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15-hydroxyprostaglandin dehydrogenase [NAD( )] (15-PGDH) (EC 1.1.1.141) (Prostaglandin dehydrogenase 1) (Short chain dehydrogenase/reductase family 36C member 1)

 PGDH_HUMAN              Reviewed;         266 AA.
P15428; B4DTA4; B4DU74; B4DV57; D3DP43; E7EV11; O00749; Q06F08;
Q12998;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
28-MAR-2018, entry version 185.
RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)];
Short=15-PGDH;
EC=1.1.1.141;
AltName: Full=Prostaglandin dehydrogenase 1;
AltName: Full=Short chain dehydrogenase/reductase family 36C member 1;
Name=HPGD; Synonyms=PGDH1, SDR36C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE.
TISSUE=Placenta;
PubMed=2337593; DOI=10.1021/bi00455a021;
Krook M., Marekov L., Joernvall H.;
"Purification and structural characterization of placental NAD(+)-
linked 15-hydroxyprostaglandin dehydrogenase. The primary structure
reveals the enzyme to belong to the short-chain alcohol dehydrogenase
family.";
Biochemistry 29:738-743(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=1697582;
Ensor C.M., Yang J.Y., Okita R.T., Tai H.-H.;
"Cloning and sequence analysis of the cDNA for human placental NAD(+)-
dependent 15-hydroxyprostaglandin dehydrogenase.";
J. Biol. Chem. 265:14888-14891(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Leukemia;
PubMed=7557451; DOI=10.1016/0378-1119(95)00319-2;
Pichaud F., Frendo J.L., Delage-Mourroux R., de Vernejoul M.C.,
Moukhtar M.S., Jullienne A.;
"Sequence of a novel mRNA coding for a C-terminal-truncated form of
human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase.";
Gene 162:319-322(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=9099873; DOI=10.1016/S0378-1119(96)00800-1;
Delage-Mourroux R., Pichaud F., Frendo J.L., Pidoux E., Guliana J.M.,
Moukhtar M.S., Jullienne A.;
"Cloning and sequencing of a new 15-hydroxyprostaglandin dehydrogenase
related mRNA.";
Gene 188:143-148(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5).
TISSUE=Colon, Placenta, and Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
MUTAGENESIS OF TYR-151.
PubMed=2025296; DOI=10.1016/S0006-291X(05)80262-1;
Ensor C.M., Tai H.-H.;
"Site-directed mutagenesis of the conserved tyrosine 151 of human
placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase
yields a catalytically inactive enzyme.";
Biochem. Biophys. Res. Commun. 176:840-845(1991).
[11]
FUNCTION.
PubMed=10837478; DOI=10.1074/jbc.M002863200;
Clish C.B., Levy B.D., Chiang N., Tai H.-H., Serhan C.N.;
"Oxidoreductases in lipoxin A4 metabolic inactivation: a novel role
for 15-onoprostaglandin 13-reductase/leukotriene B4 12-
hydroxydehydrogenase in inflammation.";
J. Biol. Chem. 275:25372-25380(2000).
[12]
INDUCTION.
PubMed=12788907; DOI=10.1210/jc.2002-021710;
Patel F.A., Funder J.W., Challis J.R.G.;
"Mechanism of cortisol/progesterone antagonism in the regulation of
15-hydroxyprostaglandin dehydrogenase activity and messenger
ribonucleic acid levels in human chorion and placental trophoblast
cells at term.";
J. Clin. Endocrinol. Metab. 88:2922-2933(2003).
[13]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=15574495; DOI=10.1073/pnas.0406142101;
Yan M., Rerko R.M., Platzer P., Dawson D., Willis J., Tong M.,
Lawrence E., Lutterbaugh J., Lu S., Willson J.K.V., Luo G.,
Hensold J., Tai H.-H., Wilson K., Markowitz S.D.;
"15-Hydroxyprostaglandin dehydrogenase, a COX-2 oncogene antagonist,
is a TGF-beta-induced suppressor of human gastrointestinal cancers.";
Proc. Natl. Acad. Sci. U.S.A. 101:17468-17473(2004).
