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AL1A1_HUMAN
ID   AL1A1_HUMAN             Reviewed;         501 AA.
AC   P00352; O00768; Q5SYR1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 215.
DE   RecName: Full=Aldehyde dehydrogenase 1A1 {ECO:0000305|PubMed:19296407};
DE            EC=1.2.1.19 {ECO:0000250|UniProtKB:P24549};
DE            EC=1.2.1.28 {ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407};
DE            EC=1.2.1.3 {ECO:0000269|PubMed:12941160, ECO:0000269|PubMed:15623782, ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407};
DE            EC=1.2.1.36 {ECO:0000250|UniProtKB:P51647};
DE   AltName: Full=3-deoxyglucosone dehydrogenase {ECO:0000305|PubMed:17175089};
DE   AltName: Full=ALDH-E1;
DE   AltName: Full=ALHDII;
DE   AltName: Full=Aldehyde dehydrogenase family 1 member A1 {ECO:0000312|HGNC:HGNC:402};
DE   AltName: Full=Aldehyde dehydrogenase, cytosolic {ECO:0000303|PubMed:2591967};
DE   AltName: Full=Retinal dehydrogenase 1 {ECO:0000250|UniProtKB:P51647};
DE            Short=RALDH 1 {ECO:0000250|UniProtKB:P51647};
DE            Short=RalDH1 {ECO:0000250|UniProtKB:P51647};
GN   Name=ALDH1A1 {ECO:0000312|HGNC:HGNC:402};
GN   Synonyms=ALDC, ALDH1 {ECO:0000312|HGNC:HGNC:402},
GN   PUMB1 {ECO:0000312|HGNC:HGNC:402};
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 [GENOMIC DNA].
RX   PubMed=2591967; DOI=10.1016/0888-7543(89)90127-4;
RA   Hsu L.C., Chang W.-C., Yoshida A.;
RT   "Genomic structure of the human cytosolic aldehyde dehydrogenase gene.";
RL   Genomics 5:857-865(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-121.
RC   TISSUE=Liver;
RX   PubMed=8214422; DOI=10.1111/j.1530-0277.1993.tb00849.x;
RA   Zheng C.F., Wang T.T., Weiner H.;
RT   "Cloning and expression of the full-length cDNAs encoding human liver class
RT   1 and class 2 aldehyde dehydrogenase.";
RL   Alcohol. Clin. Exp. Res. 17:828-831(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC   TISSUE=Lens;
RX   PubMed=19296407; DOI=10.1080/15287390802706371;
RA   Xiao T., Shoeb M., Siddiqui M.S., Zhang M., Ramana K.V., Srivastava S.K.,
RA   Vasiliou V., Ansari N.H.;
RT   "Molecular cloning and oxidative modification of human lens ALDH1A1:
RT   implication in impaired detoxification of lipid aldehydes.";
RL   J. Toxicol. Environ. Health Part A 72:577-584(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-177.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX   PubMed=8493914; DOI=10.1007/978-1-4615-2904-0_5;
RA   Yoshida A., Hsu L.C., Yanagawa Y.;
RT   "Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal
RT   response, retinal oxidation and implication in testicular feminization.";
RL   Adv. Exp. Med. Biol. 328:37-44(1993).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-501, AND ACETYLATION AT SER-2.
RC   TISSUE=Liver;
RX   PubMed=6723659; DOI=10.1111/j.1432-1033.1984.tb08150.x;
RA   Hempel J., von Bahr-Lindstroem H., Joernvall H.;
RT   "Aldehyde dehydrogenase from human liver. Primary structure of the
RT   cytoplasmic isoenzyme.";
RL   Eur. J. Biochem. 141:21-35(1984).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
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   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
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   [13]
RP   PROTEIN SEQUENCE OF 266-273, ACTIVE SITE, AND NAD-BINDING.
RX   PubMed=3676276; DOI=10.1021/bi00392a015;
RA   Abriola D.P., Fields R., Stein S., Mackerell A.D. Jr., Pietruszko R.;
RT   "Active site of human liver aldehyde dehydrogenase.";
RL   Biochemistry 26:5679-5684(1987).
