P47739 · AL3A1_MOUSE
- ProteinAldehyde dehydrogenase, dimeric NADP-preferring
- GeneAldh3a1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids453 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:25286108).
Preferentially oxidizes aromatic aldehyde substrates (PubMed:11784860).
Comprises about 50 percent of corneal epithelial soluble proteins (PubMed:11784860).
May play a role in preventing corneal damage caused by ultraviolet light (PubMed:10376761).
Preferentially oxidizes aromatic aldehyde substrates (PubMed:11784860).
Comprises about 50 percent of corneal epithelial soluble proteins (PubMed:11784860).
May play a role in preventing corneal damage caused by ultraviolet light (PubMed:10376761).
Catalytic activity
- an aldehyde + H2O + NAD+ = a carboxylate + 2 H+ + NADH
- H2O + NAD+ + octanal = 2 H+ + NADH + octanoate
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | 3-chloroallyl aldehyde dehydrogenase activity | |
Molecular Function | alcohol dehydrogenase (NADP+) activity | |
Molecular Function | aldehyde dehydrogenase (NAD+) activity | |
Molecular Function | benzaldehyde dehydrogenase (NAD+) activity | |
Molecular Function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor | |
Biological Process | cellular aldehyde metabolic process | |
Biological Process | lipid metabolic process | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | response to cAMP | |
Biological Process | response to glucocorticoid | |
Biological Process | response to hypoxia | |
Biological Process | response to organic cyclic compound | |
Biological Process | response to xenobiotic stimulus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameAldehyde dehydrogenase, dimeric NADP-preferring
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP47739
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 154 | in allele Ald3a1c | ||||
Sequence: I → N | ||||||
Natural variant | 305 | in allele Ald3a1c | ||||
Sequence: H → R | ||||||
Natural variant | 352 | in allele Ald3a1c | ||||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000056471 | 2-453 | Aldehyde dehydrogenase, dimeric NADP-preferring | |||
Sequence: SNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDWAEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKVAHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLVRSLRNEEANKARYPPSPAKMPRH | ||||||
Modified residue | 178 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 194 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Constitutively expressed in cornea, stomach, skin, bladder and lungs. Lowest expression levels in lungs and bladder.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length453
- Mass (Da)50,481
- Last updated2012-10-03 v2
- Checksum7B4EA1CC56B5FAA1
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B1ATI6 | B1ATI6_MOUSE | Aldh3a1 | 34 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 88 | in Ref. 1; AAA20670 | ||||
Sequence: A → G | ||||||
Sequence conflict | 88 | in Ref. 3; AAD15964 | ||||
Sequence: A → R |
Polymorphism
There are two alleles, Ald3a1a and Ald3a1c. Ald3a1c codes for a low activity enzyme and is associated with extensive corneal clouding after exposure to ultraviolet light. Ald3a1a encodes the high activity enzyme.
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U12785 EMBL· GenBank· DDBJ | AAA20670.1 EMBL· GenBank· DDBJ | mRNA | ||
AF072815 EMBL· GenBank· DDBJ | AAD15964.1 EMBL· GenBank· DDBJ | mRNA | ||
AL646093 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |