ALDH2_HUMAN
ID ALDH2_HUMAN Reviewed; 517 AA.
AC P05091; B4DW54; E7EUE5; Q03639; Q6IB13; Q6IV71;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 248.
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=ALDHI;
DE Flags: Precursor;
GN Name=ALDH2; Synonyms=ALDM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=3582651; DOI=10.1016/0014-5793(87)80152-7;
RA Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
RT "Evidence for a signal peptide at the amino-terminal end of human
RT mitochondrial aldehyde dehydrogenase.";
RL FEBS Lett. 215:233-236(1987).
RN [2]
RP ERRATUM OF PUBMED:3582651, AND SEQUENCE REVISION TO N-TERMINUS.
RA Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
RL FEBS Lett. 233:440-440(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=3562250; DOI=10.1093/nar/15.7.3179;
RA Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
RT "Isolation and sequence analysis of a full length cDNA clone coding for
RT human mitochondrial aldehyde dehydrogenase.";
RL Nucleic Acids Res. 15:3179-3179(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2838413; DOI=10.1016/0888-7543(88)90109-7;
RA Hsu L.C., Bendel R.E., Yoshida A.;
RT "Genomic structure of the human mitochondrial aldehyde dehydrogenase
RT gene.";
RL Genomics 2:57-65(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lassen N., Estey T., Vasiliou V.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lymph;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 18-517 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=4065146; DOI=10.1111/j.1432-1033.1985.tb09260.x;
RA Hempel J., Kaiser R., Joernvall H.;
RT "Mitochondrial aldehyde dehydrogenase from human liver. Primary structure,
RT differences in relation to the cytosolic enzyme, and functional
RT correlations.";
RL Eur. J. Biochem. 153:13-28(1985).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 119-517 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=2987944; DOI=10.1073/pnas.82.11.3771;
RA Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A.;
RT "Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 119-517 (ISOFORM 1).
RX PubMed=4015823; DOI=10.1016/0741-8329(85)90024-2;
RA Yoshida A., Ikawa M., Hsu L.C., Tani K.;
RT "Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases.";
RL Alcohol 2:103-106(1985).
RN [13]
RP PROTEIN SEQUENCE OF 160-172 AND 325-338, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [14]
RP PROTEIN SEQUENCE OF 196-226 AND 325-338.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 214-500, AND VARIANT VAL-337.
RC TISSUE=Liver;
RX PubMed=3610592;
RA Agarwal D.P., Goedde H.W.;
RT "Human aldehyde dehydrogenase isozymes and alcohol sensitivity.";
RL Isozymes Curr. Top. Biol. Med. Res. 16:21-48(1987).
RN [16]
RP DESCRIPTION OF ORIGIN OF CONFLICTS BETWEEN THE SEQUENCE DESCRIBED IN
RP PUBMED:4065146 AND DNA SEQUENCES.
RX PubMed=3653404; DOI=10.1016/0014-5793(87)80198-9;
RA Hempel J., Hoeoeg J.-O., Joernvall H.;
RT "Mitochondrial aldehyde dehydrogenase. Homology of putative targeting
RT sequence to that of carbamyl phosphate synthetase I revealed by correlation
RT of cDNA and protein data.";
RL FEBS Lett. 222:95-98(1987).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS).
RX PubMed=10631996; DOI=10.1110/ps.8.12.2784;
RA Ni L., Zhou J., Hurley T.D., Weiner H.;
RT "Human liver mitochondrial aldehyde dehydrogenase: three-dimensional
RT structure and the restoration of solubility and activity of chimeric
RT forms.";
RL Protein Sci. 8:2784-2790(1999).
RN [20]
RP VARIANT LYS-504.
RX PubMed=6582480; DOI=10.1073/pnas.81.1.258;
RA Yoshida A., Huang I.-Y., Ikawa M.;
RT "Molecular abnormality of an inactive aldehyde dehydrogenase variant
RT commonly found in Orientals.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:258-261(1984).
RN [21]
RP VARIANT LYS-496.
