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P11884 (ALDH2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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·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):
ALDH class 2
ALDH-E2
ALDH1
Gene names
Name:Aldh2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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)

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to fatty acid

Inferred from expression pattern PubMed 11463352. Source: RGD

cellular response to hormone stimulus

Inferred from expression pattern PubMed 8749803. Source: RGD

ethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

liver development

Inferred from expression pattern PubMed 16291827. Source: RGD

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 21123025. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 16339744. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 16782756. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 11578593. Source: RGD

response to nicotine

Inferred from expression pattern PubMed 12359213. Source: RGD

response to progesterone

Inferred from expression pattern PubMed 8749803. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 8749803. Source: RGD

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.4. Source: RGD

   Molecular_functionNADH binding

Inferred from direct assay PubMed 21276780. Source: RGD

aldehyde dehydrogenase (NAD) activity

Inferred from direct assay PubMed 4149764. Source: RGD

identical protein binding

Inferred from direct assay Ref.4. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1919Mitochondrion
Chain20 – 519500Aldehyde dehydrogenase, mitochondrial
PRO_0000007170

Regions

Nucleotide binding264 – 2696NAD By similarity

Sites

Active site2871Proton acceptor
Active site3211Nucleophile
Site1881Transition state stabilizer

Amino acid modifications

Modified residue201N-acetylserine Probable
Modified residue541N6-acetyllysine By similarity
Modified residue751N6-acetyllysine By similarity
Modified residue801N6-acetyllysine By similarity
Modified residue1611N6-acetyllysine By similarity
Modified residue3701N6-acetyllysine By similarity
Modified residue3771N6-acetyllysine By similarity
Modified residue3851N6-acetyllysine By similarity
Modified residue4091N6-acetyllysine By similarity
Modified residue4281N6-acetyllysine By similarity
Modified residue4301N6-acetyllysine By similarity
Modified residue4431N6-acetyllysine By similarity
Modified residue4531N6-acetyllysine By similarity

Natural variations

Natural variant861Q → R in allele Aldh2*2 and allele Aldh2*3; in strains UChA and UChB. Ref.5
Natural variant4981E → K in allele Aldh2*3; in strain UChB. Ref.5

Secondary structure

... 519
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11884 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 75C748202F1333E5

FASTA51956,488
        10         20         30         40         50         60 
MLRAALSTAR RGPRLSRLLS AAATSAVPAP NQQPEVFCNQ IFINNEWHDA VSKKTFPTVN 

        70         80         90        100        110        120 
PSTGEVICQV AEGNKEDVDK AVKAAQAAFQ 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 IASHEDVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA 

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

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

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

       490        500        510 
QSPFGGYKMS GSGRELGEYG LQAYTEVKTV TVKVPQKNS 

« Hide

References

« Hide 'large scale' references
[1]"Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences."
Farres J., Guan K.-L., Weiner H.
Eur. J. Biochem. 180:67-74(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"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].
Tissue: Prostate.
[3]"Sequence of the signal peptide for rat liver mitochondrial aldehyde dehydrogenase."
Farres J., Guan K.-L., Weiner H.
Biochem. Biophys. Res. Commun. 150:1083-1087(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-29.
Tissue: Liver.
[4]"Purification and characterization of catalytically active precursor of rat liver mitochondrial aldehyde dehydrogenase expressed in Escherichia coli."
Jeng J., Weiner H.
Arch. Biochem. Biophys. 289:214-222(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-19.
Tissue: Liver.
[5]"Mutations in mitochondrial aldehyde dehydrogenase (ALDH2) change cofactor affinity and segregate with voluntary alcohol consumption in rats."
Sapag A., Tampier L., Valle-Prieto A., Quintanilla M.E., Moncada C., Israel Y.
Pharmacogenetics 13:509-515(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-519, VARIANTS ARG-86 AND LYS-498.
Strain: UChA, UChB and Wistar.
Tissue: Liver.
[6]"Genomic structure and sequence of the mitochondrial aldehyde dehydrogenase gene (ALDH2) of the Lewis rat."
Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-519.
Strain: Lewis.
[7]"Genomic structure and sequence of the mitochondrial aldehyde dehydrogenase gene of the Lewis rat."
Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-519.
Strain: Lewis.
Tissue: Liver.
[8]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 162-174; 198-228; 260-340; 327-340; 358-370; 397-409 AND 495-508, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[9]"A mitochondrial protein fraction catalyzing transport of the K+ analog T1+."
Diwan J.J., Paliwal R., Kaftan E., Bawa R.
FEBS Lett. 273:215-218(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 327-340.
[10]"Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20."
Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S., Endo T., Kohda D.
Cell 100:551-560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 12-22.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14977 mRNA. Translation: CAA33101.1.
BC062081 mRNA. Translation: AAH62081.1.
M19030 mRNA. Translation: AAA40719.1.
AY566467 mRNA. Translation: AAS75813.1.
AY566468 mRNA. Translation: AAS75814.1.
AY566469 mRNA. Translation: AAS75815.1.
AF529165 mRNA. Translation: AAM94394.2.
AY034137 Genomic DNA. Translation: AAK57732.1.
PIRS03564.
RefSeqNP_115792.1. NM_032416.1.
UniGeneRn.101781.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OM2NMR-B12-20[»]
2V1SX-ray2.05H/I/J/K/L/M/N12-24[»]
2V1TX-ray1.92C/D12-22[»]
3AWRX-ray2.00C/D12-20[»]
3AX2X-ray1.90B/D/F/H12-20[»]
3AX3X-ray2.10B/D/F/H12-20[»]
3AX5X-ray2.20B/D12-20[»]
ProteinModelPortalP11884.
SMRP11884. Positions 26-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11884. 2 interactions.
MINTMINT-4569918.

Chemistry

BindingDBP11884.
ChEMBLCHEMBL2812.

PTM databases

PhosphoSiteP11884.

2D gel databases

World-2DPAGE0004:P11884.

Proteomic databases

PaxDbP11884.
PRIDEP11884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29539.
KEGGrno:29539.
UCSCRGD:69219. rat.

Organism-specific databases

CTD217.
RGD69219. Aldh2.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidP11884.
KOK00128.
PhylomeDBP11884.

Enzyme and pathway databases

SABIO-RKP11884.
UniPathwayUPA00780; UER00768.

Gene expression databases

GenevestigatorP11884.

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_CYS.
IPR029510. Ald_DH_CS_GLU.
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

EvolutionaryTraceP11884.
NextBio609531.

Entry information

Entry nameALDH2_RAT
AccessionPrimary (citable) accession number: P11884
Secondary accession number(s): Q6Q288 expand/collapse secondary AC list , Q6Q289, Q6Q290, Q8K3V8, Q91ZD7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 138 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways