GenomeNet

Database: UniProt/SWISS-PROT
Entry: ALDH2_RAT
LinkDB: ALDH2_RAT
Original site: ALDH2_RAT 
ID   ALDH2_RAT               Reviewed;         519 AA.
AC   P11884; Q6Q288; Q6Q289; Q6Q290; Q8K3V8; Q91ZD7;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   16-JAN-2019, entry version 167.
DE   RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=ALDH-E2;
DE   AltName: Full=ALDH1;
DE   Flags: Precursor;
GN   Name=Aldh2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2540003; DOI=10.1111/j.1432-1033.1989.tb14616.x;
RA   Farres J., Guan K.-L., Weiner H.;
RT   "Primary structures of rat and bovine liver mitochondrial aldehyde
RT   dehydrogenases deduced from cDNA sequences.";
RL   Eur. J. Biochem. 180:67-74(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-29.
RC   TISSUE=Liver;
RX   PubMed=3342060; DOI=10.1016/0006-291X(88)90740-1;
RA   Farres J., Guan K.-L., Weiner H.;
RT   "Sequence of the signal peptide for rat liver mitochondrial aldehyde
RT   dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 150:1083-1087(1988).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-19.
RC   TISSUE=Liver;
RX   PubMed=1898068; DOI=10.1016/0003-9861(91)90464-T;
RA   Jeng J., Weiner H.;
RT   "Purification and characterization of catalytically active precursor
RT   of rat liver mitochondrial aldehyde dehydrogenase expressed in
RT   Escherichia coli.";
RL   Arch. Biochem. Biophys. 289:214-222(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-519, AND VARIANTS ARG-86 AND LYS-498.
RC   STRAIN=UChA, UChB, and Wistar; TISSUE=Liver;
RX   PubMed=12893989; DOI=10.1097/00008571-200308000-00009;
RA   Sapag A., Tampier L., Valle-Prieto A., Quintanilla M.E., Moncada C.,
RA   Israel Y.;
RT   "Mutations in mitochondrial aldehyde dehydrogenase (ALDH2) change
RT   cofactor affinity and segregate with voluntary alcohol consumption in
RT   rats.";
RL   Pharmacogenetics 13:509-515(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 32-519.
RC   STRAIN=Lewis;
RA   Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.;
RT   "Genomic structure and sequence of the mitochondrial aldehyde
RT   dehydrogenase gene (ALDH2) of the Lewis rat.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-519.
RC   STRAIN=Lewis; TISSUE=Liver;
RA   Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.;
RT   "Genomic structure and sequence of the mitochondrial aldehyde
RT   dehydrogenase gene of the Lewis rat.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PROTEIN SEQUENCE OF 162-174; 198-228; 260-340; 327-340; 358-370;
RP   397-409 AND 495-508, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [9]
RP   PROTEIN SEQUENCE OF 327-340.
RX   PubMed=1699808; DOI=10.1016/0014-5793(90)81088-6;
RA   Diwan J.J., Paliwal R., Kaftan E., Bawa R.;
RT   "A mitochondrial protein fraction catalyzing transport of the K+
RT   analog T1+.";
RL   FEBS Lett. 273:215-218(1990).
RN   [10]
RP   STRUCTURE BY NMR OF 12-22.
RX   PubMed=10721992; DOI=10.1016/S0092-8674(00)80691-1;
RA   Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S.,
RA   Endo T., Kohda D.;
RT   "Structural basis of presequence recognition by the mitochondrial
RT   protein import receptor Tom20.";
RL   Cell 100:551-560(2000).
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.
CC   -!- INTERACTION:
CC       Q02776:TIM50 (xeno); NbExp=3; IntAct=EBI-916402, EBI-30302;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; X14977; CAA33101.1; -; mRNA.
DR   EMBL; BC062081; AAH62081.1; -; mRNA.
DR   EMBL; M19030; AAA40719.1; -; mRNA.
DR   EMBL; AY566467; AAS75813.1; -; mRNA.
DR   EMBL; AY566468; AAS75814.1; -; mRNA.
DR   EMBL; AY566469; AAS75815.1; -; mRNA.
DR   EMBL; AF529165; AAM94394.2; -; mRNA.
DR   EMBL; AY034137; AAK57732.1; -; Genomic_DNA.
DR   PIR; S03564; S03564.
DR   RefSeq; NP_115792.1; NM_032416.1.
DR   UniGene; Rn.101781; -.
DR   PDB; 1OM2; NMR; -; B=12-20.
DR   PDB; 2V1S; X-ray; 2.05 A; H/I/J/K/L/M/N=12-24.
DR   PDB; 2V1T; X-ray; 1.92 A; C/D=12-22.
DR   PDB; 3AWR; X-ray; 2.00 A; C/D=12-20.
DR   PDB; 3AX2; X-ray; 1.90 A; B/D/F/H=12-20.