RX PubMed=8561277; DOI=10.1111/j.1530-0277.1995.tb01587.x;
RA Novoradovsky A., Tsai S.J., Goldfarb L., Peterson R., Long J.C.,
RA Goldman D.;
RT "Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American
RT Indian populations: detection of new ALDH2 alleles.";
RL Alcohol. Clin. Exp. Res. 19:1105-1110(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05091-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05091-2; Sequence=VSP_046715;
CC -!- POLYMORPHISM: Genetic variation in ALDH2 is responsible for individual
CC differences in responses to drinking alcohol [MIM:610251]. Allele
CC ALDH2*2 is associated with a very high incidence of acute alcohol
CC intoxication in Orientals and South American Indians, as compared to
CC Caucasians. {ECO:0000269|PubMed:8561277}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62825.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA68290.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA68290.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ALDH2ID250.html";
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DR EMBL; X05409; CAA28990.1; -; mRNA.
DR EMBL; Y00109; CAA68290.1; ALT_SEQ; mRNA.
DR EMBL; M20456; AAA51693.1; -; Genomic_DNA.
DR EMBL; M20444; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20445; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20446; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20447; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20448; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20449; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20450; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20451; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20452; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20453; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; M20454; AAA51693.1; JOINED; Genomic_DNA.
DR EMBL; AY621070; AAT41621.1; -; mRNA.
DR EMBL; CR456991; CAG33272.1; -; mRNA.
DR EMBL; AK301375; BAG62916.1; -; mRNA.
DR EMBL; AC002996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC003029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002967; AAH02967.1; -; mRNA.
DR EMBL; BC071839; AAH71839.1; -; mRNA.
DR EMBL; K03001; AAB59500.1; -; mRNA.
DR EMBL; M26760; AAA51694.1; -; mRNA.
DR EMBL; M54931; AAA62825.1; ALT_FRAME; mRNA.
DR CCDS; CCDS55885.1; -. [P05091-2]
DR CCDS; CCDS9155.1; -. [P05091-1]
DR PIR; A29975; DEHUE2.
DR RefSeq; NP_000681.2; NM_000690.3. [P05091-1]
DR RefSeq; NP_001191818.1; NM_001204889.1. [P05091-2]
DR PDB; 1CW3; X-ray; 2.58 A; A/B/C/D/E/F/G/H=24-517.
DR PDB; 1NZW; X-ray; 2.65 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1NZX; X-ray; 2.45 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1NZZ; X-ray; 2.45 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1O00; X-ray; 2.60 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1O01; X-ray; 2.15 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1O02; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1O04; X-ray; 1.42 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1O05; X-ray; 2.25 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 1ZUM; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=18-517.
DR PDB; 2ONM; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=18-517.
DR PDB; 2ONN; X-ray; 2.75 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 2ONO; X-ray; 2.15 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 2ONP; X-ray; 2.00 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 2VLE; X-ray; 2.40 A; A/B/C/D/E/F/G/H=24-517.
DR PDB; 3INJ; X-ray; 1.69 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 3INL; X-ray; 1.86 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 3N80; X-ray; 1.50 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 3N81; X-ray; 1.70 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 3N82; X-ray; 2.25 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 3N83; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 3SZ9; X-ray; 2.10 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 4FQF; X-ray; 2.28 A; A/B/C/D=18-517.
DR PDB; 4FR8; X-ray; 2.20 A; A/B/C/D/E/F/G/H=18-517.
DR PDB; 4KWF; X-ray; 2.31 A; A/B/C/D/E/F/G/H=24-517.
DR PDB; 4KWG; X-ray; 2.10 A; A/B/C/D/E/F/G/H=24-517.
DR PDB; 5L13; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-517.
DR PDBsum; 1CW3; -.
DR PDBsum; 1NZW; -.
DR PDBsum; 1NZX; -.
DR PDBsum; 1NZZ; -.
DR PDBsum; 1O00; -.
DR PDBsum; 1O01; -.
DR PDBsum; 1O02; -.
DR PDBsum; 1O04; -.
DR PDBsum; 1O05; -.
DR PDBsum; 1ZUM; -.
DR PDBsum; 2ONM; -.
