PGDH_BOVIN
ID PGDH_BOVIN Reviewed; 266 AA.
AC Q3T0C2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)];
DE Short=15-PGDH;
DE EC=1.1.1.141 {ECO:0000250|UniProtKB:P15428};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 Decreases the levels of the pro-proliferative prostaglandins such as
CC prostaglandin E2 (whose activity is increased in cancer because of an
CC increase in the expression of cyclooxygenase 2) and generates oxo-fatty
CC acid products that can profoundly influence cell function by abrogating
CC pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2
CC to their oxo products, which represents a mode of resolvin
CC inactivation. Resolvin E1 plays important roles during the resolution
CC phase of acute inflammation, while resolvins D1 and D2 have a unique
CC role in obesity-induced adipose inflammation.
CC {ECO:0000250|UniProtKB:P15428}.
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:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11877;
CC Evidence={ECO:0000250|UniProtKB:P15428};
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: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 -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BC102458; AAI02459.1; -; mRNA.
DR RefSeq; NP_001029591.1; NM_001034419.2.
DR AlphaFoldDB; Q3T0C2; -.
DR SMR; Q3T0C2; -.
DR STRING; 9913.ENSBTAP00000027024; -.
DR PaxDb; Q3T0C2; -.
DR PRIDE; Q3T0C2; -.
DR GeneID; 512259; -.
DR KEGG; bta:512259; -.
DR CTD; 3248; -.
DR eggNOG; KOG4169; Eukaryota.
DR InParanoid; Q3T0C2; -.
DR OrthoDB; 1053465at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016404; F:15-hydroxyprostaglandin dehydrogenase (NAD+) activity; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0004957; F:prostaglandin E receptor activity; ISS:UniProtKB.
DR GO; GO:0097070; P:ductus arteriosus closure; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
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:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR GO; GO:1905828; P:regulation of prostaglandin catabolic process; ISS:UniProtKB.
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 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 2: Evidence at transcript level;
KW Cytoplasm; Fatty acid metabolism; Lipid metabolism; NAD; Oxidoreductase;
KW Prostaglandin metabolism; Reference proteome; Tumor suppressor.
FT CHAIN 1..266
FT /note="15-hydroxyprostaglandin dehydrogenase [NAD(+)]"
FT /id="PRO_0000240130"
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"
SQ SEQUENCE 266 AA; 29026 MW; CC666DC08319DA09 CRC64;
MHVNGKVALV TGAAQGIGRA FAEALLLKGA KVALVDWNLE AGVKCKAALD EQFEPQKTLF
IQCDVADQEQ LRDTFRKVVD HFGKLDILVN NAGVNNEKNW EKTLQINLVS VISGTYLGLD
YMSKQNGGEG GININMSSLA GLMPVAQQPV YCASKHGIVG FTRSAAMAAN LMNSGVRLNA
ICPGFVDTPI LKSIEKEENM GKYIEYMGPI KDMMKYYGIL DPSMIANGLI TLIEDDALNG
AIMKITTSKG IHFQDYDTTP FHMKMQ
