.1021/bi00455a021;
RA Krook M., Marekov L., Joernvall H.;
RT "Purification and structural characterization of placental NAD(+)-linked
RT 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the
RT enzyme to belong to the short-chain alcohol dehydrogenase family.";
RL Biochemistry 29:738-743(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1697582; DOI=10.1016/s0021-9258(18)77199-8;
RA Ensor C.M., Yang J.Y., Okita R.T., Tai H.-H.;
RT "Cloning and sequence analysis of the cDNA for human placental NAD(+)-
RT dependent 15-hydroxyprostaglandin dehydrogenase.";
RL J. Biol. Chem. 265:14888-14891(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Leukemia;
RX PubMed=7557451; DOI=10.1016/0378-1119(95)00319-2;
RA Pichaud F., Frendo J.L., Delage-Mourroux R., de Vernejoul M.C.,
RA Moukhtar M.S., Jullienne A.;
RT "Sequence of a novel mRNA coding for a C-terminal-truncated form of human
RT NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase.";
RL Gene 162:319-322(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=9099873; DOI=10.1016/s0378-1119(96)00800-1;
RA Delage-Mourroux R., Pichaud F., Frendo J.L., Pidoux E., Guliana J.M.,
RA Moukhtar M.S., Jullienne A.;
RT "Cloning and sequencing of a new 15-hydroxyprostaglandin dehydrogenase
RT related mRNA.";
RL Gene 188:143-148(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5).
RC TISSUE=Colon, Placenta, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [10]
RP MUTAGENESIS OF TYR-151.
RX PubMed=2025296; DOI=10.1016/s0006-291x(05)80262-1;
RA Ensor C.M., Tai H.-H.;
RT "Site-directed mutagenesis of the conserved tyrosine 151 of human placental
RT NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a
RT catalytically inactive enzyme.";
RL Biochem. Biophys. Res. Commun. 176:840-845(1991).
RN [11]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-151 AND LYS-155.
RX PubMed=8086429; DOI=10.1016/0167-4838(94)90172-4;
RA Ensor C.M., Tai H.H.;
RT "Bacterial expression and site-directed mutagenesis of two critical
RT residues (tyrosine-151 and lysine-155) of human placental NAD(+)-dependent
RT 15-hydroxyprostaglandin dehydrogenase.";
RL Biochim. Biophys. Acta 1208:151-156(1994).
RN [12]
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 [13]
RP INDUCTION.
RX PubMed=12788907; DOI=10.1210/jc.2002-021710;
RA Patel F.A., Funder J.W., Challis J.R.G.;
RT "Mechanism of cortisol/progesterone antagonism in the regulation of 15-
RT hydroxyprostaglandin dehydrogenase activity and messenger ribonucleic acid
RT levels in human chorion and placental trophoblast cells at term.";
RL J. Clin. Endocrinol. Metab. 88:2922-2933(2003).
RN [14]
RP CATALYTIC ACTIVITY.
RX PubMed=15044627; DOI=10.1124/mol.65.4.973;
RA Nomura T., Lu R., Pucci M.L., Schuster V.L.;
RT "The two-step model of prostaglandin signal termination: in vitro
RT reconstitution with the prostaglandin transporter and prostaglandin 15
RT dehydrogenase.";
RL Mol. Pharmacol. 65:973-978(2004).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15574495; DOI=10.1073/pnas.0406142101;
RA Yan M., Rerko R.M., Platzer P., Dawson D., Willis J., Tong M., Lawrence E.,
RA Lutterbaugh J., Lu S., Willson J.K.V., Luo G., Hensold J., Tai H.-H.,
RA Wilson K., Markowitz S.D.;
RT "15-Hydroxyprostaglandin dehydrogenase, a COX-2 oncogene antagonist, is a
RT TGF-beta-induced suppressor of human gastrointestinal cancers.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17468-17473(2004).
RN [16]
RP FUNCTION, MUTAGENESIS OF GLN-148, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND 3D-STRUCTURE MODELING.
RX PubMed=16828555; DOI=10.1016/j.bmc.2006.06.030;
RA Cho H., Huang L., Hamza A., Gao D., Zhan C.-G., Tai H.-H.;
RT "Role of glutamine 148 of human 15-hydroxyprostaglandin dehydrogenase in
RT catalytic oxidation of prostaglandin E2.";
RL Bioorg. Med. Chem. 14:6486-6491(2006).