DR PDBsum; 2ONN; -.
DR PDBsum; 2ONO; -.
DR PDBsum; 2ONP; -.
DR PDBsum; 2VLE; -.
DR PDBsum; 3INJ; -.
DR PDBsum; 3INL; -.
DR PDBsum; 3N80; -.
DR PDBsum; 3N81; -.
DR PDBsum; 3N82; -.
DR PDBsum; 3N83; -.
DR PDBsum; 3SZ9; -.
DR PDBsum; 4FQF; -.
DR PDBsum; 4FR8; -.
DR PDBsum; 4KWF; -.
DR PDBsum; 4KWG; -.
DR PDBsum; 5L13; -.
DR AlphaFoldDB; P05091; -.
DR SMR; P05091; -.
DR BioGRID; 106719; 121.
DR DIP; DIP-40262N; -.
DR IntAct; P05091; 54.
DR MINT; P05091; -.
DR STRING; 9606.ENSP00000261733; -.
DR BindingDB; P05091; -.
DR ChEMBL; CHEMBL1935; -.
DR DrugBank; DB01612; Amyl Nitrite.
DR DrugBank; DB06770; Benzyl alcohol.
DR DrugBank; DB04381; Crotonaldehyde.
DR DrugBank; DB02115; Daidzin.
DR DrugBank; DB00822; Disulfiram.
DR DrugBank; DB00536; Guanidine.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00435; Nitric Oxide.
DR DrugBank; DB00727; Nitroglycerin.
DR DrugBank; DB09117; Paraldehyde.
DR DrugBank; DB06154; Pentaerythritol tetranitrate.
DR DrugBank; DB06207; Silodosin.
DR DrugCentral; P05091; -.
DR GuidetoPHARMACOLOGY; 2595; -.
DR GlyGen; P05091; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P05091; -.
DR PhosphoSitePlus; P05091; -.
DR SwissPalm; P05091; -.
DR BioMuta; ALDH2; -.
DR DMDM; 118504; -.
DR REPRODUCTION-2DPAGE; IPI00006663; -.
DR REPRODUCTION-2DPAGE; P05091; -.
DR UCD-2DPAGE; P05091; -.
DR CPTAC; CPTAC-12; -.
DR CPTAC; CPTAC-13; -.
DR CPTAC; CPTAC-14; -.
DR CPTAC; CPTAC-1594; -.
DR EPD; P05091; -.
DR jPOST; P05091; -.
DR MassIVE; P05091; -.
DR MaxQB; P05091; -.
DR PaxDb; P05091; -.
DR PeptideAtlas; P05091; -.
DR PRIDE; P05091; -.
DR ProteomicsDB; 18413; -.
DR ProteomicsDB; 51788; -. [P05091-1]
DR Antibodypedia; 31130; 677 antibodies from 41 providers.
DR DNASU; 217; -.
DR Ensembl; ENST00000261733.7; ENSP00000261733.2; ENSG00000111275.13. [P05091-1]
DR Ensembl; ENST00000416293.7; ENSP00000403349.3; ENSG00000111275.13. [P05091-2]
DR GeneID; 217; -.
DR KEGG; hsa:217; -.
DR MANE-Select; ENST00000261733.7; ENSP00000261733.2; NM_000690.4; NP_000681.2.
DR UCSC; uc001tst.4; human. [P05091-1]
DR CTD; 217; -.
DR DisGeNET; 217; -.
DR GeneCards; ALDH2; -.
DR HGNC; HGNC:404; ALDH2.
DR HPA; ENSG00000111275; Tissue enhanced (liver).
DR MalaCards; ALDH2; -.
DR MIM; 100650; gene+phenotype.
DR MIM; 610251; phenotype.
DR neXtProt; NX_P05091; -.
DR OpenTargets; ENSG00000111275; -.
DR PharmGKB; PA24696; -.
DR VEuPathDB; HostDB:ENSG00000111275; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000156240; -.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; P05091; -.
DR OMA; HGIGYYP; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; P05091; -.
DR TreeFam; TF300455; -.
DR BioCyc; MetaCyc:MON66-302; -.
