Reviewed,
UniProtKB/Swiss-Prot P47738 (ALDH2_MOUSE)
Last modified
June 16, 2009.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aldehyde dehydrogenase, mitochondrial EC=1.2.1.3 Alternative name(s): ALDH class 2 AHD-M1 ALDHI ALDH-E2 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 519 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Is capable of converting retinaldehyde to retinoic acid. |
| Catalytic activity | An aldehyde + NAD+ + H2O = an acid + NADH. |
| Pathway | Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Induction | By retinoic acid; 3-5 fold increase. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 19 | 19 | Mitochondrion By similarity | ||||||
| Chain | 20 – 519 | 500 | Aldehyde dehydrogenase, mitochondrial | PRO_0000007169 | |||||
Regions | |||||||||
| Nucleotide binding | 264 – 269 | 6 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 287 | 1 | Proton acceptor By similarity | ||||||
| Active site | 321 | 1 | Nucleophile By similarity | ||||||
| Site | 188 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 20 | 1 | N-acetylserine Probable | ||||||
| Modified residue | 370 | 1 | N6-acetyllysine Ref.6 | ||||||
Experimental info | |||||||||
| Sequence conflict | 88 – 89 | 2 | AF → C in AAC60691. Ref.2 | ||||||
| Sequence conflict | 181 | 1 | Missing in AAC60691. Ref.2 | ||||||
| Sequence conflict | 227 | 1 | I → S in AAC60691. Ref.2 | ||||||
| Sequence conflict | 344 | 1 | R → G in AAC60691. Ref.2 | ||||||
| Sequence conflict | 370 | 1 | K → N in AAC60691. Ref.2 | ||||||
| Sequence conflict | 378 | 1 | S → M in AAC60691. Ref.2 | ||||||
| Sequence conflict | 476 | 1 | D → V in AAC60691. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of the gene encoding mouse mitochondrial aldehyde dehydrogenase." Chang C., Yoshida A. Gene 148:331-336(1994) [PubMed: 7958964] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J. |
| [2] | "Enzymatic conversion of retinaldehyde to retinoic acid by cloned murine cytosolic and mitochondrial aldehyde dehydrogenases." Chen M., Achkar C., Gudas L.J. Mol. Pharmacol. 46:88-96(1994) [PubMed: 8058062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland. |
| [4] | Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 54-80; 87-96; 162-174; 198-228; 260-282; 327-340; 349-370; 386-409; 417-428; 431-438 AND 444-453, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus. |
| [5] | "Isolation of genomic DNA fragments corresponding to genes modulated in vivo by a transcription factor." Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., Zaballos A. Nucleic Acids Res. 22:4132-4138(1994) [PubMed: 7937138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-509. |
| [6] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-370, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U07235 mRNA. Translation: AAA64636.1. S71509 mRNA. Translation: AAC60691.1. BC005476 mRNA. Translation: AAH05476.1. Z32545 Genomic DNA. No translation available. | |
| IPI | IPI00111218. |
| PIR | I48966. |
| RefSeq | NP_033786.1. |
| UniGene | Mm.284446 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1O01 based on UniProtKB P05091. |
| SMR | P47738. Positions 26-519. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P47738. |
2-D gel databases | |
| SWISS-2DPAGE | P47738. |
| REPRODUCTION-2DPAGE | P47738. |
Proteomic databases | |
| PRIDE | P47738. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000029455. Mus musculus. [Contig view] |
| GeneID | 11669. |
| KEGG | mmu:11669. |
Organism-specific databases | |
| MGI | MGI:99600. Aldh2. |
Phylogenomic databases | |
| HOGENOM | P47738. |
| HOVERGEN | P47738. |
| OMA | P47738. PFDSQTE. |
Enzyme and pathway databases | |
| BRENDA | 1.2.1.3. 244. |
Gene expression databases | |
| ArrayExpress | P47738. |
| Bgee | P47738. |
| CleanEx | MM_ALDH2. |
| GermOnline | ENSMUSG00000029455. Mus musculus. |
Family and domain databases | |
| InterPro | IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [Graphical view] |
| Gene3D | G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| PANTHER | PTHR11699. Aldehyde_dehyd. 1 hit. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 279291. |
| SOURCE | Search... |
Entry information
| Entry name | ALDH2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P47738 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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