DR   PDB; 3AX3; X-ray; 2.10 A; B/D/F/H=12-20.
DR   PDB; 3AX5; X-ray; 2.20 A; B/D=12-20.
DR   PDB; 5AZ8; X-ray; 1.70 A; B=12-24.
DR   PDBsum; 1OM2; -.
DR   PDBsum; 2V1S; -.
DR   PDBsum; 2V1T; -.
DR   PDBsum; 3AWR; -.
DR   PDBsum; 3AX2; -.
DR   PDBsum; 3AX3; -.
DR   PDBsum; 3AX5; -.
DR   PDBsum; 5AZ8; -.
DR   ProteinModelPortal; P11884; -.
DR   SMR; P11884; -.
DR   BioGrid; 248173; 2.
DR   IntAct; P11884; 3.
DR   MINT; P11884; -.
DR   STRING; 10116.ENSRNOP00000001816; -.
DR   BindingDB; P11884; -.
DR   ChEMBL; CHEMBL2812; -.
DR   GuidetoPHARMACOLOGY; 2595; -.
DR   CarbonylDB; P11884; -.
DR   iPTMnet; P11884; -.
DR   PhosphoSitePlus; P11884; -.
DR   World-2DPAGE; 0004:P11884; -.
DR   jPOST; P11884; -.
DR   PaxDb; P11884; -.
DR   PRIDE; P11884; -.
DR   GeneID; 29539; -.
DR   KEGG; rno:29539; -.
DR   UCSC; RGD:69219; rat.
DR   CTD; 217; -.
DR   RGD; 69219; Aldh2.
DR   eggNOG; KOG2450; Eukaryota.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   HOVERGEN; HBG000097; -.
DR   InParanoid; P11884; -.
DR   KO; K00128; -.
DR   OrthoDB; 153834at2759; -.
DR   PhylomeDB; P11884; -.
DR   BRENDA; 1.2.1.3; 5301.
DR   BRENDA; 1.2.1.5; 5301.
DR   SABIO-RK; P11884; -.
DR   UniPathway; UPA00780; UER00768.
DR   EvolutionaryTrace; P11884; -.
DR   PRO; PR:P11884; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:RGD.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR   GO; GO:0070404; F:NADH binding; IDA:RGD.
DR   GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR   GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR   GO; GO:0033574; P:response to testosterone; IEP:RGD.
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   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW   Polymorphism; Reference proteome; Transit peptide.
FT   TRANSIT       1     19       Mitochondrion.
FT   CHAIN        20    519       Aldehyde dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007170.
FT   NP_BIND     264    269       NAD. {ECO:0000250}.
FT   ACT_SITE    287    287       Proton acceptor.
FT   ACT_SITE    321    321       Nucleophile.
FT   SITE        188    188       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P20000}.
FT   MOD_RES      54     54       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      75     75       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      80     80       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     161    161       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     370    370       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     377    377       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     385    385       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     409    409       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     428    428       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     430    430       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     443    443       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     453    453       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   VARIANT      86     86       Q -> R (in allele Aldh2*2 and allele
FT                                Aldh2*3; in strains UChA and UChB).
FT                                {ECO:0000269|PubMed:12893989}.
FT   VARIANT     498    498       E -> K (in allele Aldh2*3; in strain
FT                                UChB). {ECO:0000269|PubMed:12893989}.
FT   HELIX        13     15       {ECO:0000244|PDB:2V1T}.
FT   HELIX        16     18       {ECO:0000244|PDB:5AZ8}.
SQ   SEQUENCE   519 AA;  56488 MW;  75C748202F1333E5 CRC64;
     MLRAALSTAR RGPRLSRLLS AAATSAVPAP NQQPEVFCNQ IFINNEWHDA VSKKTFPTVN
     PSTGEVICQV AEGNKEDVDK AVKAAQAAFQ LGSPWRRMDA SDRGRLLYRL ADLIERDRTY
     LAALETLDNG KPYVISYLVD LDMVLKCLRY YAGWADKYHG KTIPIDGDFF SYTRHEPVGV
     CGQIIPWNFP LLMQAWKLGP ALATGNVVVM KVAEQTPLTA LYVANLIKEA GFPPGVVNIV
     PGFGPTAGAA IASHEDVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA
     DMDWAVEQAH FALFFNQGQC CCAGSRTFVQ EDVYDEFVER SVARAKSRVV GNPFDSRTEQ
     GPQVDETQFK KILGYIKSGQ QEGAKLLCGG GAAADRGYFI QPTVFGDVKD GMTIAKEEIF
     GPVMQILKFK TIEEVVGRAN NSKYGLAAAV FTKDLDKANY LSQALQAGTV WINCYDVFGA
     QSPFGGYKMS GSGRELGEYG LQAYTEVKTV TVKVPQKNS
//
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