RN [17]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=16757471; DOI=10.1074/jbc.m603766200;
RA Arita M., Oh S.F., Chonan T., Hong S., Elangovan S., Sun Y.P., Uddin J.,
RA Petasis N.A., Serhan C.N.;
RT "Metabolic inactivation of resolvin E1 and stabilization of its anti-
RT inflammatory actions.";
RL J. Biol. Chem. 281:22847-22854(2006).
RN [18]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21916491; DOI=10.1021/tx200336f;
RA Liu X., Zhang S., Arora J.S., Snyder N.W., Shah S.J., Blair I.A.;
RT "11-Oxoeicosatetraenoic acid is a cyclooxygenase-2/15-hydroxyprostaglandin
RT dehydrogenase-derived antiproliferative eicosanoid.";
RL Chem. Res. Toxicol. 24:2227-2236(2011).
RN [19]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=22844113; DOI=10.4049/jimmunol.1201272;
RA Claria J., Dalli J., Yacoubian S., Gao F., Serhan C.N.;
RT "Resolvin D1 and resolvin D2 govern local inflammatory tone in obese fat.";
RL J. Immunol. 189:2597-2605(2012).
RN [20]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=25586183; DOI=10.1074/jbc.m114.635151;
RA Wendell S.G., Golin-Bisello F., Wenzel S., Sobol R.W., Holguin F.,
RA Freeman B.A.;
RT "15-Hydroxyprostaglandin dehydrogenase generation of electrophilic lipid
RT signaling mediators from hydroxy omega-3 fatty acids.";
RL J. Biol. Chem. 290:5868-5880(2015).
RN [21]
RP 3D-STRUCTURE MODELING.
RX PubMed=8482380; DOI=10.1016/0014-5793(93)81554-d;
RA Krook M., Ghosh D., Duax W.L., Joernvall H.;
RT "Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin
RT dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl
RT reductase).";
RL FEBS Lett. 322:139-142(1993).
RN [22]
RP INVOLVEMENT IN PHOAR1, VARIANT COA PRO-140, AND CHARACTERIZATION OF VARIANT
RP COA PRO-140.
RX PubMed=18500342; DOI=10.1038/ng.153;
RA Uppal S., Diggle C.P., Carr I.M., Fishwick C.W.G., Ahmed M., Ibrahim G.H.,
RA Helliwell P.S., Latos-Bielenska A., Phillips S.E.V., Markham A.F.,
RA Bennett C.P., Bonthron D.T.;
RT "Mutations in 15-hydroxyprostaglandin dehydrogenase cause primary
RT hypertrophic osteoarthropathy.";
RL Nat. Genet. 40:789-793(2008).
RN [23]
RP ERRATUM OF PUBMED:18500342.
RA Uppal S., Diggle C.P., Carr I.M., Fishwick C.W.G., Ahmed M., Ibrahim G.H.,
RA Helliwell P.S., Latos-Bielenska A., Phillips S.E.V., Markham A.F.,
RA Bennett C.P., Bonthron D.T.;
RL Nat. Genet. 40:927-927(2008).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 3-256 IN COMPLEX WITH NAD.
RX PubMed=21072165; DOI=10.1371/journal.pone.0013719;
RA Niesen F.H., Schultz L., Jadhav A., Bhatia C., Guo K., Maloney D.J.,
RA Pilka E.S., Wang M., Oppermann U., Heightman T.D., Simeonov A.;
RT "High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin
RT dehydrogenase: mechanisms of inhibition and structure-activity
RT relationships.";
RL PLoS ONE 5:E13719-E13719(2010).
RN [25]
RP VARIANT DIGC PRO-193.
RX PubMed=18805827; DOI=10.1136/jmg.2008.061234;
RA Tariq M., Azeem Z., Ali G., Chishti M.S., Ahmad W.;
RT "Mutation in the HPGD gene encoding NAD+ dependent 15-hydroxyprostaglandin
RT dehydrogenase underlies isolated congenital nail clubbing (ICNC).";
RL J. Med. Genet. 46:14-20(2009).
