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UniProtKB/Swiss-Prot entry P20000


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

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Entry information
Entry name ALDH2_BOVIN
Primary accession number P20000
Secondary accession number Q1LZC6
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on July 1, 2008 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 71)
Name and origin of the protein
Protein name Aldehyde dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.2.1.3
ALDH class 2
ALDHI
ALDH-E2
Gene name
Name: ALDH2
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1016/0003-9861(90)90590-U; PubMed=1689984 [NCBI, ExPASy, EBI, Israel, Japan]
Guan K., Weiner H.;
"Sequence of the precursor of bovine liver mitochondrial aldehyde dehydrogenase as determined from its cDNA, its gene, and its functionality.";
Arch. Biochem. Biophys. 277:351-360(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 92-520.
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).
[4]
PROTEIN SEQUENCE OF 22-34.
TISSUE=Brain;
DOI=10.1016/0006-291X(92)91530-4; PubMed=1449496 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.E., Cho Y.D.;
"Purification and characterization of bovine brain gamma-aminobutyraldehyde dehydrogenase.";
Biochem. Biophys. Res. Commun. 189:450-454(1992).
[5]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
DOI=10.1016/S0969-2126(97)00224-4; PubMed=9195888 [NCBI, ExPASy, EBI, Israel, Japan]
Steinmetz C.G., Xie P., Weiner H., Hurley T.D.;
"Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion.";
Structure 5:701-711(1997).
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
BC116084; AAI16085.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S09030; S09030.
RefSeq NP_001068835.1; -.
UniGene Bt.44041
3D structure databases
PDB
1A4Z; X-ray; 2.75 A; A/B/C/D=22-520.[ExPASy / RCSB / EBI]
1AG8; X-ray; 2.65 A; A/B/C/D=22-520.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A4Z; -.
1AG8; -.
ModBase P20000.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS P20000.
Genome annotation databases
Ensembl ENSBTAG00000008743; Bos taurus. [Contig view]
GeneID 508629; -.
KEGG bta:508629; -.
Phylogenomic databases
HOVERGEN P20000; -.
Other
LinkHub P20000; -.
ProtoNet P20000.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    21  21     Mitochondrion. 
CHAIN   22   520  499     Aldehyde dehydrogenase, mitochondrial. PRO_0000007167
NP_BIND   265   270  6     NAD (By similarity). 
ACT_SITE   288   288        Proton acceptor. 
ACT_SITE   322   322        Nucleophile. 
SITE   189   189  1     Transition state stabilizer. 
MOD_RES   371   371        N6-acetyllysine (By similarity). 
CONFLICT   289   289        L -> I (in Ref. 1 and 3). 
CONFLICT   385   385        A -> L (in Ref. 1 and 3). 
CONFLICT   409   409        V -> L (in Ref. 1 and 3). 
STRAND   41    44  4      
STRAND   47    49  3      
STRAND   56    60  5      
TURN   62    64  3      
STRAND   67    72  6      
HELIX   76    90  15      
HELIX   95    98  4      
HELIX   101   117  17      
HELIX   119   130  12      
HELIX   134   139  6      
HELIX   141   153  13      
TURN   154   158  5      
STRAND   167   178  12      
STRAND   180   185  6      
STRAND   188   190  3      
HELIX   191   204  14      
STRAND   208   213  6      
HELIX   219   231  13      
STRAND   237   243  7      
HELIX   245   253  9      
STRAND   260   265  6      
HELIX   267   279  13      
STRAND   284   288  5      
STRAND   293   297  5      
HELIX   303   315  13      
HELIX   316   319  4      
STRAND   325   331  7      
HELIX   332   348  17      
HELIX   367   383  17      
STRAND   386   389  4      
STRAND   392   394  3      
STRAND   396   398  3      
STRAND   404   408  5      
HELIX   414   417  4      
STRAND   422   431  10      
HELIX   433   441  9      
STRAND   449   452  4      
HELIX   456   465  10      
STRAND   469   474  6      
STRAND   492   494  3      
HELIX   500   503  4      
STRAND   506   514  9      
Sequence information
Length: 520 AA [This is the length of the unprocessed precursor] Molecular weight: 56653 Da [This is the MW of the unprocessed precursor] CRC64: 713FC1EE8F82B2C4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRAVALAAA RLGPRQGRRL LSAATQAVPT PNQQPEVLYN QIFINNEWHD AVSKKTFPTV 

        70         80         90        100        110        120 
NPSTGDVICH VAEGDKADVD RAVKAARAAF QLGSPWRRMD ASERGRLLNR LADLIERDRT 

       130        140        150        160        170        180 
YLAALETLDN GKPYIISYLV DLDMVLKCLR YYAGWADKYH GKTIPIDGDY FSYTRHEPVG 

       190        200        210        220        230        240 
VCGQIIPWNF PLLMQAWKLG PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNV 

       250        260        270        280        290        300 
IPGFGPTAGA AIASHEDVDK VAFTGSTEVG HLIQVAAGKS NLKRVTLELG GKSPNIIMSD 

       310        320        330        340        350        360 
ADMDWAVEQA HFALFFNQGQ CCCAGSRTFV QEDIYAEFVE RSVARAKSRV VGNPFDSRTE 

       370        380        390        400        410        420 
QGPQVDETQF KKVLGYIKSG KEEGAKLLCG GGAAADRGYF IQPTVFGDVQ DGMTIAKEEI 

       430        440        450        460        470        480 
FGPVMQILKF KSMEEVVGRA NNSKYGLAAA VFTKDLDKAN YLSQALQAGT VWVNCYDVFG 

       490        500        510        520 
AQSPFGGYKL SGSGRELGEY GLQAYTEVKT VTVRVPQKNS 

P20000 in FASTA format

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