RN   [14]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Erythrocyte;
RX   PubMed=2776714; DOI=10.1159/000469006;
RA   Agarwal D.P., Cohn P., Goedde H.W., Hempel J.;
RT   "Aldehyde dehydrogenase from human erythrocytes: structural relationship to
RT   the liver cytosolic isozyme.";
RL   Enzyme 42:47-52(1989).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12941160; DOI=10.1089/104454903322216671;
RA   Manzer R., Qamar L., Estey T., Pappa A., Petersen D.R., Vasiliou V.;
RT   "Molecular cloning and baculovirus expression of the rabbit corneal
RT   aldehyde dehydrogenase (ALDH1A1) cDNA.";
RL   DNA Cell Biol. 22:329-338(2003).
RN   [16]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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   [17]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17175089; DOI=10.1016/j.biochi.2006.11.005;
RA   Collard F., Vertommen D., Fortpied J., Duester G., Van Schaftingen E.;
RT   "Identification of 3-deoxyglucosone dehydrogenase as aldehyde dehydrogenase
RT   1A1 (retinaldehyde dehydrogenase 1).";
RL   Biochimie 89:369-373(2007).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-128; LYS-252; LYS-353;
RP   LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [19]
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   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337 AND SER-413, AND
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   [22]
RP   INTERACTION WITH PRMT3, AND REGION.
RX   PubMed=33495566; DOI=10.1038/s42003-020-01644-3;
RA   Verma M., Khan M.I.K., Kadumuri R.V., Chakrapani B., Awasthi S., Mahesh A.,
RA   Govindaraju G., Chavali P.L., Rajavelu A., Chavali S., Dhayalan A.;
RT   "PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting
RT   retinoic acid signaling.";
RL   Commun. Biol. 4:109-109(2021).
RN   [23] {ECO:0007744|PDB:5AC2}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH DUOCARMYCIN ANALOG,
RP   FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF CYS-302.
RX   PubMed=26373694; DOI=10.1002/anie.201505749;
RA   Koch M.F., Harteis S., Blank I.D., Pestel G., Tietze L.F., Ochsenfeld C.,
RA   Schneider S., Sieber S.A.;
RT   "Structural, biochemical, and computational studies reveal the mechanism of
RT   selective aldehyde dehydrogenase 1A1 inhibition by cytotoxic duocarmycin
RT   analogues.";
RL   Angew. Chem. Int. Ed. Engl. 54:13550-13554(2015).
RN   [24] {ECO:0007744|PDB:4WB9, ECO:0007744|PDB:4WJ9}
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF VARIANT SER-121 ALONE AND IN
RP   COMPLEX WITH NADH, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=25450233; DOI=10.1016/j.cbi.2014.10.028;
RA   Morgan C.A., Hurley T.D.;
RT   "Development of a high-throughput in vitro assay to identify selective
RT   inhibitors for human ALDH1A1.";
RL   Chem. Biol. Interact. 234:29-37(2015).
RN   [25] {ECO:0007744|PDB:4WP7, ECO:0007744|PDB:4WPN, ECO:0007744|PDB:4X4L}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITORS,
RP   AND MUTAGENESIS OF GLY-458.
RX   PubMed=25634381; DOI=10.1021/jm501900s;
RA   Morgan C.A., Hurley T.D.;
RT   "Characterization of two distinct structural classes of selective aldehyde
RT   dehydrogenase 1A1 inhibitors.";
RL   J. Med. Chem. 58:1964-1975(2015).
CC   -!- FUNCTION: Cytosolic dehydrogenase that catalyzes the irreversible
CC       oxidation of a wide range of aldehydes to their corresponding
CC       carboxylic acid (PubMed:19296407, PubMed:12941160, PubMed:15623782,
CC       PubMed:17175089, PubMed:26373694, PubMed:25450233). Functions
CC       downstream of retinol dehydrogenases and catalyzes the oxidation of
CC       retinaldehyde into retinoic acid, the second step in the oxidation of
CC       retinol/vitamin A into retinoic acid (By similarity). This pathway is
CC       crucial to control the levels of retinol and retinoic acid, two
CC       important molecules which excess can be teratogenic and cytotoxic (By
CC       similarity). Also oxidizes aldehydes resulting from lipid peroxidation
CC       like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form
CC       protein adducts and are highly cytotoxic. By participating for instance
CC       to the 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:19296407, PubMed:12941160, PubMed:15623782). Functions also
CC       downstream of fructosamine-3-kinase in the fructosamine degradation
CC       pathway by catalyzing the oxidation of 3-deoxyglucosone, the
CC       carbohydrate product of fructosamine 3-phosphate decomposition, which
CC       is itself a potent glycating agent that may react with lysine and
CC       arginine side-chains of proteins (PubMed:17175089). 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:P24549,
CC       ECO:0000269|PubMed:12941160, ECO:0000269|PubMed:15623782,
CC       ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407,
CC       ECO:0000269|PubMed:25450233, ECO:0000269|PubMed:26373694}.
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:12941160,
CC         ECO:0000269|PubMed:15623782, ECO:0000269|PubMed:17175089,
CC         ECO:0000269|PubMed:19296407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC         Evidence={ECO:0000305|PubMed:19296407};
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:0000250|UniProtKB:P51647};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC         Evidence={ECO:0000250|UniProtKB:P51647};
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:0000250|UniProtKB:P51647};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42085;
CC         Evidence={ECO:0000250|UniProtKB:P51647};
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:0000250|UniProtKB:P51647};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47133;
CC         Evidence={ECO:0000250|UniProtKB:P51647};
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:0000269|PubMed:17175089};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67245;
CC         Evidence={ECO:0000305|PubMed:17175089};
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:0000269|PubMed:12941160, ECO:0000269|PubMed:15623782,
CC         ECO:0000269|PubMed:19296407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC         Evidence={ECO:0000269|PubMed:15623782};
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:0000269|PubMed:12941160,
CC         ECO:0000269|PubMed:19296407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67253;
CC         Evidence={ECO:0000305|PubMed:19296407};
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:0000269|PubMed:12941160};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC         Evidence={ECO:0000305|PubMed:12941160};
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:0000269|PubMed:12941160,
CC         ECO:0000269|PubMed:19296407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67257;
CC         Evidence={ECO:0000305|PubMed:19296407};
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:0000269|PubMed:19296407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295;
CC         Evidence={ECO:0000305|PubMed:19296407};
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:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841;
CC         Evidence={ECO:0000305|PubMed:19296407};
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 citral, disulfiram, and cyanamide.
CC       Activated by diethylstilbestrol (PubMed:19296407). Inhibited by
CC       duocarmycin analogs (PubMed:26373694). {ECO:0000269|PubMed:19296407,
CC       ECO:0000269|PubMed:26373694}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=59.4 uM for NAD (at pH 8.0) {ECO:0000269|PubMed:19296407};
CC         KM=85 uM for NAD (at pH 7.1 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:17175089};
CC         KM=2 uM for benzaldehyde (at pH 7.1 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:17175089};
CC         KM=4.8 uM for (E)-4-hydroxynon-2-enal (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         KM=17.9 uM for (E)-4-hydroxynon-2-enal (at pH 8.0 and 25 degrees
CC         Celsius) {ECO:0000269|PubMed:12941160};
CC         KM=114.4 uM for malonaldehyde (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:12941160};
CC         KM=3.5 uM for malonaldehyde (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         KM=95 uM for 3-deoxyglucosone (at pH 7.1 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:17175089};
CC         KM=238.2 uM for acetaldehyde (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         KM=121.4 uM for propanal (at pH 8.0) {ECO:0000269|PubMed:19296407};
CC         KM=137.2 uM for propanal (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:12941160};
CC         KM=15 uM for propanal (at pH 7.5) {ECO:0000269|PubMed:25450233};
CC         KM=13.4 uM for hexanal (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:12941160};
CC         KM=142.2 uM for benzaldehyde (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         KM=177.1 uM for trans-2-heptenal (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         Vmax=254.6 nmol/min/mg enzyme with (E)-4-hydroxynon-2-enal (at pH 8.0
CC         and 25 degrees Celsius) {ECO:0000269|PubMed:12941160};
CC         Vmax=135 nmol/min/mg enzyme with (E)-4-hydroxynon-2-enal (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         Vmax=564.9 nmol/min/mg enzyme with malonaldehyde (at pH 8.0 and 25
CC         degrees Celsius) {ECO:0000269|PubMed:12941160};
CC         Vmax=381.6 nmol/min/mg enzyme with malonaldehyde (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         Vmax=45 nmol/min/mg enzyme with 3-deoxyglucosone (at pH 7.1 and 30
CC         degrees Celsius) {ECO:0000269|PubMed:17175089};
CC         Vmax=631.4 nmol/min/mg enzyme with acetaldehyde (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         Vmax=747.3 nmol/min/mg enzyme with propanal (at pH 8.0 and 25 degrees
CC         Celsius) {ECO:0000269|PubMed:12941160};
CC         Vmax=445.3 nmol/min/mg enzyme with propanal (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         Vmax=707.1 nmol/min/mg enzyme with hexanal (at pH 8.0 and 25 degrees
CC         Celsius) {ECO:0000269|PubMed:12941160};
CC         Vmax=750.3 nmol/min/mg enzyme with benzaldehyde (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC         Vmax=72 nmol/min/mg enzyme with benzaldehyde (at pH 7.1 and 30
CC         degrees Celsius) {ECO:0000269|PubMed:17175089};
CC         Vmax=155.8 nmol/min/mg enzyme with trans-2-heptenal (at pH 8.0)
CC         {ECO:0000269|PubMed:19296407};
CC       pH dependence:
CC         Optimum pH is 7.1-9 for the 3-deoxyglucosone dehydrogenase activity.
