ID AL1A1_MOUSE Reviewed; 501 AA.
AC P24549; Q7TQJ0; Q811J0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 27-MAR-2024, entry version 203.
DE RecName: Full=Aldehyde dehydrogenase 1A1 {ECO:0000305|PubMed:12851412};
DE EC=1.2.1.19 {ECO:0000305|PubMed:26430123};
DE EC=1.2.1.28 {ECO:0000250|UniProtKB:P00352};
DE EC=1.2.1.3 {ECO:0000269|PubMed:12851412};
DE EC=1.2.1.36 {ECO:0000269|PubMed:12851412};
DE AltName: Full=3-deoxyglucosone dehydrogenase {ECO:0000250|UniProtKB:P00352};
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A1 {ECO:0000312|MGI:MGI:1353450};
DE AltName: Full=Aldehyde dehydrogenase, cytosolic {ECO:0000303|PubMed:2055490};
DE AltName: Full=Retinal dehydrogenase 1 {ECO:0000305|PubMed:12851412};
DE Short=RALDH 1 {ECO:0000305};
DE Short=RalDH1 {ECO:0000305};
GN Name=Aldh1a1 {ECO:0000312|MGI:MGI:1353450}; Synonyms=Ahd-2, Ahd2, Aldh1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Liver;
RX PubMed=2055490; DOI=10.1016/0378-1119(91)90421-7;
RA Rongnoparut P., Weaver S.;
RT "Isolation and characterization of a cytosolic aldehyde dehydrogenase-
RT encoding cDNA from mouse liver.";
RL Gene 101:261-265(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/ReJ, BALB/cJ, and C57BL/6J; TISSUE=Liver;
RX PubMed=7993664; DOI=10.1006/bmmb.1994.1048;
RA Bond S.L., Singh S.M.;
RT "DNA sequence analysis of the cytosolic acetaldehyde dehydrogenase gene
RT (Ahd-2) in mouse strains with variable ethanol preferences.";
RL Biochem. Med. Metab. Biol. 52:155-159(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Liver;
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 [4]
RP PROTEIN SEQUENCE OF 23-52; 140-156; 211-230; 309-320; 330-349; 400-410;
RP 421-435 AND 477-490, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic retina;
RX PubMed=1935685; DOI=10.1242/dev.112.3.693;
RA McCaffery P., Tempst P., Lara G., Drager U.C.;
RT "Aldehyde dehydrogenase is a positional marker in the retina.";
RL Development 112:693-702(1991).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=12851412; DOI=10.1074/jbc.m303709200;
RA Molotkov A., Duester G.;
RT "Genetic evidence that retinaldehyde dehydrogenase Raldh1 (Aldh1a1)
RT functions downstream of alcohol dehydrogenase Adh1 in metabolism of retinol
RT to retinoic acid.";
RL J. Biol. Chem. 278:36085-36090(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17567582; DOI=10.1074/jbc.m702076200;
RA Lassen N., Bateman J.B., Estey T., Kuszak J.R., Nees D.W., Piatigorsky J.,
RA Duester G., Day B.J., Huang J., Hines L.M., Vasiliou V.;
RT "Multiple and additive functions of ALDH3A1 and ALDH1A1: cataract phenotype
RT and ocular oxidative damage in Aldh3a1(-/-)/Aldh1a1(-/-) knock-out mice.";
RL J. Biol. Chem. 282:25668-25676(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26430123; DOI=10.1126/science.aac4690;
RA Kim J.I., Ganesan S., Luo S.X., Wu Y.W., Park E., Huang E.J., Chen L.,
RA Ding J.B.;
RT "Aldehyde dehydrogenase 1a1 mediates a GABA synthesis pathway in midbrain
RT dopaminergic neurons.";
RL Science 350:102-106(2015).
CC -!- FUNCTION: Cytosolic dehydrogenase that catalyzes the irreversible
CC oxidation of a wide range of aldehydes to their corresponding
CC carboxylic acid (PubMed:12851412). Functions downstream of retinol
CC dehydrogenases and catalyzes the oxidation of retinaldehyde into
CC retinoic acid, the second step in the oxidation of retinol/vitamin A
CC into retinoic acid (PubMed:12851412). This pathway is crucial to
CC control the levels of retinol and retinoic acid, two important
CC molecules which excess can be teratogenic and cytotoxic (Probable).
CC Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-
CC hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein
CC adducts and are highly cytotoxic. By participating for instance to the
CC clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium
CC prevents the formation of HNE-protein adducts and lens opacification
CC (PubMed:17567582). Functions also downstream of fructosamine-3-kinase
CC in the fructosamine degradation pathway by catalyzing the oxidation of
CC 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate
CC decomposition, which is itself a potent glycating agent that may react
CC with lysine and arginine side-chains of proteins (By similarity). Has
CC also an aminobutyraldehyde dehydrogenase activity and is probably part
CC of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate
CC in midbrain, thereby playing a role in GABAergic synaptic transmission
CC (PubMed:26430123). {ECO:0000250|UniProtKB:P00352,
CC ECO:0000269|PubMed:12851412, ECO:0000269|PubMed:17567582,
CC ECO:0000269|PubMed:26430123, ECO:0000305|PubMed:12851412}.
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 Evidence={ECO:0000269|PubMed:12851412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000305|PubMed:12851412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000269|PubMed:12851412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC Evidence={ECO:0000269|PubMed:12851412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:42084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78273,
CC ChEBI:CHEBI:78630; Evidence={ECO:0000305|PubMed:12851412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42085;
CC Evidence={ECO:0000305|PubMed:12851412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:47132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16066, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:87435; Evidence={ECO:0000305|PubMed:12851412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47133;
CC Evidence={ECO:0000305|PubMed:12851412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:169952; Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67333;
CC Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000305|PubMed:26430123};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000305|PubMed:26430123};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-
CC gluconate + 2 H(+) + NADH; Xref=Rhea:RHEA:67244, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:57990, ChEBI:CHEBI:60777;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67245;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33190, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:566274; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67253;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate;
CC Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67257;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- ACTIVITY REGULATION: The aminobutyraldehyde dehydrogenase activity is
CC negatively regulated by ethanol in vivo. {ECO:0000269|PubMed:26430123}.
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:12851412}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with PRMT3; the
CC interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity
CC and is independent of the methyltransferase activity of PRMT3 (By
CC similarity). {ECO:0000250|UniProtKB:P00352,
CC ECO:0000250|UniProtKB:P51977}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1935685}.
CC Cell projection, axon {ECO:0000269|PubMed:26430123}.
CC -!- TISSUE SPECIFICITY: Expressed in retina (PubMed:1935685). Expressed in
CC lens and cornea (at protein level) (PubMed:17567582). Expressed by
CC midbrain dopamine neurons (PubMed:26430123).
CC {ECO:0000269|PubMed:17567582, ECO:0000269|PubMed:1935685,
CC ECO:0000269|PubMed:26430123}.
CC -!- PTM: The N-terminus is blocked most probably by acetylation.
CC {ECO:0000250|UniProtKB:P15437}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Aldh1a1, obtained at the expected
CC Mendelian ratio, are viable and fertile without obvious defects in
CC growth or survival (PubMed:12851412). However, they are more sensitive
CC to retinol toxicity and are less efficient at metabolizing excess
CC retinol to retinoic acid/RA (PubMed:12851412). An excess of retinol
CC leads to the accumulation of retinaldehyde in these mice
CC (PubMed:12851412). Enhanced alcohol consumption and preference is also
CC observed in knockout mice (PubMed:26430123). A consistent lenticular
CC opacification is also detected in old mice (PubMed:17567582).
CC {ECO:0000269|PubMed:12851412, ECO:0000269|PubMed:17567582,
CC ECO:0000269|PubMed:26430123}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44729.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M74570; AAA37202.1; -; mRNA.
DR EMBL; M74571; AAA37203.1; -; Genomic_DNA.
DR EMBL; S75713; AAB32754.2; -; mRNA.
DR EMBL; S77047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044729; AAH44729.1; ALT_INIT; mRNA.
DR EMBL; BC054386; AAH54386.1; -; mRNA.
DR CCDS; CCDS29695.1; -.
DR PIR; JQ1004; JQ1004.
DR RefSeq; NP_038495.2; NM_013467.3.
DR PDB; 7YOB; X-ray; 2.89 A; A/B/C/D/E/F/G/H=1-501.
DR PDBsum; 7YOB; -.
DR AlphaFoldDB; P24549; -.
DR SMR; P24549; -.
DR BioGRID; 198063; 6.
DR IntAct; P24549; 1.
DR MINT; P24549; -.
DR STRING; 10090.ENSMUSP00000153410; -.
DR iPTMnet; P24549; -.
DR PhosphoSitePlus; P24549; -.
DR SwissPalm; P24549; -.
DR REPRODUCTION-2DPAGE; IPI00626662; -.
