DHRS4
entrez
10901
canonical
uniprot
Q9BTZ2
canonical
ensembl
ENSG00000157326
resolver
ensembl
ENSG00000284807
resolver
ensp
ENSP00000326219
resolver
ensp
ENSP00000380264
resolver
ensp
ENSP00000380265
resolver
ensp
ENSP00000440508
resolver
ensp
ENSP00000452645
resolver
ensp
ENSP00000453367
resolver
ensp
ENSP00000453983
resolver
ensp
ENSP00000495517
resolver
enst
ENST00000543741
resolver
enst
ENST00000643517
resolver
genesymbol
DHRS4
resolver
genesymbol_syn
SDR25C2
resolver
hgnc
HGNC:16985
resolver
uniprot
B2RB10
resolver
uniprot
B7WNS9
resolver
uniprot
D3YTB8
resolver
uniprot
E2QRL8
resolver
uniprot
F5GWZ1
resolver
uniprot
O95162
resolver
uniprot
Q20CR0
resolver
uniprot
Q2LC19
resolver
uniprot
Q2LE81
resolver
uniprot
Q58IU4
resolver
uniprot
Q6E0Y1
resolver
uniprot
Q6UWU3
resolver
uniprot
Q71UQ6
resolver
uniprot
Q8TD03
resolver
uniprot
Q9H3N5
resolver
uniprot
Q9NV08
resolver
uniprot_entry
DHRS4_HUMAN
resolver
uniprot_entry
F5GWZ1_HUMAN
resolver
uniprot_sec
B2RB10
resolver
uniprot_sec
B7WNS9
resolver
uniprot_sec
D3YTB8
resolver
uniprot_sec
E2QRL8
resolver
uniprot_sec
O95162
resolver
uniprot_sec
Q20CR0
resolver
uniprot_sec
Q2LC19
resolver
uniprot_sec
Q2LE81
resolver
uniprot_sec
Q58IU4
resolver
uniprot_sec
Q6E0Y1
resolver
uniprot_sec
Q6UWU3
resolver
uniprot_sec
Q71UQ6
resolver
uniprot_sec
Q8TD03
resolver
uniprot_sec
Q9H3N5
resolver
uniprot_sec
Q9NV08
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by flavonoids (quercetin and genistein), cetylpyridium chloride, phenylhexane and valproic acid. Low inhibition is observed with fatty acids (myristic acid and lauric acid). No significant inhibition is observed with barbital, dicumarol, indomethacin, metyrapone, ethacrynic acid, disulfiram, hexestrol and benzodiazepines (diazepam and nitrazepam). {ECO:0000269|PubMed:18571493}.
uniprot
proteins
amino_acid_sequence
MHKAGLLGLCARAWNSVRMASSGMTRRDPLANKVALVTASTDGIGFAIARRLAQDGAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVKLHGGIDILVSNAAVNPFFGSIMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLTKTLAIELAPRNIRVNCLAPGLIKTSFSRMLWMDKEKEESMKETLRIRRLGEPEDCAGIVSFLCSEDASYITGETVVVGGGTPSRL
uniprot
proteins
ec_number
1.1.1.184
uniprot
proteins
function
FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones (PubMed:18571493, PubMed:19056333). Reduces 3-ketosteroids and benzil into 3beta-hydroxysteroids and R-benzoin, respectively, in contrast to the stereoselectivity of non-primate DHRS4s which produce 3alpha-hydroxysteroids and S-benzoin (PubMed:19056333). Displays low activity toward all-trans-retinal and no activity toward 9-cis-retinal as compared to non-primate mammals (PubMed:18571493, PubMed:19056333). In the reverse reaction, catalyze the NAD-dependent oxidation of 3beta-hydroxysteroids and alcohol, but with much lower efficiency (PubMed:18571493, PubMed:19056333). Involved in the metabolism of 3beta-hydroxysteroids, isatin and xenobiotic carbonyl compounds (PubMed:18571493, PubMed:19056333). {ECO:0000269|PubMed:18571493, ECO:0000269|PubMed:19056333}.; FUNCTION: [Isoform 7]: No detected catalytic activity in vitro, possibly due to the lack of catalytic site. {ECO:0000269|PubMed:22227495}.; FUNCTION: [Isoform 8]: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Involved in the metabolism of 3beta-hydroxysteroids, isatin and xenobiotic carbonyl compounds. Has a higher catalytic activity for xenobiotic alpha-dicarbonyl compounds, sucha as benzil, than isoform 1 and is involved in benzil detoxification. {ECO:0000269|PubMed:23128527}.
uniprot
proteins
mass_dalton
29537
uniprot
proteins
mutagenesis
MUTAGEN 176; /note="S->F: Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195."; /evidence="ECO:0000269|PubMed:19056333"; MUTAGEN 179; /note="F->L: Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195."; /evidence="ECO:0000269|PubMed:19056333"; MUTAGEN 195; /note="T->N: Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179."; /evidence="ECO:0000269|PubMed:18571493, ECO:0000269|PubMed:19056333
uniprot
proteins
protein_family
Short-chain dehydrogenases/reductases (SDR) family
uniprot
proteins
pubmed
10333503
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15473316
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17230527
uniprot
proteins
pubmed
18571493
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19027726
uniprot
proteins
pubmed
19056333
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22227495
uniprot
proteins
pubmed
23128527
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27323117
uniprot
proteins
sequence_length
278
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Peroxisome {ECO:0000269|PubMed:10333503, ECO:0000269|PubMed:17230527}. Note=Isoform 4 is not peroxisomal. {ECO:0000269|PubMed:17230527}.; SUBCELLULAR LOCATION: [Isoform 7]: Nucleus {ECO:0000269|PubMed:22227495}.
uniprot
proteins