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
CC (PubMed:8086429, PubMed:10837478, PubMed:16828555, PubMed:16757471,
CC PubMed:21916491, PubMed:25586183). 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 (PubMed:25586183, PubMed:15574495). Converts
CC resolvins E1, D1 and D2 to their oxo products, which represents a mode
CC of resolvin inactivation. Resolvin E1 plays important roles during the
CC resolution phase of acute inflammation, while resolvins D1 and D2 have
CC a unique role in obesity-induced adipose inflammation (PubMed:16757471,
CC PubMed:22844113). {ECO:0000269|PubMed:10837478,
CC ECO:0000269|PubMed:15574495, ECO:0000269|PubMed:16757471,
CC ECO:0000269|PubMed:16828555, ECO:0000269|PubMed:21916491,
CC ECO:0000269|PubMed:22844113, ECO:0000269|PubMed:25586183,
CC ECO:0000269|PubMed:8086429}.
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:0000269|PubMed:15044627,
CC ECO:0000269|PubMed:15574495, ECO:0000269|PubMed:16757471,
CC ECO:0000269|PubMed:16828555, ECO:0000269|PubMed:25586183,
CC ECO:0000269|PubMed:8086429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11877;
CC Evidence={ECO:0000269|PubMed:15574495, ECO:0000269|PubMed:16828555,
CC ECO:0000269|PubMed:25586183};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + 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:0000269|PubMed:21916491};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23261;
CC Evidence={ECO:0000305|PubMed:21916491};
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:0000269|PubMed:21916491};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48641;
CC Evidence={ECO:0000305|PubMed:21916491};
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:0000269|PubMed:10837478};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41573;
CC Evidence={ECO:0000305|PubMed:10837478};
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:0000269|PubMed:10837478};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41597;
CC Evidence={ECO:0000305|PubMed:10837478};
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:0000269|PubMed:8086429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41264;
CC Evidence={ECO:0000305|PubMed:8086429};
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:0000269|PubMed:8086429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16478;
CC Evidence={ECO:0000305|PubMed:8086429};
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:0000269|PubMed:25586183};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48953;
CC Evidence={ECO:0000269|PubMed:25586183};
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:0000269|PubMed:16757471};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49245;
CC Evidence={ECO:0000305|PubMed:16757471};
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:0000269|PubMed:22844113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50125;
CC Evidence={ECO:0000305|PubMed:22844113};
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:0000269|PubMed:22844113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50129;
CC Evidence={ECO:0000305|PubMed:22844113};
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:0000269|PubMed:22844113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53585;
CC Evidence={ECO:0000305|PubMed:22844113};
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:0000269|PubMed:22844113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53589;
CC Evidence={ECO:0000305|PubMed:22844113};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 uM for prostaglandin E2 {ECO:0000269|PubMed:16828555,
CC ECO:0000269|PubMed:8086429};
CC KM=5.5 uM for prostaglandin E1 {ECO:0000269|PubMed:8086429};
CC KM=4.5 uM for prostaglandin A1 {ECO:0000269|PubMed:8086429};
CC KM=22 uM for prostaglandin A2 {ECO:0000269|PubMed:8086429};
CC KM=3.42 uM for (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate
CC {ECO:0000269|PubMed:21916491};
CC KM=1.65 uM for (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate
CC {ECO:0000269|PubMed:21916491};
CC KM=22 uM for NAD in the presence of prostaglandin E1
CC {ECO:0000269|PubMed:8086429};
CC KM=38 uM for NAD in the presence of prostaglandin E2
CC {ECO:0000269|PubMed:16828555};
CC Vmax=296 nmol/min/mg enzyme toward (11R)-hydroxy-(5Z,8Z,12E,14Z)-
CC eicosatetraenoate {ECO:0000269|PubMed:21916491};
CC Vmax=403.8 nmol/min/mg enzyme toward (5Z,8Z,11Z,13E,15S)-
CC hydroxyeicosatetraenoate {ECO:0000269|PubMed:21916491};
CC Vmax=13.1 umol/min/mg enzyme toward prostaglandin A2
CC {ECO:0000269|PubMed:8086429};
CC Vmax=21.58 umol/min/mg enzyme toward prostaglandin A1
CC {ECO:0000269|PubMed:8086429};
CC Vmax=24.98 umol/min/mg enzyme toward NAD in the presence of
CC prostaglandin E1 {ECO:0000269|PubMed:8086429};
CC Vmax=22.8 umol/min/mg enzyme toward prostaglandin E1
CC {ECO:0000269|PubMed:8086429};
CC Vmax=24.6 umol/min/mg enzyme toward prostaglandin E2
CC {ECO:0000269|PubMed:8086429};
CC Note=kcat is 8.6 min(-1) with (11R)-hydroxy-(5Z,8Z,12E,14Z)-
CC eicosatetraenoate and (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate as
CC substrates. {ECO:0000269|PubMed:21916491};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21072165}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P15428-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15428-2; Sequence=VSP_043032;
CC Name=3;
CC IsoId=P15428-3; Sequence=VSP_045106;
CC Name=4;
CC IsoId=P15428-4; Sequence=VSP_045107, VSP_045108;
CC Name=5;
CC IsoId=P15428-5; Sequence=VSP_045579;
CC -!- TISSUE SPECIFICITY: Detected in colon epithelium (at protein level).