[14]
FUNCTION, MUTAGENESIS OF GLN-148, BIOPHYSICOCHEMICAL PROPERTIES, AND
3D-STRUCTURE MODELING.
PubMed=16828555; DOI=10.1016/j.bmc.2006.06.030;
Cho H., Huang L., Hamza A., Gao D., Zhan C.-G., Tai H.-H.;
"Role of glutamine 148 of human 15-hydroxyprostaglandin dehydrogenase
in catalytic oxidation of prostaglandin E2.";
Bioorg. Med. Chem. 14:6486-6491(2006).
[15]
3D-STRUCTURE MODELING.
PubMed=8482380; DOI=10.1016/0014-5793(93)81554-D;
Krook M., Ghosh D., Duax W.L., Joernvall H.;
"Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin
dehydrogenase and relationships to the NADP(+)-dependent enzyme
(carbonyl reductase).";
FEBS Lett. 322:139-142(1993).
[16]
INVOLVEMENT IN PHOAR1, VARIANT COA PRO-140, AND CHARACTERIZATION OF
VARIANT COA PRO-140.
PubMed=18500342; DOI=10.1038/ng.153;
Uppal S., Diggle C.P., Carr I.M., Fishwick C.W.G., Ahmed M.,
Ibrahim G.H., Helliwell P.S., Latos-Bielenska A., Phillips S.E.V.,
Markham A.F., Bennett C.P., Bonthron D.T.;
"Mutations in 15-hydroxyprostaglandin dehydrogenase cause primary
hypertrophic osteoarthropathy.";
Nat. Genet. 40:789-793(2008).
[17]
ERRATUM.
Uppal S., Diggle C.P., Carr I.M., Fishwick C.W.G., Ahmed M.,
Ibrahim G.H., Helliwell P.S., Latos-Bielenska A., Phillips S.E.V.,
Markham A.F., Bennett C.P., Bonthron D.T.;
Nat. Genet. 40:927-927(2008).
[18]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 3-256 IN COMPLEX WITH NAD.
PubMed=21072165; DOI=10.1371/journal.pone.0013719;
Niesen F.H., Schultz L., Jadhav A., Bhatia C., Guo K., Maloney D.J.,
Pilka E.S., Wang M., Oppermann U., Heightman T.D., Simeonov A.;
"High-affinity inhibitors of human NAD-dependent 15-
hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and
structure-activity relationships.";
PLoS ONE 5:E13719-E13719(2010).
[19]
VARIANT ICNC PRO-193.
PubMed=18805827; DOI=10.1136/jmg.2008.061234;
Tariq M., Azeem Z., Ali G., Chishti M.S., Ahmad W.;
"Mutation in the HPGD gene encoding NAD+ dependent 15-
hydroxyprostaglandin dehydrogenase underlies isolated congenital nail
clubbing (ICNC).";
J. Med. Genet. 46:14-20(2009).
-!- FUNCTION: Prostaglandin inactivation. Contributes to the
regulation of events that are under the control of prostaglandin
levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4
to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon
cancer cells. {ECO:0000269|PubMed:10837478,
ECO:0000269|PubMed:15574495, ECO:0000269|PubMed:16828555}.
-!- CATALYTIC ACTIVITY: (5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-
5,13-dienoate + NAD(+) = (5Z,13E)-11-alpha-hydroxy-9,15-
dioxoprost-5,13-dienoate + NADH.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.4 uM for prostaglandin E2 {ECO:0000269|PubMed:16828555};
KM=38 uM for NAD {ECO:0000269|PubMed:16828555};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21072165}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P15428-1; Sequence=Displayed;
Name=2;
IsoId=P15428-2; Sequence=VSP_043032;
Name=3;
IsoId=P15428-3; Sequence=VSP_045106;
Name=4;
IsoId=P15428-4; Sequence=VSP_045107, VSP_045108;
Name=5;
IsoId=P15428-5; Sequence=VSP_045579;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in colon epithelium (at protein
level). {ECO:0000269|PubMed:15574495}.