CC         {ECO:0000269|PubMed:17175089};
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000250|UniProtKB:P51647}.
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
CC       (PubMed:33495566). {ECO:0000250|UniProtKB:P51977,
CC       ECO:0000269|PubMed:33495566}.
CC   -!- INTERACTION:
CC       P00352; P09172: DBH; NbExp=3; IntAct=EBI-752170, EBI-8589586;
CC       P00352; P14136: GFAP; NbExp=3; IntAct=EBI-752170, EBI-744302;
CC       P00352; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-752170, EBI-1055254;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12941160}.
CC       Cell projection, axon {ECO:0000250|UniProtKB:P24549}.
CC   -!- TISSUE SPECIFICITY: Expressed by erythrocytes (at protein level).
CC       {ECO:0000269|PubMed:17175089}.
CC   -!- PTM: The N-terminus is blocked most probably by acetylation.
CC       {ECO:0000250|UniProtKB:P15437}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/aldh1a1/";
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DR   EMBL; M31994; AAA51692.1; -; Genomic_DNA.
DR   EMBL; M31982; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31983; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31984; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31985; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31986; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31987; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31988; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31989; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31990; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31991; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; M31992; AAA51692.1; JOINED; Genomic_DNA.
DR   EMBL; AF003341; AAC51652.1; -; mRNA.
DR   EMBL; AY390731; AAR92229.1; -; mRNA.
DR   EMBL; BT006921; AAP35567.1; -; mRNA.
DR   EMBL; AY338497; AAP88039.1; -; Genomic_DNA.
DR   EMBL; AL591031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62543.1; -; Genomic_DNA.
DR   EMBL; BC001505; AAH01505.1; -; mRNA.
DR   EMBL; S61235; AAD13925.1; -; Genomic_DNA.
DR   EMBL; M26761; AAA35518.1; -; mRNA.
DR   EMBL; K03000; AAA51695.1; -; mRNA.
DR   CCDS; CCDS6644.1; -.
DR   PIR; A33371; DEHUE1.
DR   RefSeq; NP_000680.2; NM_000689.4.
DR   PDB; 4WB9; X-ray; 2.07 A; A=1-501.
DR   PDB; 4WJ9; X-ray; 1.74 A; A=1-501.
DR   PDB; 4WP7; X-ray; 1.80 A; A=1-501.
DR   PDB; 4WPN; X-ray; 1.95 A; A=1-501.
DR   PDB; 4X4L; X-ray; 1.85 A; A=1-501.
DR   PDB; 5AC2; X-ray; 1.85 A; A=1-501.
DR   PDB; 5L2M; X-ray; 1.70 A; A=1-501.
DR   PDB; 5L2N; X-ray; 1.70 A; A=1-501.
DR   PDB; 5L2O; X-ray; 2.05 A; A/B/C/D/E/F/G/H=1-501.
DR   PDB; 5TEI; X-ray; 2.10 A; A=1-501.
DR   PDB; 6DUM; X-ray; 2.00 A; A=1-501.
DR   PDB; 7JWS; X-ray; 1.60 A; A=1-501.
DR   PDB; 7JWT; X-ray; 1.80 A; A=1-501.
DR   PDB; 7JWU; X-ray; 1.90 A; A=1-501.
DR   PDB; 7JWV; X-ray; 1.60 A; A=1-501.
DR   PDB; 7JWW; X-ray; 1.60 A; A=1-501.
DR   PDBsum; 4WB9; -.
DR   PDBsum; 4WJ9; -.
DR   PDBsum; 4WP7; -.
DR   PDBsum; 4WPN; -.
DR   PDBsum; 4X4L; -.