DR BRENDA; 1.2.1.3; 2681.
DR PathwayCommons; P05091; -.
DR Reactome; R-HSA-380612; Metabolism of serotonin.
DR Reactome; R-HSA-71384; Ethanol oxidation.
DR SABIO-RK; P05091; -.
DR SignaLink; P05091; -.
DR UniPathway; UPA00780; UER00768.
DR BioGRID-ORCS; 217; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; ALDH2; human.
DR EvolutionaryTrace; P05091; -.
DR GeneWiki; ALDH2; -.
DR GenomeRNAi; 217; -.
DR Pharos; P05091; Tclin.
DR PRO; PR:P05091; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P05091; protein.
DR Bgee; ENSG00000111275; Expressed in right lobe of liver and 206 other tissues.
DR ExpressionAtlas; P05091; baseline and differential.
DR Genevisible; P05091; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; TAS:ProtInc.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR GO; GO:0018547; F:nitroglycerin reductase activity; IDA:UniProtKB.
DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0006066; P:alcohol metabolic process; TAS:ProtInc.
DR GO; GO:0046185; P:aldehyde catabolic process; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1903179; P:regulation of dopamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905627; P:regulation of serotonin biosynthetic process; ISS:UniProtKB.
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; Alternative splicing; Direct protein sequencing;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT CHAIN 18..517
FT /note="Aldehyde dehydrogenase, mitochondrial"
FT /id="PRO_0000007168"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT ACT_SITE 319
FT /note="Nucleophile"
FT BINDING 262..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 159
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 368
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 383
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 428
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT VAR_SEQ 74..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046715"
FT VARIANT 337
FT /note="E -> V (in dbSNP:rs1062136)"
FT /evidence="ECO:0000269|PubMed:3610592"
FT /id="VAR_011869"
FT VARIANT 496
FT /note="E -> K (in allele ALDH2*3; dbSNP:rs769724893)"
FT /evidence="ECO:0000269|PubMed:8561277"
FT /id="VAR_011302"
FT VARIANT 504
FT /note="E -> K (in allele ALDH2*2; drastic reduction of
FT enzyme activity; dbSNP:rs671)"
FT /evidence="ECO:0000269|PubMed:6582480"
FT /id="VAR_002248"
FT CONFLICT 7..12
FT /note="RFGPRL -> ARAPP (in Ref. 1; CAA28990)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="S -> A (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="S -> F (in Ref. 6; CAG33272)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..85
FT /note="VKAARA -> REGRPG (in Ref. 1; CAA28990)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> S (in Ref. 1; CAA28990)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="R -> Q (in Ref. 5; AAT41621)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="L -> S (in Ref. 15; AAA62825)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> R (in Ref. 15; AAA62825)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="A -> P (in Ref. 15; AAA62825)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="Y -> C (in Ref. 7; BAG62916)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="V -> L (in Ref. 6; CAG33272)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="E -> Q (in Ref. 4; AAA51693)"
FT /evidence="ECO:0000305"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1O04"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:1O04"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 164..175
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4KWF"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1O04"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 364..379
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:3INL"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 419..427
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:3INL"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:2ONO"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1O04"
FT HELIX 496..502
FT /evidence="ECO:0007829|PDB:1O04"
FT STRAND 503..511
FT /evidence="ECO:0007829|PDB:1O04"
SQ SEQUENCE 517 AA; 56381 MW; E8F74D44D285A00E CRC64;
MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS RKTFPTVNPS
TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH RGRLLNRLAD LIERDRTYLA
ALETLDNGKP YVISYLVDLD MVLKCLRYYA GWADKYHGKT IPIDGDFFSY TRHEPVGVCG
QIIPWNFPLL MQAWKLGPAL ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG
FGPTAGAAIA SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM
DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN PFDSKTEQGP
QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP TVFGDVQDGM TIAKEEIFGP
VMQILKFKTI EEVVGRANNS TYGLAAAVFT KDLDKANYLS QALQAGTVWV NCYDVFGAQS
PFGGYKMSGS GRELGEYGLQ AYTEVKTVTV KVPQKNS
