Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P47738 (ALDH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase, mitochondrial

EC=1.2.1.3
Alternative name(s):
AHD-M1
ALDH class 2
ALDH-E2
ALDHI
Gene names
Name:Aldh2
Synonyms:Ahd-1, Ahd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is capable of converting retinaldehyde to retinoic acid.

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathway

Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix.

Induction

By retinoic acid; 3-5 fold increase.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sirt3Q8R1042EBI-2308120,EBI-6999888

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1919Mitochondrion By similarity
Chain20 – 519500Aldehyde dehydrogenase, mitochondrial
PRO_0000007169

Regions

Nucleotide binding264 – 2696NAD By similarity

Sites

Active site2871Proton acceptor By similarity
Active site3211Nucleophile By similarity
Site1881Transition state stabilizer By similarity

Amino acid modifications

Modified residue201N-acetylserine Probable
Modified residue541N6-acetyllysine Ref.7
Modified residue751N6-acetyllysine Ref.7
Modified residue801N6-acetyllysine Ref.7
Modified residue1611N6-acetyllysine Ref.7
Modified residue3701N6-acetyllysine Ref.7
Modified residue3771N6-acetyllysine Ref.7
Modified residue3851N6-acetyllysine Ref.7
Modified residue4091N6-acetyllysine Ref.7
Modified residue4281N6-acetyllysine Ref.7
Modified residue4301N6-acetyllysine Ref.6 Ref.7
Modified residue4431N6-acetyllysine Ref.7
Modified residue4531N6-acetyllysine Ref.7

Experimental info

Sequence conflict88 – 892AF → C in AAC60691. Ref.2
Sequence conflict1811Missing in AAC60691. Ref.2
Sequence conflict2271I → S in AAC60691. Ref.2
Sequence conflict3441R → G in AAC60691. Ref.2
Sequence conflict3701K → N in AAC60691. Ref.2
Sequence conflict3781S → M in AAC60691. Ref.2
Sequence conflict4761D → V in AAC60691. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P47738 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 200806F63D48F4DA

FASTA51956,538
        10         20         30         40         50         60 
MLRAALTTVR RGPRLSRLLS AAATSAVPAP NHQPEVFCNQ IFINNEWHDA VSRKTFPTVN 

        70         80         90        100        110        120 
PSTGEVICQV AEGNKEDVDK AVKAARAAFQ LGSPWRRMDA SDRGRLLYRL ADLIERDRTY 

       130        140        150        160        170        180 
LAALETLDNG KPYVISYLVD LDMVLKCLRY YAGWADKYHG KTIPIDGDFF SYTRHEPVGV 

       190        200        210        220        230        240 
CGQIIPWNFP LLMQAWKLGP ALATGNVVVM KVAEQTPLTA LYVANLIKEA GFPPGVVNIV 

       250        260        270        280        290        300 
PGFGPTAGAA IASHEGVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA 

       310        320        330        340        350        360 
DMDWAVEQAH FALFFNQGQC CCAGSRTFVQ ENVYDEFVER SVARAKSRVV GNPFDSRTEQ 

       370        380        390        400        410        420 
GPQVDETQFK KILGYIKSGQ QEGAKLLCGG GAAADRGYFI QPTVFGDVKD GMTIAKEEIF 

       430        440        450        460        470        480 
GPVMQILKFK TIEEVVGRAN DSKYGLAAAV FTKDLDKANY LSQALQAGTV WINCYDVFGA 

       490        500        510 
QSPFGGYKMS GSGRELGEYG LQAYTEVKTV TVKVPQKNS 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-509.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-75; LYS-80; LYS-161; LYS-370; LYS-377; LYS-385; LYS-409; LYS-428; LYS-430; LYS-443 AND LYS-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07235 mRNA. Translation: AAA64636.1.
S71509 mRNA. Translation: AAC60691.1.
BC005476 mRNA. Translation: AAH05476.1.
Z32545 Genomic DNA. No translation available.
PIRI48966.
RefSeqNP_033786.1. NM_009656.3.
UniGeneMm.284446.

3D structure databases

ProteinModelPortalP47738.
SMRP47738. Positions 26-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP47738. 5 interactions.
MINTMINT-1859437.

PTM databases

PhosphoSiteP47738.

2D gel databases

REPRODUCTION-2DPAGEP47738.
SWISS-2DPAGEP47738.
UCD-2DPAGEP47738.

Proteomic databases

PaxDbP47738.
PRIDEP47738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031411; ENSMUSP00000031411; ENSMUSG00000029455.
GeneID11669.
KEGGmmu:11669.
UCSCuc008zjt.1. mouse.

Organism-specific databases

CTD217.
MGIMGI:99600. Aldh2.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidP47738.
KOK00128.
OMAVAYHIYE.
OrthoDBEOG7PS1F7.
PhylomeDBP47738.
TreeFamTF300455.

Enzyme and pathway databases

UniPathwayUPA00780; UER00768.

Gene expression databases

ArrayExpressP47738.
BgeeP47738.
CleanExMM_ALDH2.
GenevestigatorP47738.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDH2. mouse.
NextBio279291.
PROP47738.
SOURCESearch...

Entry information

Entry nameALDH2_MOUSE
AccessionPrimary (citable) accession number: P47738
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot