ID   ALDH2_MOUSE             Reviewed;         519 AA.
AC   P47738;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 80.
DE   RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=AHD-M1;
DE   AltName: Full=ALDHI;
DE   AltName: Full=ALDH-E2;
DE   Flags: Precursor;
GN   Name=Aldh2; Synonyms=Ahd-1, Ahd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=95047445; PubMed=7958964; DOI=10.1016/0378-1119(94)90708-0;
RA   Chang C., Yoshida A.;
RT   "Cloning and characterization of the gene encoding mouse mitochondrial
RT   aldehyde dehydrogenase.";
RL   Gene 148:331-336(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94335908; PubMed=8058062;
RA   Chen M., Achkar C., Gudas L.J.;
RT   "Enzymatic conversion of retinaldehyde to retinoic acid by cloned
RT   murine cytosolic and mitochondrial aldehyde dehydrogenases.";
RL   Mol. Pharmacol. 46:88-96(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 54-80; 87-96; 162-174; 198-228; 260-282; 327-340;
RP   349-370; 386-409; 417-428; 431-438 AND 444-453, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-509.
RX   MEDLINE=95023181; PubMed=7937138; DOI=10.1093/nar/22.20.4132;
RA   Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L.,
RA   Zaballos A.;
RT   "Isolation of genomic DNA fragments corresponding to genes modulated
RT   in vivo by a transcription factor.";
RL   Nucleic Acids Res. 22:4132-4138(1994).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-370, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Is capable of converting retinaldehyde to retinoic acid.
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: step 2/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- INDUCTION: By retinoic acid; 3-5 fold increase.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; U07235; AAA64636.1; -; mRNA.
DR   EMBL; S71509; AAC60691.1; -; mRNA.
DR   EMBL; BC005476; AAH05476.1; -; mRNA.
DR   EMBL; Z32545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00111218; -.
DR   PIR; I48966; I48966.
DR   RefSeq; NP_033786.1; -.
DR   UniGene; Mm.284446; -.
DR   HSSP; P05091; 1O01.
DR   SMR; P47738; 26-519.
DR   PhosphoSite; P47738; -.
DR   SWISS-2DPAGE; P47738; -.
DR   REPRODUCTION-2DPAGE; P47738; -.
DR   PRIDE; P47738; -.
DR   Ensembl; ENSMUSG00000029455; Mus musculus.
DR   GeneID; 11669; -.
DR   KEGG; mmu:11669; -.
DR   MGI; MGI:99600; Aldh2.
DR   HOGENOM; P47738; -.
DR   HOVERGEN; P47738; -.
DR   OMA; P47738; PFDSQTE.
DR   BRENDA; 1.2.1.3; 244.
DR   NextBio; 279291; -.
DR   ArrayExpress; P47738; -.
DR   Bgee; P47738; -.
DR   CleanEx; MM_ALDH2; -.
DR   GermOnline; ENSMUSG00000029455; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Mitochondrion; NAD;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     19       Mitochondrion (By similarity).
FT   CHAIN        20    519       Aldehyde dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007169.
FT   NP_BIND     264    269       NAD (By similarity).
FT   ACT_SITE    287    287       Proton acceptor (By similarity).
FT   ACT_SITE    321    321       Nucleophile (By similarity).
FT   SITE        188    188       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES      20     20       N-acetylserine (Probable).
FT   MOD_RES     370    370       N6-acetyllysine.
FT   CONFLICT     88     89       AF -> C (in Ref. 2; AAC60691).
FT   CONFLICT    181    181       Missing (in Ref. 2; AAC60691).
FT   CONFLICT    227    227       I -> S (in Ref. 2; AAC60691).
FT   CONFLICT    344    344       R -> G (in Ref. 2; AAC60691).
FT   CONFLICT    370    370       K -> N (in Ref. 2; AAC60691).
FT   CONFLICT    378    378       S -> M (in Ref. 2; AAC60691).
FT   CONFLICT    476    476       D -> V (in Ref. 2; AAC60691).
SQ   SEQUENCE   519 AA;  56538 MW;  200806F63D48F4DA CRC64;
     MLRAALTTVR RGPRLSRLLS AAATSAVPAP NHQPEVFCNQ IFINNEWHDA VSRKTFPTVN
     PSTGEVICQV AEGNKEDVDK AVKAARAAFQ LGSPWRRMDA SDRGRLLYRL ADLIERDRTY
     LAALETLDNG KPYVISYLVD LDMVLKCLRY YAGWADKYHG KTIPIDGDFF SYTRHEPVGV
     CGQIIPWNFP LLMQAWKLGP ALATGNVVVM KVAEQTPLTA LYVANLIKEA GFPPGVVNIV
     PGFGPTAGAA IASHEGVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA
     DMDWAVEQAH FALFFNQGQC CCAGSRTFVQ ENVYDEFVER SVARAKSRVV GNPFDSRTEQ
     GPQVDETQFK KILGYIKSGQ QEGAKLLCGG GAAADRGYFI QPTVFGDVKD GMTIAKEEIF
     GPVMQILKFK TIEEVVGRAN DSKYGLAAAV FTKDLDKANY LSQALQAGTV WINCYDVFGA
     QSPFGGYKMS GSGRELGEYG LQAYTEVKTV TVKVPQKNS
//