ID   AL1B1_MOUSE             Reviewed;         519 AA.
AC   Q9CZS1; Q3UAH5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Aldehyde dehydrogenase X, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=Aldehyde dehydrogenase family 1 member B1;
DE   Flags: Precursor;
GN   Name=Aldh1b1; Synonyms=Aldhx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, 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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-83; LYS-366; LYS-385;
RP   LYS-401; LYS-416 AND LYS-428, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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., Zhang Y.,
RA   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   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-54; LYS-366; LYS-385;
RP   LYS-401; LYS-416; LYS-428 AND LYS-431, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE 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., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: ALDHs play a major role in the detoxification of alcohol-
CC       derived acetaldehyde. They are involved in the metabolism of
CC       corticosteroids, biogenic amines, neurotransmitters, and lipid
CC       peroxidation (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AK012213; BAB28101.1; -; mRNA.
DR   EMBL; AK088396; BAC40326.1; -; mRNA.
DR   EMBL; AK150992; BAE30016.1; -; mRNA.
DR   EMBL; AK151349; BAE30325.1; -; mRNA.
DR   EMBL; AK151364; BAE30339.1; -; mRNA.
DR   EMBL; AK153416; BAE31976.1; -; mRNA.
DR   EMBL; BC020001; AAH20001.1; -; mRNA.
DR   EMBL; BC086768; AAH86768.1; -; mRNA.
DR   CCDS; CCDS18139.1; -.
DR   RefSeq; NP_082546.1; NM_028270.4.
DR   AlphaFoldDB; Q9CZS1; -.
DR   SMR; Q9CZS1; -.
DR   BioGRID; 215422; 13.
DR   IntAct; Q9CZS1; 2.
DR   STRING; 10090.ENSMUSP00000041260; -.
DR   GlyGen; Q9CZS1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CZS1; -.
DR   PhosphoSitePlus; Q9CZS1; -.
DR   SwissPalm; Q9CZS1; -.
DR   EPD; Q9CZS1; -.
DR   jPOST; Q9CZS1; -.
DR   MaxQB; Q9CZS1; -.
DR   PaxDb; 10090-ENSMUSP00000041260; -.
DR   PeptideAtlas; Q9CZS1; -.
DR   ProteomicsDB; 296090; -.
DR   Antibodypedia; 12074; 334 antibodies from 35 providers.
DR   DNASU; 72535; -.
DR   Ensembl; ENSMUST00000044384.5; ENSMUSP00000041260.5; ENSMUSG00000035561.6.
DR   GeneID; 72535; -.
DR   KEGG; mmu:72535; -.
DR   UCSC; uc008ssx.1; mouse.
DR   AGR; MGI:1919785; -.
DR   CTD; 219; -.
DR   MGI; MGI:1919785; Aldh1b1.
DR   VEuPathDB; HostDB:ENSMUSG00000035561; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   GeneTree; ENSGT00940000162530; -.
DR   HOGENOM; CLU_005391_0_1_1; -.
DR   InParanoid; Q9CZS1; -.
DR   OMA; WVNRYGR; -.
DR   OrthoDB; 2291791at2759; -.
DR   PhylomeDB; Q9CZS1; -.
DR   TreeFam; TF300455; -.
DR   BRENDA; 1.2.1.3; 3474.
DR   Reactome; R-MMU-71384; Ethanol oxidation.
DR   UniPathway; UPA00780; UER00768.
DR   BioGRID-ORCS; 72535; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Aldh1b1; mouse.
DR   PRO; PR:Q9CZS1; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9CZS1; Protein.
DR   Bgee; ENSMUSG00000035561; Expressed in crypt of Lieberkuhn of small intestine and 115 other cell types or tissues.
DR   ExpressionAtlas; Q9CZS1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07141; ALDH_F1AB_F2_RALDH1; 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   PANTHER; PTHR11699:SF207; ALDEHYDE DEHYDROGENASE X, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   Genevisible; Q9CZS1; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..519
FT                   /note="Aldehyde dehydrogenase X, mitochondrial"
FT                   /id="PRO_0000271411"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         264..269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            188
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         54
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         54
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         83
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         366
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         366
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         385
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         385
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         401
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         401
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         416
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         416
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         428
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         428
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         431
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   CONFLICT        146
FT                   /note="K -> R (in Ref. 1; BAE30339)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        261
FT                   /note="A -> T (in Ref. 1; BAE30339)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   519 AA;  57553 MW;  69222D7409BFEEF3 CRC64;
     MLTARLLLPR LLCLQGRTTS YSTAAALPNP IPNPEICYNK LFINNEWHDA VSKKTFPTVN
     PTTGEVIGHV AEGDRADVDL AVKAAREAFR LGSPWRRMDA SERGRLLNRL ADLVERDRVY
     LASLETLDNG KPFQESYVLD LDEVIKVYRY FAGWADKWHG KTIPMDGEHF CFTRHEPVGV
     CGQIIPWNFP LVMQGWKLAP ALATGNTVVM KVAEQTPLSA LYLASLIKEA GFPPGVVNII
     TGYGPTAGAA IAQHMDVDKV AFTGSTEVGH LIQKAAGESN LKRVTLELGG KSPSIVLADA
     DMEHAVDQCH EALFFNMGQC CCAGSRTFVE ESIYREFLER TVEKAKQRKV GNPFELDTQQ
     GPQVDKEQFE RILGYIRLGQ KEGAKLLCGG ERLGERGFFI KPTVFGDVQD GMRIAKEEIF
     GPVQPLFKFK KIEEVIQRAN NTRYGLAAAV FTRDLDKAIY FTQALQAGTV WVNTYNIVTC
     HTPFGGFKES GNGRELGEDG LRAYTEVKTV TIKVPEKNS
//