DHRS4_PIG
ID DHRS4_PIG Reviewed; 279 AA.
AC Q8WNV7;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Dehydrogenase/reductase SDR family member 4 {ECO:0000303|PubMed:19056333};
DE EC=1.1.1.184 {ECO:0000269|PubMed:12604222, ECO:0000269|PubMed:19056333};
DE EC=1.1.1.300 {ECO:0000305|PubMed:12604222};
DE AltName: Full=NADPH-dependent carbonyl reductase {ECO:0000303|PubMed:12604222};
DE Short=CR {ECO:0000303|PubMed:12604222};
DE Short=PHCR {ECO:0000303|PubMed:12604222};
DE AltName: Full=NADPH-dependent retinol dehydrogenase/reductase {ECO:0000303|PubMed:12604222};
DE Short=NDRD {ECO:0000303|PubMed:12604222};
DE AltName: Full=Peroxisomal carbonyl reductase {ECO:0000303|PubMed:18334214};
DE Short=PerCR {ECO:0000303|PubMed:18334214};
DE AltName: Full=Peroxisomal short-chain alcohol dehydrogenase;
DE Short=PSCD;
DE AltName: Full=Short chain dehydrogenase/reductase family 25C member 2 {ECO:0000250|UniProtKB:Q9BTZ2};
DE Short=Protein SDR25C2 {ECO:0000250|UniProtKB:Q9BTZ2};
GN Name=DHRS4;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-279, PROTEIN SEQUENCE OF 24-33; 104-118;
RP 158-169 AND 235-249, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Heart;
RX PubMed=12604222; DOI=10.1016/s0009-2797(02)00210-7;
RA Usami N., Ishikura S., Abe H., Nagano M., Uebuchi M., Kuniyasu A.,
RA Otagiri M., Nakayama H., Imamura Y., Hara A.;
RT "Cloning, expression and tissue distribution of a tetrameric form of pig
RT carbonyl reductase.";
RL Chem. Biol. Interact. 143:353-361(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NADPH, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND ACTIVE SITE.
RX PubMed=18334214; DOI=10.1016/j.str.2007.12.022;
RA Tanaka N., Aoki K., Ishikura S., Nagano M., Imamura Y., Hara A.,
RA Nakamura K.T.;
RT "Molecular basis for peroxisomal localization of tetrameric carbonyl
RT reductase.";
RL Structure 16:388-397(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND
RP MUTAGENESIS OF PHE-177 AND LEU-180.
RX PubMed=19056333; DOI=10.1016/j.abb.2008.11.014;
RA Endo S., Maeda S., Matsunaga T., Dhagat U., El-Kabbani O., Tanaka N.,
RA Nakamura K.T., Tajima K., Hara A.;
RT "Molecular determinants for the stereospecific reduction of 3-ketosteroids
RT and reactivity towards all-trans-retinal of a short-chain
RT dehydrogenase/reductase (DHRS4).";
RL Arch. Biochem. Biophys. 481:183-190(2009).
CC -!- FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction
CC of a variety of compounds bearing carbonyl groups including
CC ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones
CC and quinones (PubMed:12604222, PubMed:19056333). Reduces all-trans-
CC retinal and 9-cis retinal (Probable). Reduces 3-ketosteroids and benzil
CC into 3alpha-hydroxysteroids and S-benzoin, respectively, in contrast to
CC the stereoselectivity of primates DHRS4s which produce 3beta-
CC hydroxysteroids and R-benzoin (PubMed:19056333). In the reverse
CC reaction, catalyzes the NADP-dependent oxidation of 3alpha-
CC hydroxysteroids and alcohol, but with much lower efficiency
CC (PubMed:19056333). Involved in the metabolism of 3alpha-
CC hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds
CC (PubMed:12604222, PubMed:19056333). {ECO:0000269|PubMed:12604222,
CC ECO:0000269|PubMed:19056333, ECO:0000305|PubMed:12604222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH;
CC Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.184; Evidence={ECO:0000269|PubMed:12604222,
CC ECO:0000269|PubMed:19056333};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259;
CC Evidence={ECO:0000305|PubMed:12604222, ECO:0000305|PubMed:19056333};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha-hydroxy-5beta-pregnan-20-one + NADP(+) = 5beta-pregnan-
CC 3,20-dione + H(+) + NADPH; Xref=Rhea:RHEA:69016, ChEBI:CHEBI:1712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30154, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:19056333};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69017;
CC Evidence={ECO:0000305|PubMed:19056333};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5beta-dihydrotestosterone + H(+) + NADPH = 5beta-androstane-
CC 3alpha,17beta-diol + NADP(+); Xref=Rhea:RHEA:69028, ChEBI:CHEBI:2150,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36714, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:19056333};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69029;
CC Evidence={ECO:0000305|PubMed:19056333};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300; Evidence={ECO:0000269|PubMed:12604222};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25035;
CC Evidence={ECO:0000305|PubMed:12604222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + isatin + NADPH = 3-hydroxyindolin-2-one + NADP(+);
CC Xref=Rhea:RHEA:68608, ChEBI:CHEBI:15378, ChEBI:CHEBI:27539,
CC ChEBI:CHEBI:28536, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000305|PubMed:12604222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68609;
CC Evidence={ECO:0000305|PubMed:12604222};
CC -!- ACTIVITY REGULATION: Inhibited by kaempferol, quercetin, genistein and
CC myristic acid. {ECO:0000269|PubMed:12604222}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.086 mM for 16-Ketoestrone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.017 mM for 16-Ketoestrone (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.003 mM for all-trans-Retinal (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.032 mM for 9-cis-retinal (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.03 mM for isatin (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.005 mM for isatin (at pH7.4) {ECO:0000269|PubMed:12604222};
