AL1A1_RAT
ID AL1A1_RAT Reviewed; 501 AA.
AC P51647; O09184;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Aldehyde dehydrogenase 1A1 {ECO:0000305|PubMed:7832787};
DE EC=1.2.1.19 {ECO:0000250|UniProtKB:P24549};
DE EC=1.2.1.28 {ECO:0000250|UniProtKB:P00352};
DE EC=1.2.1.3 {ECO:0000269|PubMed:7832787};
DE EC=1.2.1.36 {ECO:0000269|PubMed:7832787};
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|RGD:2087};
DE AltName: Full=Aldehyde dehydrogenase, cytosolic {ECO:0000303|PubMed:8543180};
DE AltName: Full=Retinal dehydrogenase 1 {ECO:0000305};
DE Short=RALDH 1 {ECO:0000303|PubMed:9218716};
DE Short=RalDH1 {ECO:0000303|PubMed:9218716};
GN Name=Aldh1a1 {ECO:0000312|RGD:2087};
GN Synonyms=Aldh {ECO:0000303|PubMed:8543180};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8543180; DOI=10.1016/0378-1119(96)81752-5;
RA Bhat P.V., Labrecque J., Boutin J.-M., Lacroix A., Yoshida A.;
RT "Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity
RT for retinal oxidation.";
RL Gene 166:303-306(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9059608; DOI=10.1007/978-1-4615-5871-2_9;
RA Kathmann E.C., Lipsky J.J.;
RT "A preliminary report on the cloning of a constitutively expressed rat
RT liver cytosolic ALDH cDNA by PCR.";
RL Adv. Exp. Med. Biol. 414:69-72(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9240474; DOI=10.1006/bbrc.1997.6998;
RA Kathmann E.C., Lipsky J.J.;
RT "Cloning of a cDNA encoding a constitutively expressed rat liver cytosolic
RT aldehyde dehydrogenase.";
RL Biochem. Biophys. Res. Commun. 236:527-531(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9218716; DOI=10.1016/s0378-1119(97)00054-1;
RA Penzes P., Wang X., Sperkova Z., Napoli J.L.;
RT "Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I and
RT its expression in E. coli.";
RL Gene 191:167-172(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [6]
RP PROTEIN SEQUENCE OF 2-19; 80-91; 96-121; 205-225; 237-258 AND 394-438,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=7832787; DOI=10.1042/bj3050681;
RA Labrecque J., Dumas F., Lacroix A., Bhat P.V.;
RT "A novel isoenzyme of aldehyde dehydrogenase specifically involved in the
RT biosynthesis of 9-cis and all-trans retinoic acid.";
RL Biochem. J. 305:681-684(1995).
RN [7]
RP FUNCTION.
RX PubMed=15623782; DOI=10.1167/iovs.04-0120;
RA Choudhary S., Xiao T., Vergara L.A., Srivastava S., Nees D.,
RA Piatigorsky J., Ansari N.H.;
RT "Role of aldehyde dehydrogenase isozymes in the defense of rat lens and
RT human lens epithelial cells against oxidative stress.";
RL Invest. Ophthalmol. Vis. Sci. 46:259-267(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cytosolic dehydrogenase that catalyzes the irreversible
CC oxidation of a wide range of aldehydes to their corresponding
CC carboxylic acid (PubMed:7832787, PubMed:15623782). Functions downstream
CC of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde
CC into retinoic acid, the second step in the oxidation of retinol/vitamin
CC A into retinoic acid. This pathway is crucial to control the levels of
CC retinol and retinoic acid, two important molecules which excess can be
CC teratogenic and cytotoxic (PubMed:7832787). Also oxidizes aldehydes
CC resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE,
CC malonaldehyde and hexanal that form protein adducts and are highly
CC cytotoxic. By participating for instance to the clearance of (E)-4-
CC hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of
CC HNE-protein adducts and lens opacification (PubMed:15623782). Functions
CC also downstream of fructosamine-3-kinase in the fructosamine
CC degradation pathway by catalyzing the oxidation of 3-deoxyglucosone,
CC the carbohydrate product of fructosamine 3-phosphate decomposition,
CC which is itself a potent glycating agent that may react with lysine and
CC arginine side-chains of proteins (By similarity). Has also an
CC aminobutyraldehyde dehydrogenase activity and is probably part of an
CC alternative pathway for the biosynthesis of GABA/4-aminobutanoate in
CC midbrain, thereby playing a role in GABAergic synaptic transmission (By
CC similarity). {ECO:0000250|UniProtKB:P00352,
CC ECO:0000250|UniProtKB:P24549, ECO:0000269|PubMed:15623782,
CC ECO:0000269|PubMed:7832787}.
