Q9QYY9 · ADH4_MOUSE
- ProteinAll-trans-retinol dehydrogenase [NAD(+)] ADH4
- GeneAdh4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (PubMed:17279314).
Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420).
Also catalyzes the reduction of benzoquinones (By similarity).
Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420).
Also catalyzes the reduction of benzoquinones (By similarity).
Catalytic activity
- all-trans-retinol + NAD+ = all-trans-retinal + H+ + NADHThis reaction proceeds in the forward direction.
- 9-cis-retinol + NAD+ = 9-cis-retinal + H+ + NADHThis reaction proceeds in the forward direction.
- 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD+ = 20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H+ + NADHThis reaction proceeds in the forward direction.
- 20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD+ = (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H+ + NADHThis reaction proceeds in the forward direction.
- 1,4-benzoquinone + H+ + NADH = hydroquinone + NAD+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Activity regulation
Oxidation of 20-HETE is inhibited by low concentrations of N-heptylformamide (PubMed:16081420).
Oxidation of 20-HETE is a decreased by 55-65% by either all-trans-retinol or all-trans-retinoic acid (PubMed:16081420).
Strongly inhibited by omega-hydroxy fatty acids (PubMed:10514444).
Oxidation of 20-HETE is a decreased by 55-65% by either all-trans-retinol or all-trans-retinoic acid (PubMed:16081420).
Strongly inhibited by omega-hydroxy fatty acids (PubMed:10514444).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
35 μM | 20-HETE | |||||
0.24 mM | 1,4-benzoquinone |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 49 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 68 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 98 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 101 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 104 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 112 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 179 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 204-209 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GLGCVG | ||||||
Binding site | 228 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 233 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 297-299 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VGA | ||||||
Binding site | 320-322 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TFF | ||||||
Binding site | 372 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Molecular Function | alcohol dehydrogenase (NAD+) activity | |
Molecular Function | alcohol dehydrogenase (NAD+) activity, zinc-dependent | |
Molecular Function | aldose reductase (NADPH) activity | |
Molecular Function | all-trans retinal binding | |
Molecular Function | all-trans-retinol dehydrogenase (NAD+) activity | |
Molecular Function | benzaldehyde dehydrogenase [NAD(P)+] activity | |
Molecular Function | ethanol binding | |
Molecular Function | NAD binding | |
Molecular Function | NADPH:quinone reductase activity | |
Molecular Function | retinol binding | |
Molecular Function | S-(hydroxymethyl)glutathione dehydrogenase (NAD(P)+) activity | |
Molecular Function | zinc ion binding | |
Biological Process | alcohol catabolic process | |
Biological Process | cellular aldehyde metabolic process | |
Biological Process | ethanol metabolic process | |
Biological Process | fatty acid omega-oxidation | |
Biological Process | formaldehyde catabolic process | |
Biological Process | quinone metabolic process | |
Biological Process | retinol metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameAll-trans-retinol dehydrogenase [NAD(+)] ADH4
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QYY9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 48 | Strongly increases NAD-retinol dehydrogenase activity. | ||||
Sequence: P → H | ||||||
Mutagenesis | 52 | No effect. | ||||
Sequence: N → H | ||||||
Mutagenesis | 183 | Strongly increases activity towards ethanol, increases KM for benzoquinone 10-fold. | ||||
Sequence: S → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 28 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000160682 | 1-377 | All-trans-retinol dehydrogenase [NAD+] ADH4 | |||
Sequence: MGTQGKVIKCKAAIAWKTGSPLCIEEIEVSPPKACEVRIQVIATCVCPTDINATDPKKKALFPVVLGHECAGIVESVGPGVTNFKPGDKVIPFFAPQCKRCKLCLSPLTNLCGKLRNFKYPTIDQELMEDRTSRFTCKGRSIYHFMGVSSFSQYTVVSEANLARVDDEANLERVCLIGCGFSSGYGAAINTAKVTPSSTCAVFGLGCVGLSAIIGCKIAGASRIIAIDINGEKFPKAKALGATDCLNPRELDKPVQDVITELTAGGVDYSLDCAGTAQTLKAAVDCTVLGWGSCTVVGAKVDKMTIPTVDVILGRSINGTFFGGWKSVDSVPNLVSDYKNKKFDLDLLVTHALPFESINDAIDLMKEGKSIRTILTF |
Proteomic databases
PTM databases
Expression
Structure
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)40,211
- Last updated2011-06-28 v4
- Checksum5B527E48BB745E14
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E0CYI4 | E0CYI4_MOUSE | Adh4 | 216 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 197 | in Ref. 1; CAB57455 | ||||
Sequence: S → G | ||||||
Sequence conflict | 303 | in Ref. 1; CAB57455 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ245750 EMBL· GenBank· DDBJ | CAB57455.1 EMBL· GenBank· DDBJ | mRNA | ||
AK132994 EMBL· GenBank· DDBJ | BAE21459.1 EMBL· GenBank· DDBJ | mRNA |