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UniProtKB/Swiss-Prot entry P47738

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

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Entry information
Entry name ALDH2_MOUSE
Primary accession number P47738
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 72)
Name and origin of the protein
Protein name Aldehyde dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.2.1.3
ALDH class 2
AHD-M1
ALDHI
ALDH-E2
Gene name
Name: Aldh2
Synonyms: Ahd-1, Ahd1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
DOI=10.1016/0378-1119(94)90708-0; PubMed=7958964 [NCBI, ExPASy, EBI, Israel, Japan]
Chang C., Yoshida A.;
"Cloning and characterization of the gene encoding mouse mitochondrial aldehyde dehydrogenase.";
Gene 148:331-336(1994).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8058062 [NCBI, ExPASy, EBI, Israel, Japan]
Chen M., Achkar C., Gudas L.J.;
"Enzymatic conversion of retinaldehyde to retinoic acid by cloned murine cytosolic and mitochondrial aldehyde dehydrogenases.";
Mol. Pharmacol. 46:88-96(1994).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary gland;
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).
[4]
 PROTEIN SEQUENCE OF 87-96; 162-174; 198-228; 260-282; 349-357; 397-409; 431-438 AND 444-453, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
 PROTEIN SEQUENCE OF 162-174 AND 397-409, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[6]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-509.
DOI=10.1093/nar/22.20.4132; PubMed=7937138 [NCBI, ExPASy, EBI, Israel, Japan]
Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., Zaballos A.;
"Isolation of genomic DNA fragments corresponding to genes modulated in vivo by a transcription factor.";
Nucleic Acids Res. 22:4132-4138(1994).
[7]
 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-370, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
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
U07235; AAA64636.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S71509; AAC60691.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005476; AAH05476.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z32545; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR I48966; I48966.
RefSeq NP_033786.1; -.
UniGene Mm.284446
3D structure databases
HSSP P05091; 1O01. [HSSP ENTRY / PDB]
SMR P47738; 26-519.
ModBase P47738.
PTM databases
PhosphoSite P47738; -.
2D gel databases
SWISS-2DPAGE P47738; -.
REPRODUCTION-2DPAGE P47738; -.
Organism-specific databases
MGI MGI:99600; Aldh2.
Gene expression databases
ArrayExpress P47738; -.
CleanEx MM_ALDH2; -.
GermOnline ENSMUSG00000029455; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
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 P47738.
Genome annotation databases
Ensembl ENSMUSG00000029455; Mus musculus. [Contig view]
GeneID 11669; -.
KEGG mmu:11669; -.
Phylogenomic databases
HOGENOM P47738; -.
HOVERGEN P47738; -.
Other
SOURCE Aldh2; Mus musculus.
ProtoNet P47738.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    19  19     Mitochondrion (By similarity). 
CHAIN   20   519  500     Aldehyde dehydrogenase, mitochondrial. PRO_0000007169
NP_BIND   264   269  6     NAD (By similarity). 
ACT_SITE   287   287        Proton acceptor (By similarity). 
ACT_SITE   321   321        Nucleophile (By similarity). 
SITE   188   188  1     Transition state stabilizer (By similarity). 
MOD_RES   20    20        N-acetylserine (Probable). 
MOD_RES   370   370        N6-acetyllysine. 
CONFLICT   88    89        AF -> C (in Ref. 2; AAC60691). 
CONFLICT   181   181        Missing (in Ref. 2; AAC60691). 
CONFLICT   227   227        I -> S (in Ref. 2; AAC60691). 
CONFLICT   344   344        R -> G (in Ref. 2; AAC60691). 
CONFLICT   370   370        K -> N (in Ref. 2; AAC60691). 
CONFLICT   378   378        S -> M (in Ref. 2; AAC60691). 
CONFLICT   476   476        D -> V (in Ref. 2; AAC60691). 
Sequence information
Length: 519 AA [This is the length of the unprocessed precursor] Molecular weight: 56538 Da [This is the MW of the unprocessed precursor] CRC64: 200806F63D48F4DA [This is a checksum on the sequence] 
        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
P47738 in FASTA format

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