-!- INDUCTION: Down-regulated by cortisol, dexamethasone and
betamethasone. Down-regulated in colon cancer. Up-regulated by
TGFB1. {ECO:0000269|PubMed:12788907, ECO:0000269|PubMed:15574495}.
-!- DISEASE: Hypertrophic osteoarthropathy, primary, autosomal
recessive, 1 (PHOAR1) [MIM:259100]: A disease characterized by
digital clubbing, periostosis, acroosteolysis, painful joint
enlargement, and variable features of pachydermia that include
thickened facial skin and a thickened scalp. Other developmental
anomalies include delayed closure of the cranial sutures and
congenital heart disease. {ECO:0000269|PubMed:18500342}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cranioosteoarthropathy (COA) [MIM:259100]: A form of
osteoarthropathy characterized by swelling of the joints, digital
clubbing, hyperhidrosis, delayed closure of the fontanels,
periostosis, and variable patent ductus arteriosus. Pachydermia is
not a prominent feature. {ECO:0000269|PubMed:18500342}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Isolated congenital nail clubbing (ICNC) [MIM:119900]: A
rare genodermatosis characterized by enlargement of the nail plate
and terminal segments of the fingers and toes, resulting from
proliferation of the connective tissues between the nail matrix
and the distal phalanx. It is usually symmetrical and bilateral
(in some cases unilateral). In nail clubbing usually the distal
end of the nail matrix is relatively high compared to the proximal
end, while the nail plate is complete but its dimensions and
diameter more or less vary in comparison to normal. There may be
different fingers and toes involved to varying degrees. Some
fingers or toes are spared, but the thumbs are almost always
involved. {ECO:0000269|PubMed:18805827}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/hpgd/";
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EMBL; L76465; AAA89175.1; -; mRNA.
EMBL; J05594; AAA89174.1; -; mRNA.
EMBL; X82460; CAA57843.1; -; mRNA.
EMBL; U63296; AAB53034.1; -; mRNA.
EMBL; AK296642; BAH12408.1; -; mRNA.
EMBL; AK300125; BAG61916.1; -; mRNA.
EMBL; AK300524; BAG62236.1; -; mRNA.
EMBL; AK300940; BAG62569.1; -; mRNA.
EMBL; AK314624; BAG37190.1; -; mRNA.
EMBL; DQ903072; ABI75347.1; -; Genomic_DNA.
EMBL; AC096751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX04734.1; -; Genomic_DNA.
EMBL; CH471056; EAX04735.1; -; Genomic_DNA.
EMBL; CH471056; EAX04736.1; -; Genomic_DNA.
EMBL; CH471056; EAX04737.1; -; Genomic_DNA.
EMBL; BC018986; AAH18986.1; -; mRNA.
CCDS; CCDS3821.1; -. [P15428-1]
CCDS; CCDS54821.1; -. [P15428-2]
CCDS; CCDS58933.1; -. [P15428-3]
CCDS; CCDS58934.1; -. [P15428-5]
CCDS; CCDS58935.1; -. [P15428-4]
PIR; A35802; A35802.
RefSeq; NP_000851.2; NM_000860.5. [P15428-1]
RefSeq; NP_001139288.1; NM_001145816.2. [P15428-2]
RefSeq; NP_001243230.1; NM_001256301.1. [P15428-3]
RefSeq; NP_001243234.1; NM_001256305.1. [P15428-4]
RefSeq; NP_001243235.1; NM_001256306.1. [P15428-5]
RefSeq; NP_001243236.1; NM_001256307.1. [P15428-3]
UniGene; Hs.596913; -.
PDB; 2GDZ; X-ray; 1.65 A; A=3-256.
PDBsum; 2GDZ; -.
ProteinModelPortal; P15428; -.
SMR; P15428; -.
BioGrid; 109485; 1.
STRING; 9606.ENSP00000296522; -.
BindingDB; P15428; -.
ChEMBL; CHEMBL1293255; -.
DrugBank; DB00157; NADH.
GuidetoPHARMACOLOGY; 1384; -.
SwissLipids; SLP:000000732; -.
iPTMnet; P15428; -.
PhosphoSitePlus; P15428; -.
BioMuta; HPGD; -.
