ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P11884


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ALDH2_RAT
Primary accession number P11884
Secondary accession numbers Q6Q288 Q6Q289 Q6Q290 Q8K3V8 Q91ZD7
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 87)
Name and origin of the protein
Protein name Aldehyde dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.2.1.3
ALDH class 2
ALDH1
ALDH-E2
Gene name
Name: Aldh2
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
PubMed=2540003 [NCBI, ExPASy, EBI, Israel, Japan]
Farres J., Guan K.-L., Weiner H.;
"Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences.";
Eur. J. Biochem. 180:67-74(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-29.
TISSUE=Liver;
DOI=10.1016/0006-291X(88)90740-1; PubMed=3342060 [NCBI, ExPASy, EBI, Israel, Japan]
Farres J., Guan K.-L., Weiner H.;
"Sequence of the signal peptide for rat liver mitochondrial aldehyde dehydrogenase.";
Biochem. Biophys. Res. Commun. 150:1083-1087(1988).
[4]
PROTEIN SEQUENCE OF 1-19.
TISSUE=Liver;
DOI=10.1016/0003-9861(91)90464-T; PubMed=1898068 [NCBI, ExPASy, EBI, Israel, Japan]
Jeng J., Weiner H.;
"Purification and characterization of catalytically active precursor of rat liver mitochondrial aldehyde dehydrogenase expressed in Escherichia coli.";
Arch. Biochem. Biophys. 289:214-222(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-519, AND VARIANTS ARG-86 AND LYS-498.
STRAIN=UChA, UChB, and Wistar;
TISSUE=Liver;
DOI=10.1097/00008571-200308000-00009; PubMed=12893989 [NCBI, ExPASy, EBI, Israel, Japan]
Sapag A., Tampier L., Valle-Prieto A., Quintanilla M.E., Moncada C., Israel Y.;
"Mutations in mitochondrial aldehyde dehydrogenase (ALDH2) change cofactor affinity and segregate with voluntary alcohol consumption in rats.";
Pharmacogenetics 13:509-515(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-519.
STRAIN=Lewis;
Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.;
"Genomic structure and sequence of the mitochondrial aldehyde dehydrogenase gene (ALDH2) of the Lewis rat.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-519.
STRAIN=Lewis;
TISSUE=Liver;
Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.;
"Genomic structure and sequence of the mitochondrial aldehyde dehydrogenase gene of the Lewis rat.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 162-174; 27-340 AND 397-409, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 327-340.
DOI=10.1016/0014-5793(90)81088-6; PubMed=1699808 [NCBI, ExPASy, EBI, Israel, Japan]
Diwan J.J., Paliwal R., Kaftan E., Bawa R.;
"A mitochondrial protein fraction catalyzing transport of the K+ analog T1+.";
FEBS Lett. 273:215-218(1990).
[10]
STRUCTURE BY NMR OF 12-22.
DOI=10.1016/S0092-8674(00)80691-1; PubMed=10721992 [NCBI, ExPASy, EBI, Israel, Japan]
Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S., Endo T., Kohda D.;
"Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.";
Cell 100:551-560(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X14977; CAA33101.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062081; AAH62081.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19030; AAA40719.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY566467; AAS75813.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY566468; AAS75814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY566469; AAS75815.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF529165; AAM94394.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY034137; AAK57732.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S03564; S03564.
RefSeq NP_115792.1; -.
UniGene Rn.101781
3D structure databases
PDB
1OM2; NMR; -; B=12-22.[ExPASy / RCSB / EBI]
2V1S; X-ray; 2.05 A; H/I/J/K/L/M/N=12-24.[ExPASy / RCSB / EBI]
2V1T; X-ray; 1.92 A; C/D=12-22.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1OM2; -.
2V1S; -.
2V1T; -.
SMR P11884; 26-519.
ModBase P11884.
Protein-protein interaction databases
IntAct P11884; -.
Organism-specific databases
RGD 69219; Aldh2.
Gene expression databases
ArrayExpress P11884; -.
GermOnline ENSRNOG00000001344; Rattus norvegicus.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS P11884.
Genome annotation databases
Ensembl ENSRNOG00000001344; Rattus norvegicus. [Contig view]
GeneID 29539; -.
KEGG rno:29539; -.
Phylogenomic databases
HOVERGEN P11884; -.
Other
ProtoNet P11884.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Polymorphism; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    19  19     Mitochondrion. 
CHAIN   20   519  500     Aldehyde dehydrogenase, mitochondrial. PRO_0000007170
NP_BIND   264   269  6     NAD (By similarity). 
ACT_SITE   287   287        Proton acceptor. 
ACT_SITE   321   321        Nucleophile. 
SITE   188   188  1     Transition state stabilizer. 
MOD_RES   20    20        N-acetylserine (Probable). 
MOD_RES   370   370        N6-acetyllysine (By similarity). 
VARIANT   86    86  1     Q -> R (in allele Aldh2*2 and allele Aldh2*3; in strains UChA and UChB). 
VARIANT   498   498  1     E -> K (in allele Aldh2*3; in strain UChB). 
HELIX   15    21  7      
Sequence information
Length: 519 AA [This is the length of the unprocessed precursor] Molecular weight: 56488 Da [This is the MW of the unprocessed precursor] CRC64: 75C748202F1333E5 [This is a checksum on the sequence]
        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 

P11884 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!