CC KM=0.89 mM for Propiophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.028 mM for Heptanophenone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.031 mM for Nonanophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.09 mM for 4-Hexanoylpyridine (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.021 mM for Hexanophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.052 mM for Valerophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.17 mM for n-Butyrophenone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.76 mM for 3-Benzoylpyridine (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.29 mM for 4-Benzoylpyridine (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.47 mM for 2,3-Hexanedione (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.04 mM for 1-phenyl-1,2-propanedione (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.13 mM for Benzil (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=4.5 mM for Diacetyl (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=1.4 mM for Pyridine-4-aldehyde (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.004 mM for 1-Phenylisatin (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.002 mM for 9,10-Phenanthrenequinone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.001 mM for 9,10-Phenanthrenequinone (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.29 mM for Menadione (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.35 mM for S-(-)-1-Phenyl-1-butanol (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=1.2 mM for R-(+)-1-Phenyl-1-butanol (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.029 mM for all-trans-Retinol (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.0027 mM for 5alpha-Pregnane-3,20-dione (at pH7.4)
CC {ECO:0000269|PubMed:19056333};
CC KM=0.033 mM for 5beta-Pregnane-3,20-dione(at pH7.4)
CC {ECO:0000269|PubMed:19056333};
CC KM=0.024 mM for 5beta-Androstan-17b-ol-3-one (at pH7.4)
CC {ECO:0000269|PubMed:19056333};
CC KM=0.052 mM for Dehydrolithocholic acid (at pH7.4)
CC {ECO:0000269|PubMed:19056333};
CC KM=0.26 mM for Dimethyl-2-oxoglutarate (at pH6)
CC {ECO:0000269|PubMed:19056333};
CC KM=0.031 mM for Benzil (at pH6) {ECO:0000269|PubMed:19056333};
CC KM=1.5 mM for 2,3-Pentanedione (at pH6)
CC {ECO:0000269|PubMed:19056333};
CC KM=0.021 mM for Methyl benzoylformate (at pH6)
CC {ECO:0000269|PubMed:19056333};
CC KM=0.2 mM for 4-Nitrobenzaldehyde (at pH6)
CC {ECO:0000269|PubMed:19056333};
CC Vmax=23.3 umol/min/mg enzyme with 16-Ketoestrone as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=3.7 umol/min/mg enzyme with 16-Ketoestrone as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=1.7 umol/min/mg enzyme with all-trans-Retinal as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=2.8 umol/min/mg enzyme with 9-cis-retinal as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=36.5 umol/min/mg enzyme with isatin as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=4.5 umol/min/mg enzyme with isatin as substrate (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=3 umol/min/mg enzyme with Propiophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=6.3 umol/min/mg enzyme with Heptanophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=5 umol/min/mg enzyme with Nonanophenoneas substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=29.9 umol/min/mg enzyme with 4-Hexanoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=10.2 umol/min/mg enzyme with Hexanophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=9.3 umol/min/mg enzyme with Valerophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=11.6 umol/min/mg enzyme with n-Butyrophenone as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=16.2 umol/min/mg enzyme with 3-benzoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=30.2 umol/min/mg enzyme with 4-Benzoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=22.6 umol/min/mg enzyme with 2,3-Hexanedione as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=43.5 umol/min/mg enzyme with 1-phenyl-1,2-propanedione as
CC substrate (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=36.5 umol/min/mg enzyme for the reduction of Benzil into S-
CC benzoin (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=28.8 umol/min/mg enzyme with Diacetyl as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=24.9 umol/min/mg enzyme with Pyridine-4-aldehyde as substrate
CC (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=39.2 umol/min/mg enzyme with 1-Phenylisatin as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=39.2 umol/min/mg enzyme with 9,10-Phenanthrenequinone as
CC substrate (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=3.9 umol/min/mg enzyme with 9,10-Phenanthrenequinone as
CC substrate (at pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=8.7 umol/min/mg enzyme with Menadione as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=3.3 umol/min/mg enzyme with S-(-)-1-Phenyl-1-butanol as
CC substrate (at pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=0.13 umol/min/mg enzyme with R-(+)-1-Phenyl-1-butanol as
CC substrate (at pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=0.29 umol/min/mg enzyme with all-trans-Retinol as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Note=kcat is 45 min(-1) with all-trans-Retinal as substrate (at
CC pH7.4) (PubMed:12604222). kcat is 990 min(-1) with isatin as
CC substrate (at pH6) (PubMed:12604222). kcat is 1180 min(-1) with 1-
CC phenyl-1,2-propanedione as substrate (at pH6) (PubMed:12604222). kcat
CC is 780 min(-1) with Diacetyl as substrate (at pH6) (PubMed:12604222).