DMDM; 129889; -.
SWISS-2DPAGE; P15428; -.
EPD; P15428; -.
MaxQB; P15428; -.
PaxDb; P15428; -.
PeptideAtlas; P15428; -.
PRIDE; P15428; -.
Ensembl; ENST00000296521; ENSP00000296521; ENSG00000164120. [P15428-2]
Ensembl; ENST00000296522; ENSP00000296522; ENSG00000164120. [P15428-1]
Ensembl; ENST00000422112; ENSP00000398720; ENSG00000164120. [P15428-5]
Ensembl; ENST00000510901; ENSP00000422418; ENSG00000164120. [P15428-3]
Ensembl; ENST00000541923; ENSP00000438017; ENSG00000164120. [P15428-3]
Ensembl; ENST00000542498; ENSP00000443644; ENSG00000164120. [P15428-4]
GeneID; 3248; -.
KEGG; hsa:3248; -.
UCSC; uc003itu.3; human. [P15428-1]
CTD; 3248; -.
DisGeNET; 3248; -.
EuPathDB; HostDB:ENSG00000164120.13; -.
GeneCards; HPGD; -.
HGNC; HGNC:5154; HPGD.
HPA; HPA004919; -.
HPA; HPA005679; -.
MalaCards; HPGD; -.
MIM; 119900; phenotype.
MIM; 259100; phenotype.
MIM; 601688; gene.
neXtProt; NX_P15428; -.
OpenTargets; ENSG00000164120; -.
Orphanet; 1525; Cranio-osteoarthropathy.
Orphanet; 217059; Isolated congenital digital clubbing.
Orphanet; 2796; Pachydermoperiostosis.
PharmGKB; PA29424; -.
eggNOG; KOG4169; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00910000144076; -.
HOGENOM; HOG000070121; -.
HOVERGEN; HBG107379; -.
InParanoid; P15428; -.
KO; K00069; -.
OMA; SCEVHYS; -.
OrthoDB; EOG091G0OC9; -.
PhylomeDB; P15428; -.
TreeFam; TF324093; -.
BRENDA; 1.1.1.141; 2681.
Reactome; R-HSA-2142700; Synthesis of Lipoxins (LX).
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RK; P15428; -.
SIGNOR; P15428; -.
ChiTaRS; HPGD; human.
EvolutionaryTrace; P15428; -.
GeneWiki; HPGD; -.
GenomeRNAi; 3248; -.
PRO; PR:P15428; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000164120; -.
CleanEx; HS_HPGD; -.
ExpressionAtlas; P15428; baseline and differential.
Genevisible; P15428; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0016404; F:15-hydroxyprostaglandin dehydrogenase (NAD+) activity; IDA:UniProtKB.
GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
GO; GO:0004957; F:prostaglandin E receptor activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0097070; P:ductus arteriosus closure; ISS:UniProtKB.
GO; GO:0007565; P:female pregnancy; IDA:UniProtKB.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:2001301; P:lipoxin biosynthetic process; TAS:Reactome.
GO; GO:0019372; P:lipoxygenase pathway; TAS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
GO; GO:0030728; P:ovulation; ISS:UniProtKB.
GO; GO:0007567; P:parturition; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Fatty acid metabolism;
Lipid metabolism; NAD; Oxidoreductase; Polymorphism;
Prostaglandin metabolism; Reference proteome; Tumor suppressor.
CHAIN 1 266 15-hydroxyprostaglandin dehydrogenase
[NAD(+)].
/FTId=PRO_0000054744.
NP_BIND 12 20 NAD. {ECO:0000269|PubMed:21072165}.
NP_BIND 36 37 NAD. {ECO:0000269|PubMed:21072165}.
NP_BIND 63 65 NAD. {ECO:0000269|PubMed:21072165}.
NP_BIND 151 155 NAD. {ECO:0000269|PubMed:21072165}.
NP_BIND 186 188 NAD. {ECO:0000269|PubMed:21072165}.
ACT_SITE 151 151 Proton acceptor.
BINDING 91 91 NAD; via carbonyl oxygen.
{ECO:0000269|PubMed:21072165}.
