Aldehyde dehydrogenase, mitochondrial precursor

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P11884 (ALDH2_RAT)

Last modified October 13, 2009. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase, mitochondrial
    EC=1.2.1.3
Alternative name(s):
    ALDH class 2
    ALDH1
    ALDH-E2

Gene names

Name:

Aldh2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

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.

Hide | Top

General annotation (Comments)

Catalytic activity	An aldehyde + NAD⁺ + H₂O = an acid + 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.

Hide | Top

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to hormone stimulus Inferred from expression pattern. Source: RGD liver development Inferred from expression pattern. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to hyperoxia Inferred from expression pattern. Source: RGD response to lipopolysaccharide Inferred from expression pattern. Source: RGD response to nicotine Inferred from expression pattern. Source: RGD response to progesterone stimulus Inferred from expression pattern. Source: RGD response to testosterone stimulus Inferred from expression pattern. Source: RGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aldehyde dehydrogenase (NAD) activity Inferred from direct assay. Source: RGD identical protein binding Ref.4 Inferred from direct assay. Source: RGD
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 19

Mitochondrion

Chain

20 – 519

500

Aldehyde dehydrogenase, mitochondrial

PRO_0000007170

Regions

Nucleotide binding

264 – 269

NAD By similarity

Sites

Active site

287

Proton acceptor

Active site

321

Nucleophile

Site

188

Transition state stabilizer

Amino acid modifications

Modified residue

N-acetylserine Probable

Modified residue

370

N6-acetyllysine By similarity

Natural variations

Natural variant

Q → R in allele Aldh2*2 and allele Aldh2*3; in strains UChA and UChB. Ref.5

Natural variant

498

E → K in allele Aldh2*3; in strain UChB. Ref.5

Secondary structure

519

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P11884-1 [UniParc].

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

FASTA

519

56,488

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 2540003] [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: 15489334] [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: 3342060] [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: 1898068] [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: 12893989] [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, 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: 1699808] [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: 10721992] [Abstract] Cited for: STRUCTURE BY NMR OF 12-22.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

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.

IPI

IPI00197770.

PIR

S03564.

RefSeq

NP_115792.1.

UniGene

Rn.101781

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OM2	NMR	-	B	12-20	[»]
2V1S	X-ray	2.05	H/I/J/K/L/M/N	12-20	[»]
2V1T	X-ray	1.92	C/D	12-22	[»]

SMR

P11884. Positions 26-519.

ModBase

Search...

Protein-protein interaction databases

STRING

P11884.

Proteomic databases

PRIDE

P11884.

Genome annotation databases

Ensembl

ENSRNOT00000001816; ENSRNOP00000001816; ENSRNOG00000001344; Rattus norvegicus. [Genome view]

GeneID

29539.

KEGG

rno:29539.

Organism-specific databases

CTD

29539.

RGD

69219. Aldh2.

Phylogenomic databases

HOVERGEN

P11884.

Enzyme and pathway databases

BRENDA

1.2.1.3. 248.

Gene expression databases

ArrayExpress

P11884.

Genevestigator

P11884.

GermOnline

ENSRNOG00000001344. Rattus norvegicus.

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

609531.

Hide | Top

Entry information

Entry name

ALDH2_RAT

Accession

Primary (citable) accession number: P11884
Secondary accession number(s): Q6Q288

Q91ZD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	October 13, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families