CC kcat is 650 min(-1) with Pyridine-4-aldehyde as substrate (at pH6)
CC (PubMed:12604222). kcat is 1.5 min(-1) with 5beta-Pregnane-3,20-dione
CC as substrate (at pH7.4) (PubMed:19056333). kcat is 3.7 min(-1) with
CC 5beta-Pregnane-3,20-dione as substrate (at pH7.4) (PubMed:19056333).
CC kcat is 4.6 min(-1) with 5beta-Androstan-17beta-ol-3-one as substrate
CC (at pH7.4) (PubMed:19056333). kcat is 16 min(-1) with
CC Dehydrolithocholic acid as substrate (at pH7.4) (PubMed:19056333).
CC kcat is 814 min(-1) with Dimethyl-2-oxoglutarate as substrate (at
CC pH6) (PubMed:19056333). kcat is 920 min(-1) with Benzil as substrate
CC (at pH6) (PubMed:19056333). kcat is 650 min(-1) with 2,3-Pentanedione
CC as substrate (at pH6) (PubMed:19056333). kcat is 1200 min(-1) with
CC Methyl benzoylformate as substrate (at pH6) (PubMed:19056333). kcat
CC is 890 min(-1) with 4-Nitrobenzaldehyde as substrate (at pH6)
CC (PubMed:19056333). kcat is 0.02 min(-1) with 5beta-Pregnan-3alpha-ol-
CC 20-one as substrate (at pH6) (PubMed:19056333). kcat is 0.04 min(-1)
CC with 5beta-Androstane-3alpha,17beta-diol as substrate (at pH6)
CC (PubMed:19056333). kcat is 0.06 min(-1) with Lithocholic acid as
CC substrate (at pH6) (PubMed:19056333). {ECO:0000269|PubMed:12604222,
CC ECO:0000269|PubMed:19056333};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12604222,
CC ECO:0000269|PubMed:18334214}.
CC -!- INTERACTION:
CC Q8WNV7; Q8WNV7: DHRS4; NbExp=2; IntAct=EBI-15692152, EBI-15692152;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12604222,
CC ECO:0000269|PubMed:18334214}.
CC -!- TISSUE SPECIFICITY: Detected in heart, kidney, liver and small
CC intestine. Detected at lower levels in brain, lung, stomach and spleen.
CC {ECO:0000269|PubMed:12604222}.
CC -!- DOMAIN: The C-terminus peroxisomal targeting signal tripeptide is
CC important for peroxisomal import. Once in the peroxisome, it is
CC involved in intersubunit interactions. {ECO:0000269|PubMed:18334214}.
CC -!- DOMAIN: Three specific residues, Phe-177, Leu-180 and Asn-196 are
CC conserved between non-primate mammals whereas the respective residues
CC are serine, phenylalanine and threonine in primates (PubMed:19056333).
CC The two residues at positions 177 and 180 are molecular determinants
CC responsible for the stereoselective reduction of 3-ketosteroids and
CC benzil (PubMed:19056333). The presence of an asparagine at position 196
CC is important for the maintenance of the quaternary structure resulting
CC in stability at cold temperature and improved catalytic activity toward
CC retinal (PubMed:19056333). {ECO:0000269|PubMed:19056333}.
CC -!- MISCELLANEOUS: Primate DHRS4s display different stereoselectivity and
CC catalytic efficiency in the oxidoreduction of some substrates as
CC compared to other mammal DHRS4s due to a difference in conserved amino
CC acid residues. {ECO:0000269|PubMed:19056333}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB78528.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CT961055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB062757; BAB78528.1; ALT_INIT; mRNA.
DR RefSeq; NP_999184.2; NM_214019.2.
DR PDB; 2ZAT; X-ray; 1.50 A; A/B/C/D=20-279.
DR PDBsum; 2ZAT; -.
DR AlphaFoldDB; Q8WNV7; -.
DR SMR; Q8WNV7; -.
DR DIP; DIP-29647N; -.
