ID   A0A337RXY0_FELCA        Unreviewed;       197 AA.
AC   A0A337RXY0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   05-FEB-2025, entry version 24.
DE   RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)] {ECO:0000256|ARBA:ARBA00040276};
DE            EC=1.1.1.141 {ECO:0000256|ARBA:ARBA00038968};
DE            EC=1.1.1.232 {ECO:0000256|ARBA:ARBA00039060};
DE   AltName: Full=Eicosanoid/docosanoid dehydrogenase [NAD(+)] {ECO:0000256|ARBA:ARBA00042026};
DE   AltName: Full=Prostaglandin dehydrogenase 1 {ECO:0000256|ARBA:ARBA00041812};
GN   Name=HPGD {ECO:0000313|Ensembl:ENSFCAP00000040947.1,
GN   ECO:0000313|VGNC:VGNC:67638};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000040947.1, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000040947.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000040947.1,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000040947.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000040947.1,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000040947.1}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000040947.1};
RG   Ensembl;
RL   Submitted (OCT-2024) to UniProtKB.
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:0000256|ARBA:ARBA00045705}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + NAD(+) = 11-
CC         oxo-(5Z,8Z,12E,14Z)-eicosatetraenoate + NADH + H(+);
CC         Xref=Rhea:RHEA:48640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78836, ChEBI:CHEBI:90697;
CC         Evidence={ECO:0000256|ARBA:ARBA00048144};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48641;
CC         Evidence={ECO:0000256|ARBA:ARBA00048144};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + NAD(+) = 15-
CC         oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + NADH + H(+);
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:0000256|ARBA:ARBA00049151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23261;
CC         Evidence={ECO:0000256|ARBA:ARBA00049151};
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 + NADH + H(+);
CC         Xref=Rhea:RHEA:48952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:90866, ChEBI:CHEBI:90867;
CC         Evidence={ECO:0000256|ARBA:ARBA00048008};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48953;
CC         Evidence={ECO:0000256|ARBA:ARBA00048008};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z)-eicosatrienoate + NADH +
CC         H(+) = (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:0000256|ARBA:ARBA00048140};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41597;
CC         Evidence={ECO:0000256|ARBA:ARBA00048140};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lipoxin A4 + NAD(+) = 15-oxo-(5S,6R)-dihydroxy-
CC         (7E,9E,11Z,13E)-eicosatetraenoate + NADH + H(+);
CC         Xref=Rhea:RHEA:41572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:67026, ChEBI:CHEBI:78311;
CC         Evidence={ECO:0000256|ARBA:ARBA00048535};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41573;
CC         Evidence={ECO:0000256|ARBA:ARBA00048535};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin A1 + NAD(+) = 15-oxo-prostaglandin A1 + NADH +
CC         H(+); Xref=Rhea:RHEA:41263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57398,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:85072;
CC         Evidence={ECO:0000256|ARBA:ARBA00048611};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41264;
CC         Evidence={ECO:0000256|ARBA:ARBA00048611};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin E1 + NAD(+) = 15-oxoprostaglandin E1 + NADH +
CC         H(+); Xref=Rhea:RHEA:16477, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397,
CC         ChEBI:CHEBI:57401, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000256|ARBA:ARBA00047325};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16478;
CC         Evidence={ECO:0000256|ARBA:ARBA00047325};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin E2 + NAD(+) = 15-oxoprostaglandin E2 + NADH +
CC         H(+); 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:0000256|ARBA:ARBA00048739};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11877;
CC         Evidence={ECO:0000256|ARBA:ARBA00048739};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=resolvin D1 + NAD(+) = 17-oxoresolvin D1 + NADH + H(+);
CC         Xref=Rhea:RHEA:50128, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132081;
CC         Evidence={ECO:0000256|ARBA:ARBA00048170};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50129;
CC         Evidence={ECO:0000256|ARBA:ARBA00048170};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=resolvin D1 + NAD(+) = 8-oxoresolvin D1 + NADH + H(+);
CC         Xref=Rhea:RHEA:50124, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132080;
CC         Evidence={ECO:0000256|ARBA:ARBA00047672};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50125;
CC         Evidence={ECO:0000256|ARBA:ARBA00047672};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=resolvin D2 + NAD(+) = 16-oxoresolvin D2 + NADH + H(+);
CC         Xref=Rhea:RHEA:53588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137498;
CC         Evidence={ECO:0000256|ARBA:ARBA00048921};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53589;
CC         Evidence={ECO:0000256|ARBA:ARBA00048921};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=resolvin D2 + NAD(+) = 7-oxoresolvin D2 + NADH + H(+);
CC         Xref=Rhea:RHEA:53584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137497;
CC         Evidence={ECO:0000256|ARBA:ARBA00048393};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53585;
CC         Evidence={ECO:0000256|ARBA:ARBA00048393};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=resolvin E1 + NAD(+) = 18-oxo-resolvin E1 + NADH + H(+);
CC         Xref=Rhea:RHEA:49244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:91000, ChEBI:CHEBI:91001;
CC         Evidence={ECO:0000256|ARBA:ARBA00049188};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49245;
CC         Evidence={ECO:0000256|ARBA:ARBA00049188};
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; AANG04001605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A337RXY0; -.
DR   Ensembl; ENSFCAT00000051520.2; ENSFCAP00000040947.1; ENSFCAG00000004720.5.
DR   VGNC; VGNC:67638; HPGD.
DR   GeneTree; ENSGT00940000154593; -.
DR   Proteomes; UP000011712; Chromosome B1.
DR   Bgee; ENSFCAG00000004720; Expressed in adult mammalian kidney and 10 other cell types or tissues.
DR   GO; GO:0006693; P:prostaglandin metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; 2.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712}.
SQ   SEQUENCE   197 AA;  21527 MW;  3B446FEC2A02AFC5 CRC64;
     MHVNGKVALV TGAAQGIGRA FAEALLHKGA KVALVDWNLE AGVKCKAALD EQFEPQKTLF
     IQCDVADQEQ LRGLMPVAQQ PVYCASKHGI IGFTRSAAMA ANLMNSGVRL NAICPGFVNT
     PILESIEKEE NMGQYIEYKD HIKDMMKFYG ILDPSMIANG LITLIEDALN GAIMKITTSK
     GIHFQDYETT PFHAKTQ
//