CC {ECO:0000269|PubMed:15574495}.
CC -!- INDUCTION: Down-regulated by cortisol, dexamethasone and betamethasone.
CC Down-regulated in colon cancer. Up-regulated by TGFB1.
CC {ECO:0000269|PubMed:12788907, ECO:0000269|PubMed:15574495}.
CC -!- DISEASE: Hypertrophic osteoarthropathy, primary, autosomal recessive, 1
CC (PHOAR1) [MIM:259100]: A disease characterized by digital clubbing,
CC periostosis, acroosteolysis, painful joint enlargement, and variable
CC features of pachydermia that include thickened facial skin and a
CC thickened scalp. Other developmental anomalies include delayed closure
CC of the cranial sutures and congenital heart disease.
CC {ECO:0000269|PubMed:18500342}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cranioosteoarthropathy (COA) [MIM:259100]: A form of
CC osteoarthropathy characterized by swelling of the joints, digital
CC clubbing, hyperhidrosis, delayed closure of the fontanels, periostosis,
CC and variable patent ductus arteriosus. Pachydermia is not a prominent
CC feature. {ECO:0000269|PubMed:18500342}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Digital clubbing, isolated congenital (DIGC) [MIM:119900]: A
CC rare genodermatosis characterized by enlargement of the nail plate and
CC terminal segments of the fingers and toes, resulting from proliferation
CC of the connective tissues between the nail matrix and the distal
CC phalanx. It is usually symmetrical and bilateral (in some cases
CC unilateral). In nail clubbing usually the distal end of the nail matrix
CC is relatively high compared to the proximal end, while the nail plate
CC is complete but its dimensions and diameter more or less vary in
CC comparison to normal. There may be different fingers and toes involved
CC to varying degrees. Some fingers or toes are spared, but the thumbs are
CC almost always involved. {ECO:0000269|PubMed:18805827}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/hpgd/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L76465; AAA89175.1; -; mRNA.
DR EMBL; J05594; AAA89174.1; -; mRNA.
DR EMBL; X82460; CAA57843.1; -; mRNA.
DR EMBL; U63296; AAB53034.1; -; mRNA.
DR EMBL; AK296642; BAH12408.1; -; mRNA.
DR EMBL; AK300125; BAG61916.1; -; mRNA.
DR EMBL; AK300524; BAG62236.1; -; mRNA.
DR EMBL; AK300940; BAG62569.1; -; mRNA.
DR EMBL; AK314624; BAG37190.1; -; mRNA.
DR EMBL; DQ903072; ABI75347.1; -; Genomic_DNA.
DR EMBL; AC096751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04734.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04735.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04736.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04737.1; -; Genomic_DNA.
DR EMBL; BC018986; AAH18986.1; -; mRNA.
DR CCDS; CCDS3821.1; -. [P15428-1]
DR CCDS; CCDS54821.1; -. [P15428-2]
DR CCDS; CCDS58933.1; -. [P15428-3]
DR CCDS; CCDS58934.1; -. [P15428-5]
DR CCDS; CCDS58935.1; -. [P15428-4]
DR PIR; A35802; A35802.