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; Evidence={ECO:0000269|PubMed:7832787};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000305|PubMed:7832787};
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:7832787};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC Evidence={ECO:0000305|PubMed:7832787};
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:0000269|PubMed:7832787};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42085;
CC Evidence={ECO:0000305|PubMed:7832787};
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:0000269|PubMed:7832787};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47133;
CC Evidence={ECO:0000305|PubMed:7832787};
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=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 -!- 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:0000250|UniProtKB:P24549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000250|UniProtKB:P24549};
CC -!- ACTIVITY REGULATION: Inhibited by chloral hydrate.
CC {ECO:0000269|PubMed:7832787}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.7 uM for 9-cis retinal (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:7832787};
CC KM=9.8 uM for all-trans retinal (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:7832787};
CC KM=10.5 uM for 11-cis retinal (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:7832787};
CC Note=Has more than 2-fold higher catalytic efficiency for 9-cis
CC retinal compared to all-trans retinal and 11-cis retinal.
CC {ECO:0000269|PubMed:7832787};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:7832787}.
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
CC {ECO:0000250|UniProtKB:P00352}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P24549}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in kidney, lung, testis,
CC intestine, stomach, and trachea, but weakly in the liver.
CC {ECO:0000269|PubMed:8543180}.
CC -!- PTM: The N-terminus is blocked most probably by acetylation.
CC {ECO:0000305|PubMed:7832787}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; L42009; AAA96657.1; -; mRNA.
DR EMBL; AF001896; AAC53304.1; -; mRNA.
DR EMBL; AF001898; AAC53306.1; -; mRNA.
DR EMBL; AF001897; AAC53305.1; -; mRNA.
DR EMBL; U79118; AAB63423.1; -; mRNA.
DR EMBL; BC061526; AAH61526.1; -; mRNA.
DR PIR; JC4524; JC4524.
DR PIR; JC5553; JC5553.
DR RefSeq; NP_071852.2; NM_022407.3.
DR AlphaFoldDB; P51647; -.
DR SMR; P51647; -.
DR STRING; 10116.ENSRNOP00000024000; -.
DR BindingDB; P51647; -.
DR ChEMBL; CHEMBL2931; -.
DR SwissLipids; SLP:000000800; -.
DR iPTMnet; P51647; -.
DR PhosphoSitePlus; P51647; -.
DR jPOST; P51647; -.
DR PaxDb; P51647; -.
DR PRIDE; P51647; -.
DR GeneID; 24188; -.
DR KEGG; rno:24188; -.
DR UCSC; RGD:2087; rat.
DR CTD; 216; -.
DR RGD; 2087; Aldh1a1.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_2_1; -.
DR InParanoid; P51647; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; P51647; -.
DR TreeFam; TF300455; -.
DR BRENDA; 1.2.1.36; 5301.
DR Reactome; R-RNO-5365859; RA biosynthesis pathway.
DR Reactome; R-RNO-70350; Fructose catabolism.
DR Reactome; R-RNO-71384; Ethanol oxidation.
DR SABIO-RK; P51647; -.
DR UniPathway; UPA00912; -.
DR PRO; PR:P51647; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P51647; RN.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISO:RGD.
DR GO; GO:0106373; F:3-deoxyglucosone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; ISO:RGD.
DR GO; GO:0042905; P:9-cis-retinoic acid metabolic process; IDA:RGD.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IMP:UniProtKB.
DR GO; GO:0048048; P:embryonic eye morphogenesis; ISO:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0030392; P:fructosamine catabolic process; ISS:UniProtKB.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0036438; P:maintenance of lens transparency; IMP:UniProtKB.
DR GO; GO:0007494; P:midgut development; IEP:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IMP:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; ISO: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 Acetylation; Cell projection; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15437,
FT ECO:0000269|PubMed:7832787"
FT CHAIN 2..501
FT /note="Aldehyde dehydrogenase 1A1"
FT /id="PRO_0000056419"
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:0007744|PubMed:22673903"
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 100
FT /note="R -> C (in Ref. 1; AAA96657)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="I -> M (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="N -> E (in Ref. 1; AAA96657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 54459 MW; A3614C21BCE7E144 CRC64;
MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSGKKFPV LNPATEEVIC HVEEGDKADV
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATIEAIN GGKVFANAYL
SDLGGSIKAL KYCAGWADKI HGQTIPSDGD IFTFTRREPI GVCGQIIPWN FPLLMFIWKI
GPALSCGNTV VVKPAEQTPL TALHMASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG
QCCVAASRIF VEESVYDEFV RKSVERAKKY VLGNPLTQGI NQGPQIDKEQ HDKILDLIES
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSIDDVIKR
ANNTTYGLAA GVFTKDLDRA ITVSSALQAG VVWVNCYMIL SAQCPFGGFK MSGNGRELGE
HGLYEYTELK TVAMKISQKN S