DR STRING; 9823.ENSSSCP00000002200; -.
DR PaxDb; Q8WNV7; -.
DR PeptideAtlas; Q8WNV7; -.
DR PRIDE; Q8WNV7; -.
DR Ensembl; ENSSSCT00000043526; ENSSSCP00000033860; ENSSSCG00000002013.
DR Ensembl; ENSSSCT00005032776; ENSSSCP00005019979; ENSSSCG00005020358.
DR Ensembl; ENSSSCT00025102111; ENSSSCP00025045164; ENSSSCG00025074069.
DR Ensembl; ENSSSCT00035078991; ENSSSCP00035032417; ENSSSCG00035058980.
DR Ensembl; ENSSSCT00045011093; ENSSSCP00045007557; ENSSSCG00045006617.
DR Ensembl; ENSSSCT00055020730; ENSSSCP00055016395; ENSSSCG00055010404.
DR Ensembl; ENSSSCT00065089974; ENSSSCP00065039349; ENSSSCG00065065441.
DR Ensembl; ENSSSCT00070003002; ENSSSCP00070002471; ENSSSCG00070001596.
DR GeneID; 397082; -.
DR KEGG; ssc:397082; -.
DR CTD; 10901; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000158919; -.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q8WNV7; -.
DR OMA; WEVANVI; -.
DR OrthoDB; 1194344at2759; -.
DR TreeFam; TF315405; -.
DR BRENDA; 1.1.1.184; 6170.
DR Reactome; R-SSC-5365859; RA biosynthesis pathway.
DR Reactome; R-SSC-9033241; Peroxisomal protein import.
DR EvolutionaryTrace; Q8WNV7; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Chromosome 7.
DR Bgee; ENSSSCG00000002013; Expressed in testis and 44 other tissues.
DR ExpressionAtlas; Q8WNV7; baseline and differential.
DR Genevisible; Q8WNV7; SS.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0000253; F:3-keto sterol reductase activity; IDA:UniProtKB.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042180; P:cellular ketone metabolic process; IDA:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; IBA:GO_Central.
DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
DR GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
DR InterPro; IPR029511; DHRS4-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43943:SF8; PTHR43943:SF8; 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; Acetylation; Direct protein sequencing; NADP; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..279
FT /note="Dehydrogenase/reductase SDR family member 4"
FT /id="PRO_0000054649"
FT MOTIF 277..279
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000269|PubMed:18334214"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001,
FT ECO:0000269|PubMed:18334214"
FT BINDING 37..61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18334214"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18334214"
FT SITE 177
FT /note="Responsible for the stereoselective reduction of 3-
FT ketosteroids into 3alpha-hydroxysteroids and benzil into S-
FT benzoin"
FT /evidence="ECO:0000269|PubMed:19056333"
FT SITE 180
FT /note="Responsible for the stereoselective reduction of 3-
FT ketosteroids into 3alpha-hydroxysteroids and benzil into S-
FT benzoin"
FT /evidence="ECO:0000269|PubMed:19056333"
FT SITE 196
FT /note="Important for the maintenance of the quaternary
FT structure, the catalytic activity and cold stability"
FT /evidence="ECO:0000269|PubMed:18334214,
FT ECO:0000269|PubMed:19056333"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 93
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 217
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 217
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 228
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 235
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MUTAGEN 177
FT /note="F->S: Change in stereoselective activity by the
FT reduction of 3-ketosteroids and benzil into 3beta-
FT hydroxysteroid and R-benzoin, respectively; when associated
FT with F-180."
FT /evidence="ECO:0000269|PubMed:19056333"
FT MUTAGEN 180
FT /note="L->F: Change in stereoselective activity by the
FT reduction of 3-ketosteroids and benzil into 3beta-
FT hydroxysteroid and R-benzoin, respectively; when associated
FT with S-177."
FT /evidence="ECO:0000269|PubMed:19056333"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:2ZAT"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:2ZAT"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:2ZAT"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:2ZAT"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:2ZAT"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 181..201
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2ZAT"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:2ZAT"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2ZAT"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2ZAT"
SQ SEQUENCE 279 AA; 29919 MW; EB7E0AC55CACBCE5 CRC64;
MRAAGQLLRA CSQTWKSVRM ASTGVERRKP LENKVALVTA STDGIGLAIA RRLAQDGAHV
VVSSRKQENV DRTVATLQGE GLSVTGTVCH VGKAEDRERL VAMAVNLHGG VDILVSNAAV
NPFFGNIIDA TEEVWDKILH VNVKATVLMT KAVVPEMEKR GGGSVLIVSS VGAYHPFPNL
GPYNVSKTAL LGLTKNLAVE LAPRNIRVNC LAPGLIKTNF SQVLWMDKAR KEYMKESLRI
RRLGNPEDCA GIVSFLCSED ASYITGETVV VGGGTASRL