DR RefSeq; NP_000851.2; NM_000860.5. [P15428-1]
DR RefSeq; NP_001139288.1; NM_001145816.2. [P15428-2]
DR RefSeq; NP_001243230.1; NM_001256301.1. [P15428-3]
DR RefSeq; NP_001243234.1; NM_001256305.1. [P15428-4]
DR RefSeq; NP_001243235.1; NM_001256306.1. [P15428-5]
DR RefSeq; NP_001243236.1; NM_001256307.1. [P15428-3]
DR PDB; 2GDZ; X-ray; 1.65 A; A=3-256.
DR PDBsum; 2GDZ; -.
DR AlphaFoldDB; P15428; -.
DR SMR; P15428; -.
DR BioGRID; 109485; 12.
DR STRING; 9606.ENSP00000296522; -.
DR BindingDB; P15428; -.
DR ChEMBL; CHEMBL1293255; -.
DR DrugBank; DB00157; NADH.
DR GuidetoPHARMACOLOGY; 1384; -.
DR SwissLipids; SLP:000000732; -.
DR iPTMnet; P15428; -.
DR PhosphoSitePlus; P15428; -.
DR BioMuta; HPGD; -.
DR DMDM; 129889; -.
DR SWISS-2DPAGE; P15428; -.
DR EPD; P15428; -.
DR jPOST; P15428; -.
DR MassIVE; P15428; -.
DR MaxQB; P15428; -.
DR PaxDb; P15428; -.
DR PeptideAtlas; P15428; -.
DR PRIDE; P15428; -.
DR ProteomicsDB; 18546; -.
DR ProteomicsDB; 48016; -.
DR ProteomicsDB; 5156; -.
DR ProteomicsDB; 53141; -. [P15428-1]
DR ProteomicsDB; 53142; -. [P15428-2]
DR Antibodypedia; 1511; 585 antibodies from 38 providers.
DR DNASU; 3248; -.
DR Ensembl; ENST00000296521.11; ENSP00000296521.7; ENSG00000164120.14. [P15428-2]
DR Ensembl; ENST00000296522.11; ENSP00000296522.6; ENSG00000164120.14. [P15428-1]
DR Ensembl; ENST00000422112.6; ENSP00000398720.2; ENSG00000164120.14. [P15428-5]
DR Ensembl; ENST00000510901.5; ENSP00000422418.1; ENSG00000164120.14. [P15428-3]
DR Ensembl; ENST00000541923.5; ENSP00000438017.1; ENSG00000164120.14. [P15428-3]
DR Ensembl; ENST00000542498.5; ENSP00000443644.1; ENSG00000164120.14. [P15428-4]
DR GeneID; 3248; -.
DR KEGG; hsa:3248; -.
DR MANE-Select; ENST00000296522.11; ENSP00000296522.6; NM_000860.6; NP_000851.2.
DR UCSC; uc003itu.3; human. [P15428-1]
DR CTD; 3248; -.
DR DisGeNET; 3248; -.
DR GeneCards; HPGD; -.
DR HGNC; HGNC:5154; HPGD.
DR HPA; ENSG00000164120; Tissue enhanced (stomach, urinary bladder).
DR MalaCards; HPGD; -.
DR MIM; 119900; phenotype.
DR MIM; 259100; phenotype.
DR MIM; 601688; gene.
DR neXtProt; NX_P15428; -.
DR OpenTargets; ENSG00000164120; -.
DR Orphanet; 1525; Cranio-osteoarthropathy.
DR Orphanet; 217059; Isolated congenital digital clubbing.
DR Orphanet; 2796; Pachydermoperiostosis.
DR PharmGKB; PA29424; -.
DR VEuPathDB; HostDB:ENSG00000164120; -.
DR eggNOG; KOG4169; Eukaryota.
DR GeneTree; ENSGT00940000154593; -.
DR HOGENOM; CLU_010194_2_19_1; -.
DR InParanoid; P15428; -.
DR OMA; QGIHFQN; -.
DR OrthoDB; 1053465at2759; -.
DR PhylomeDB; P15428; -.
DR TreeFam; TF324093; -.
DR BioCyc; MetaCyc:HS09021-MON; -.
DR BRENDA; 1.1.1.141; 2681.
DR BRENDA; 1.3.1.48; 2681.
DR PathwayCommons; P15428; -.
