P30838 · AL3A1_HUMAN
- 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:1737758).
Preferentially oxidizes aromatic aldehyde substrates (PubMed:1737758).
Comprises about 50 percent of corneal epithelial soluble proteins (By similarity).
May play a role in preventing corneal damage caused by ultraviolet light (By similarity).
Preferentially oxidizes aromatic aldehyde substrates (PubMed:1737758).
Comprises about 50 percent of corneal epithelial soluble proteins (By similarity).
May play a role in preventing corneal damage caused by ultraviolet light (By similarity).
Catalytic activity
- an aldehyde + H2O + NAD+ = a carboxylate + 2 H+ + NADH
- H2O + NAD+ + octanal = 2 H+ + NADH + octanoate
Kinetics
Has a high Km for acetaldehyde.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular space | |
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 | aldehyde dehydrogenase [NAD(P)+] activity | |
Molecular Function | benzaldehyde dehydrogenase (NAD+) activity | |
Biological Process | cellular aldehyde metabolic process | |
Biological Process | lipid metabolic process | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAldehyde dehydrogenase, dimeric NADP-preferring
- 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 accessionP30838
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_018981 | 134 | in dbSNP:rs887241 | |||
Sequence: S → A | ||||||
Mutagenesis | 244 | Abolishes activity. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_018982 | 309 | in dbSNP:rs3744692 | |||
Sequence: G → E | ||||||
Natural variant | VAR_011303 | 329 | in allele ALDH3A1*2; dbSNP:rs2228100 | |||
Sequence: P → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 671 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
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_0000056470 | 2-453 | Aldehyde dehydrogenase, dimeric NADP-preferring | |||
Sequence: SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPPSPAKMTQH | ||||||
Modified residue | 178 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 194 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
High levels in stomach, esophagus and lung; low level in the liver and kidney.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P30838 | FKBP6 O75344 | 3 | EBI-3905126, EBI-744771 | |
BINARY | P30838 | POT1 Q9NUX5 | 2 | EBI-3905126, EBI-752420 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length453
- Mass (Da)50,395
- Last updated2010-11-02 v3
- ChecksumD35C488A022FAACA
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 2; AAB46377 and 3; AAB26658 | ||||
Sequence: R → P | ||||||
Sequence conflict | 27 | in Ref. 1; AAA51696 | ||||
Sequence: I → F | ||||||
Sequence conflict | 170 | in Ref. 9; AA sequence | ||||
Sequence: V → L | ||||||
Sequence conflict | 436 | in Ref. 9; AA sequence | ||||
Sequence: D → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M74542 EMBL· GenBank· DDBJ | AAA51696.1 EMBL· GenBank· DDBJ | mRNA | ||
M77477 EMBL· GenBank· DDBJ | AAB46377.1 EMBL· GenBank· DDBJ | mRNA | ||
S61044 EMBL· GenBank· DDBJ | AAB26658.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007102 EMBL· GenBank· DDBJ | AAP35766.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292193 EMBL· GenBank· DDBJ | BAF84882.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314584 EMBL· GenBank· DDBJ | BAG37160.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005722 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471212 EMBL· GenBank· DDBJ | EAW50909.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004370 EMBL· GenBank· DDBJ | AAH04370.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008892 EMBL· GenBank· DDBJ | AAH08892.1 EMBL· GenBank· DDBJ | mRNA | ||
BC021194 EMBL· GenBank· DDBJ | AAH21194.1 EMBL· GenBank· DDBJ | mRNA |