Q9Y394 · DHRS7_HUMAN
- ProteinDehydrogenase/reductase SDR family member 7
- GeneDHRS7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids339 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including steroids, retinoids and xenobiotics (PubMed:24246760, PubMed:26466768, PubMed:28457967, PubMed:28687384).
Catalyzes the reduction/inactivation of 5alpha-dihydrotestosterone to 3alpha-androstanediol, with a possible role in the modulation of androgen receptor function (PubMed:28457967, PubMed:28687384).
Involved in the reduction of all-trans-retinal to all-trans-retinol (PubMed:26466768).
Converts cortisone to 20beta-dihydrocortisone in vitro, although the physiological relevance of this activity is questionable (PubMed:28457967).
Reduces exogenous compounds such as quinones (1,2-naphtoquinone, 9,10-phenantrenequinone and benzoquinone) and other xenobiotics (alpha-diketones) in vitro, suggesting a role in the biotransformation of xenobiotics with carbonyl group (PubMed:24246760, PubMed:26466768).
A dehydrogenase activity has not been detected so far (PubMed:24246760).
May play a role as tumor suppressor (PubMed:26311046).
Catalyzes the reduction/inactivation of 5alpha-dihydrotestosterone to 3alpha-androstanediol, with a possible role in the modulation of androgen receptor function (PubMed:28457967, PubMed:28687384).
Involved in the reduction of all-trans-retinal to all-trans-retinol (PubMed:26466768).
Converts cortisone to 20beta-dihydrocortisone in vitro, although the physiological relevance of this activity is questionable (PubMed:28457967).
Reduces exogenous compounds such as quinones (1,2-naphtoquinone, 9,10-phenantrenequinone and benzoquinone) and other xenobiotics (alpha-diketones) in vitro, suggesting a role in the biotransformation of xenobiotics with carbonyl group (PubMed:24246760, PubMed:26466768).
A dehydrogenase activity has not been detected so far (PubMed:24246760).
May play a role as tumor suppressor (PubMed:26311046).
Catalytic activity
- all-trans-retinol + NADP+ = all-trans-retinal + H+ + NADPHThis reaction proceeds in the backward direction.
- 5alpha-androstane-3alpha,17beta-diol + NADP+ = 17beta-hydroxy-5alpha-androstan-3-one + H+ + NADPHThis reaction proceeds in the backward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
20.47 μM | NADPH | |||||
30.08 μM | NADH | |||||
24.3 μM | all-trans-retinal | |||||
48.4 μM | 17beta-hydroxy-5alpha-androstan-3-one |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
10.58 nmol/min/mg | with NADPH as substrate | ||||
2.38 nmol/min/mg | with NADH as substrate | ||||
270.3 nmol/min/mg | for the NADPH-dependent reduction of all-trans-retinal | ||||
34.4 nmol/min/mg | for the NADPH-dependent reduction of 17beta-hydroxy-5alpha-androstan-3-one to 5alpha-androstane-3alpha,17beta-diol |
kcat is 10.22 min-1 for the NADPH-dependent reduction of all-trans-retinal.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 60 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 62 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 190 | substrate | ||||
Sequence: S | ||||||
Active site | 203 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 203 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 207 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 239 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Molecular Function | all-trans-retinol dehydrogenase (NADP+) activity | |
Molecular Function | carbonyl reductase (NADPH) activity | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDehydrogenase/reductase SDR family member 7
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y394
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052319 | 218 | in dbSNP:rs34583017 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 459 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-28 | UniProt | |||||
Sequence: MNWELLLWLLVLCALLLLLVQLLRFLRA | |||||||
Chain | PRO_0000031968 | 29-339 | UniProt | Dehydrogenase/reductase SDR family member 7 | |||
Sequence: DGDLTLLWAEWQGRRPEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRGFFNGLRTELATYPGIIVSNICPGPVQSNIVENSLAGEVTKTIGNNGDQSHKMTTSRCVRLMLISMANDLKEVWISEQPFLLVTYLWQYMPTWAWWITNKMGKKRIENFKSGVDADSSYFKIFKTKHD | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y394 | SACM1L Q9NTJ5 | 3 | EBI-1387800, EBI-3917235 | |
BINARY | Q9Y394 | TMEM120A Q9BXJ8 | 3 | EBI-1387800, EBI-727322 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9Y394-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length339
- Mass (Da)38,299
- Last updated1999-11-01 v1
- Checksum7B251CE5894ED70C
Q9Y394-2
- Name2
- Differences from canonical
- 1-50: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008103 | 1-50 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF151844 EMBL· GenBank· DDBJ | AAD34081.1 EMBL· GenBank· DDBJ | mRNA | ||
AF126782 EMBL· GenBank· DDBJ | AAF06941.1 EMBL· GenBank· DDBJ | mRNA | ||
AY359031 EMBL· GenBank· DDBJ | AAQ89390.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313285 EMBL· GenBank· DDBJ | BAG36093.1 EMBL· GenBank· DDBJ | mRNA | ||
AL163853 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471061 EMBL· GenBank· DDBJ | EAW80770.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000637 EMBL· GenBank· DDBJ | AAH00637.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007337 EMBL· GenBank· DDBJ | AAH07337.1 EMBL· GenBank· DDBJ | mRNA |