DR Reactome; R-HSA-2142700; Synthesis of Lipoxins (LX).
DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-HSA-9018676; Biosynthesis of D-series resolvins.
DR Reactome; R-HSA-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR SABIO-RK; P15428; -.
DR SignaLink; P15428; -.
DR SIGNOR; P15428; -.
DR BioGRID-ORCS; 3248; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; HPGD; human.
DR EvolutionaryTrace; P15428; -.
DR GeneWiki; HPGD; -.
DR GenomeRNAi; 3248; -.
DR Pharos; P15428; Tchem.
DR PRO; PR:P15428; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P15428; protein.
DR Bgee; ENSG00000164120; Expressed in adrenal tissue and 155 other tissues.
DR ExpressionAtlas; P15428; baseline and differential.
DR Genevisible; P15428; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016404; F:15-hydroxyprostaglandin dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0004957; F:prostaglandin E receptor activity; IDA:UniProtKB.
DR GO; GO:0097070; P:ductus arteriosus closure; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IDA:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0019372; P:lipoxygenase pathway; TAS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0030728; P:ovulation; ISS:UniProtKB.
DR GO; GO:0007567; P:parturition; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR GO; GO:1905828; P:regulation of prostaglandin catabolic process; IMP:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
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; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Disease variant; Fatty acid metabolism; Lipid metabolism; NAD;
KW Oxidoreductase; Prostaglandin metabolism; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..266
FT /note="15-hydroxyprostaglandin dehydrogenase [NAD(+)]"
FT /id="PRO_0000054744"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT BINDING 12..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21072165"
FT BINDING 36..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21072165"
FT BINDING 63..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21072165"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21072165"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 151..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21072165"
FT BINDING 186..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21072165"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045106"
FT VAR_SEQ 73..140
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045579"
FT VAR_SEQ 140..143
FT /note="AGLM -> AAHH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9099873"
FT /id="VSP_045107"
FT VAR_SEQ 144..266
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9099873"
FT /id="VSP_045108"
FT VAR_SEQ 167..266
FT /note="LAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYG
FT ILDPPLIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFQAKTQ -> PTIDCQW
FT IDNTH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7557451"
FT /id="VSP_043032"
FT VARIANT 140
FT /note="A -> P (in COA; inactive; dbSNP:rs121434480)"
FT /evidence="ECO:0000269|PubMed:18500342"
FT /id="VAR_046209"
FT VARIANT 193
FT /note="S -> P (in DIGC; dbSNP:rs121434481)"
FT /evidence="ECO:0000269|PubMed:18805827"
FT /id="VAR_060792"
FT VARIANT 217
FT /note="Y -> C (in dbSNP:rs140209262)"
FT /id="VAR_006972"
FT MUTAGEN 148
FT /note="Q->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16828555"
FT MUTAGEN 148
FT /note="Q->E,H,N: Reduced affinity for NAD and prostaglandin
FT E2."
FT /evidence="ECO:0000269|PubMed:16828555"
FT MUTAGEN 151
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2025296"
FT MUTAGEN 151
FT /note="Y->F: Loss 15-hydroxyprostaglandin dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:8086429"
FT MUTAGEN 155
FT /note="K->Q: Loss 15-hydroxyprostaglandin dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:8086429"
FT CONFLICT 50
FT /note="D -> H (in Ref. 2; AAA89175/AAA89174)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="E -> K (in Ref. 3; CAA57843)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="I -> V (in Ref. 5; BAG61916)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2GDZ"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:2GDZ"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 149..172
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:2GDZ"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:2GDZ"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2GDZ"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:2GDZ"
SQ SEQUENCE 266 AA; 28977 MW; B860D2DE80E49514 CRC64;
MHVNGKVALV TGAAQGIGRA FAEALLLKGA KVALVDWNLE AGVQCKAALD EQFEPQKTLF
IQCDVADQQQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW EKTLQINLVS VISGTYLGLD
YMSKQNGGEG GIIINMSSLA GLMPVAQQPV YCASKHGIVG FTRSAALAAN LMNSGVRLNA
ICPGFVNTAI LESIEKEENM GQYIEYKDHI KDMIKYYGIL DPPLIANGLI TLIEDDALNG
AIMKITTSKG IHFQDYDTTP FQAKTQ