BINDING 138 138 Substrate. {ECO:0000305}.
BINDING 148 148 Substrate. {ECO:0000305}.
VAR_SEQ 1 121 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045106.
VAR_SEQ 73 140 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045579.
VAR_SEQ 140 143 AGLM -> AAHH (in isoform 4).
{ECO:0000303|PubMed:9099873}.
/FTId=VSP_045107.
VAR_SEQ 144 266 Missing (in isoform 4).
{ECO:0000303|PubMed:9099873}.
/FTId=VSP_045108.
VAR_SEQ 167 266 LAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYK
DHIKDMIKYYGILDPPLIANGLITLIEDDALNGAIMKITTS
KGIHFQDYDTTPFQAKTQ -> PTIDCQWIDNTH (in
isoform 2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7557451}.
/FTId=VSP_043032.
VARIANT 140 140 A -> P (in COA; inactive;
dbSNP:rs121434480).
{ECO:0000269|PubMed:18500342}.
/FTId=VAR_046209.
VARIANT 193 193 S -> P (in ICNC; dbSNP:rs121434481).
{ECO:0000269|PubMed:18805827}.
/FTId=VAR_060792.
VARIANT 217 217 Y -> C (in dbSNP:rs140209262).
/FTId=VAR_006972.
MUTAGEN 148 148 Q->A: Loss of activity.
{ECO:0000269|PubMed:16828555}.
MUTAGEN 148 148 Q->E,H,N: Reduced affinity for NAD and
prostaglandin E2.
{ECO:0000269|PubMed:16828555}.
MUTAGEN 151 151 Y->A: Loss of activity.
{ECO:0000269|PubMed:2025296}.
CONFLICT 50 50 D -> H (in Ref. 2; AAA89175/AAA89174).
{ECO:0000305}.
CONFLICT 97 97 E -> K (in Ref. 3; CAA57843).
{ECO:0000305}.
CONFLICT 219 219 I -> V (in Ref. 5; BAG61916).
{ECO:0000305}.
STRAND 7 11 {ECO:0000244|PDB:2GDZ}.
TURN 12 14 {ECO:0000244|PDB:2GDZ}.
HELIX 16 27 {ECO:0000244|PDB:2GDZ}.
STRAND 31 37 {ECO:0000244|PDB:2GDZ}.
HELIX 39 49 {ECO:0000244|PDB:2GDZ}.
TURN 50 52 {ECO:0000244|PDB:2GDZ}.
HELIX 55 57 {ECO:0000244|PDB:2GDZ}.
STRAND 58 62 {ECO:0000244|PDB:2GDZ}.
HELIX 68 82 {ECO:0000244|PDB:2GDZ}.
STRAND 87 90 {ECO:0000244|PDB:2GDZ}.
STRAND 97 99 {ECO:0000244|PDB:2GDZ}.
HELIX 100 107 {ECO:0000244|PDB:2GDZ}.
HELIX 109 122 {ECO:0000244|PDB:2GDZ}.
HELIX 124 126 {ECO:0000244|PDB:2GDZ}.
STRAND 131 136 {ECO:0000244|PDB:2GDZ}.
HELIX 139 141 {ECO:0000244|PDB:2GDZ}.
HELIX 149 172 {ECO:0000244|PDB:2GDZ}.
STRAND 176 184 {ECO:0000244|PDB:2GDZ}.
STRAND 186 188 {ECO:0000244|PDB:2GDZ}.
HELIX 189 192 {ECO:0000244|PDB:2GDZ}.
HELIX 193 195 {ECO:0000244|PDB:2GDZ}.
HELIX 197 200 {ECO:0000244|PDB:2GDZ}.
HELIX 201 206 {ECO:0000244|PDB:2GDZ}.
HELIX 207 217 {ECO:0000244|PDB:2GDZ}.
HELIX 222 234 {ECO:0000244|PDB:2GDZ}.
STRAND 242 246 {ECO:0000244|PDB:2GDZ}.
TURN 247 249 {ECO:0000244|PDB:2GDZ}.
STRAND 250 253 {ECO:0000244|PDB:2GDZ}.
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


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