DR REPRODUCTION-2DPAGE; P24549; -.
DR SWISS-2DPAGE; P24549; -.
DR CPTAC; non-CPTAC-3632; -.
DR jPOST; P24549; -.
DR MaxQB; P24549; -.
DR PaxDb; 10090-ENSMUSP00000084918; -.
DR PeptideAtlas; P24549; -.
DR ProteomicsDB; 296160; -.
DR Pumba; P24549; -.
DR DNASU; 11668; -.
DR Ensembl; ENSMUST00000087638.4; ENSMUSP00000084918.4; ENSMUSG00000053279.9.
DR Ensembl; ENSMUST00000225337.3; ENSMUSP00000153410.3; ENSMUSG00000053279.9.
DR GeneID; 11668; -.
DR KEGG; mmu:11668; -.
DR UCSC; uc008gym.1; mouse.
DR AGR; MGI:1353450; -.
DR CTD; 216; -.
DR MGI; MGI:1353450; Aldh1a1.
DR VEuPathDB; HostDB:ENSMUSG00000053279; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000154609; -.
DR HOGENOM; CLU_005391_0_2_1; -.
DR InParanoid; P24549; -.
DR OMA; WNFPLDM; -.
DR OrthoDB; 2291791at2759; -.
DR PhylomeDB; P24549; -.
DR TreeFam; TF300455; -.
DR BRENDA; 1.2.1.36; 3474.
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR Reactome; R-MMU-70350; Fructose catabolism.
DR Reactome; R-MMU-71384; Ethanol oxidation.
DR SABIO-RK; P24549; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 11668; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Aldh1a1; mouse.
DR PRO; PR:P24549; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P24549; Protein.
DR Bgee; ENSMUSG00000053279; Expressed in right lung lobe and 261 other cell types or tissues.
DR ExpressionAtlas; P24549; baseline and differential.
DR Genevisible; P24549; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI.
DR GO; GO:0106373; F:3-deoxyglucosone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; ISO:MGI.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:MGI.
DR GO; GO:0042905; P:9-cis-retinoic acid metabolic process; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IGI:MGI.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; ISS:UniProtKB.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IGI:MGI.
DR GO; GO:0030392; P:fructosamine catabolic process; ISS:UniProtKB.
DR GO; GO:0006001; P:fructose catabolic process; IDA:MGI.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0036438; P:maintenance of lens transparency; ISS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; ISO:MGI.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; ISO:MGI.
DR GO; GO:0042572; P:retinol metabolic process; IMP:MGI.
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:SF140; ALDEHYDE DEHYDROGENASE 1A1; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell projection; Cytoplasm;
KW Direct protein sequencing; Lipid metabolism; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15437"
FT CHAIN 2..501
FT /note="Aldehyde dehydrogenase 1A1"
FT /id="PRO_0000056417"
FT REGION 336..501
FT /note="Mediates interaction with PRMT3"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 167..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 193..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 226..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 246..247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 349..353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 400..402
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P15437"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 495
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT CONFLICT 8
FT /note="A -> R (in Ref. 1; AAA37202/AAA37203)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="T -> S (in Ref. 2; AAB32754)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="H -> Q (in Ref. 2; AAB32754)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="R -> C (in Ref. 1; AAA37202)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="I -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="M -> I (in Ref. 1; AAA37202)"
FT /evidence="ECO:0000305"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:7YOB"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:7YOB"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:7YOB"
FT TURN 297..300
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 473..479
FT /evidence="ECO:0007829|PDB:7YOB"
FT HELIX 480..484
FT /evidence="ECO:0007829|PDB:7YOB"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:7YOB"
SQ SEQUENCE 501 AA; 54468 MW; 0E428151B799BD1D CRC64;
MSSPAQPAVP APLADLKIQH TKIFINNEWH NSVSGKKFPV LNPATEEVIC HVEEGDKADV
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATMEALN GGKVFANAYL
SDLGGCIKAL KYCAGWADKI HGQTIPSDGD IFTYTRREPI GVCGQIIPWN FPMLMFIWKI
GPALSCGNTV VVKPAEQTPL TALHLASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG
QCCVAASRIF VEESVYDEFV KRSVERAKKY VLGNPLTPGI NQGPQIDKEQ HDKILDLIES
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSVDDVIKR
ANNTTYGLAA GLFTKDLDKA ITVSSALQAG VVWVNCYMML SAQCPFGGFK MSGNGRELGE
HGLYEYTELK TVAMKISQKN S
//
