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Database: UniProt/SWISS-PROT
Entry: ALDH2_MOUSE
LinkDB: ALDH2_MOUSE
Original site: ALDH2_MOUSE 
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   13-FEB-2019, entry version 163.
DE   RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=AHD-M1;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=ALDH-E2;
DE   AltName: Full=ALDHI;
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; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   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   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 IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, 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   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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-75; LYS-80; LYS-161;
RP   LYS-370; LYS-377; LYS-385; LYS-409; LYS-428; LYS-430; LYS-443 AND
RP   LYS-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Is capable of converting retinaldehyde to retinoic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: step 2/2.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8R104:Sirt3; NbExp=2; IntAct=EBI-2308120, EBI-6999888;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- INDUCTION: By retinoic acid; 3-5 fold increase.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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   CCDS; CCDS19638.1; -.
DR   PIR; I48966; I48966.
DR   RefSeq; NP_033786.1; NM_009656.4.
DR   UniGene; Mm.284446; -.
DR   ProteinModelPortal; P47738; -.
DR   SMR; P47738; -.
DR   BioGrid; 198064; 2.
DR   IntAct; P47738; 15.
DR   MINT; P47738; -.
DR   STRING; 10090.ENSMUSP00000031411; -.
DR   iPTMnet; P47738; -.
DR   PhosphoSitePlus; P47738; -.
DR   SwissPalm; P47738; -.
DR   REPRODUCTION-2DPAGE; P47738; -.
DR   SWISS-2DPAGE; P47738; -.
DR   UCD-2DPAGE; P47738; -.
DR   EPD; P47738; -.
DR   jPOST; P47738; -.
DR   PaxDb; P47738; -.
DR   PeptideAtlas; P47738; -.
DR   PRIDE; P47738; -.
DR   Ensembl; ENSMUST00000031411; ENSMUSP00000031411; ENSMUSG00000029455.
DR   GeneID; 11669; -.
DR   KEGG; mmu:11669; -.
DR   UCSC; uc008zjt.1; mouse.
DR   CTD; 217; -.
DR   MGI; MGI:99600; Aldh2.
DR   eggNOG; KOG2450; Eukaryota.
DR   eggNOG; COG1012; LUCA.
DR   GeneTree; ENSGT00940000156240; -.
DR   HOGENOM; HOG000271505; -.
DR   HOVERGEN; HBG000097; -.
DR   InParanoid; P47738; -.
DR   KO; K00128; -.
DR   OMA; TFVQEDV; -.
DR   OrthoDB; 153834at2759; -.
DR   PhylomeDB; P47738; -.
DR   TreeFam; TF300455; -.
DR   BRENDA; 1.2.1.3; 3474.
DR   Reactome; R-MMU-71384; Ethanol oxidation.
DR   UniPathway; UPA00780; UER00768.
DR   ChiTaRS; Aldh2; mouse.
DR   PRO; PR:P47738; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029455; Expressed in 315 organ(s), highest expression level in lung.
DR   ExpressionAtlas; P47738; baseline and differential.
DR   Genevisible; P47738; MM.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; ISO:MGI.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR   GO; GO:0070404; F:NADH binding; ISO:MGI.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Direct protein sequencing;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     19       Mitochondrion. {ECO:0000250}.
FT   CHAIN        20    519       Aldehyde dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007169.
FT   NP_BIND     264    269       NAD. {ECO:0000250}.
FT   ACT_SITE    287    287       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   ACT_SITE    321    321       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   SITE        188    188       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P20000}.
FT   MOD_RES      54     54       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES      75     75       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES      80     80       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     161    161       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     370    370       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     377    377       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     385    385       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     409    409       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     428    428       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     430    430       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753,
FT                                ECO:0000244|PubMed:23806337}.
FT   MOD_RES     443    443       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     453    453       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   CONFLICT     88     89       AF -> C (in Ref. 2; AAC60691).
FT                                {ECO:0000305}.
FT   CONFLICT    181    181       Missing (in Ref. 2; AAC60691).
FT                                {ECO:0000305}.
FT   CONFLICT    227    227       I -> S (in Ref. 2; AAC60691).
FT                                {ECO:0000305}.
FT   CONFLICT    344    344       R -> G (in Ref. 2; AAC60691).
FT                                {ECO:0000305}.
FT   CONFLICT    370    370       K -> N (in Ref. 2; AAC60691).
FT                                {ECO:0000305}.
FT   CONFLICT    378    378       S -> M (in Ref. 2; AAC60691).
FT                                {ECO:0000305}.
FT   CONFLICT    476    476       D -> V (in Ref. 2; AAC60691).
FT                                {ECO:0000305}.
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
//
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