DR   PDBsum; 5AC2; -.
DR   PDBsum; 5L2M; -.
DR   PDBsum; 5L2N; -.
DR   PDBsum; 5L2O; -.
DR   PDBsum; 5TEI; -.
DR   PDBsum; 6DUM; -.
DR   PDBsum; 7JWS; -.
DR   PDBsum; 7JWT; -.
DR   PDBsum; 7JWU; -.
DR   PDBsum; 7JWV; -.
DR   PDBsum; 7JWW; -.
DR   AlphaFoldDB; P00352; -.
DR   SMR; P00352; -.
DR   BioGRID; 106718; 59.
DR   IntAct; P00352; 11.
DR   STRING; 9606.ENSP00000297785; -.
DR   BindingDB; P00352; -.
DR   ChEMBL; CHEMBL3577; -.
DR   DrugBank; DB04447; 1,4-Dithiothreitol.
DR   DrugBank; DB09462; Glycerin.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB00755; Tretinoin.
DR   DrugBank; DB00162; Vitamin A.
DR   DrugCentral; P00352; -.
DR   GlyGen; P00352; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P00352; -.
DR   MetOSite; P00352; -.
DR   PhosphoSitePlus; P00352; -.
DR   SwissPalm; P00352; -.
DR   BioMuta; ALDH1A1; -.
DR   DMDM; 118495; -.
DR   DOSAC-COBS-2DPAGE; P00352; -.
DR   REPRODUCTION-2DPAGE; IPI00218914; -.
DR   REPRODUCTION-2DPAGE; P00352; -.
DR   SWISS-2DPAGE; P00352; -.
DR   UCD-2DPAGE; P00352; -.
DR   EPD; P00352; -.
DR   jPOST; P00352; -.
DR   MassIVE; P00352; -.
DR   PaxDb; P00352; -.
DR   PeptideAtlas; P00352; -.
DR   PRIDE; P00352; -.
DR   ProteomicsDB; 51235; -.
DR   Antibodypedia; 1064; 1049 antibodies from 47 providers.
DR   DNASU; 216; -.
DR   Ensembl; ENST00000297785.8; ENSP00000297785.3; ENSG00000165092.13.
DR   GeneID; 216; -.
DR   KEGG; hsa:216; -.
DR   MANE-Select; ENST00000297785.8; ENSP00000297785.3; NM_000689.5; NP_000680.2.
DR   CTD; 216; -.
DR   DisGeNET; 216; -.
DR   GeneCards; ALDH1A1; -.
DR   HGNC; HGNC:402; ALDH1A1.
DR   HPA; ENSG00000165092; Tissue enhanced (liver).
DR   MIM; 100640; gene.
DR   neXtProt; NX_P00352; -.
DR   OpenTargets; ENSG00000165092; -.
DR   PharmGKB; PA24692; -.
DR   VEuPathDB; HostDB:ENSG00000165092; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   GeneTree; ENSGT00940000154609; -.
DR   HOGENOM; CLU_005391_0_2_1; -.
DR   InParanoid; P00352; -.
DR   OMA; RRMDTGQ; -.
DR   OrthoDB; 153834at2759; -.
DR   PhylomeDB; P00352; -.
DR   TreeFam; TF300455; -.
DR   BioCyc; MetaCyc:HS09183-MON; -.
DR   BRENDA; 1.2.1.36; 2681.
DR   PathwayCommons; P00352; -.
DR   Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR   Reactome; R-HSA-70350; Fructose catabolism.
DR   Reactome; R-HSA-71384; Ethanol oxidation.
DR   SABIO-RK; P00352; -.
DR   SignaLink; P00352; -.
DR   SIGNOR; P00352; -.
DR   UniPathway; UPA00912; -.
DR   BioGRID-ORCS; 216; 10 hits in 1079 CRISPR screens.
DR   ChiTaRS; ALDH1A1; human.
DR   GeneWiki; ALDH1A1; -.
DR   GenomeRNAi; 216; -.
DR   Pharos; P00352; Tchem.
DR   PRO; PR:P00352; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; P00352; protein.
DR   Bgee; ENSG00000165092; Expressed in bronchial epithelial cell and 199 other tissues.
DR   ExpressionAtlas; P00352; baseline and differential.
DR   Genevisible; P00352; HS.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0106373; F:3-deoxyglucosone dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0005497; F:androgen binding; TAS:ProtInc.
DR   GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:RHEA.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR   GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; TAS:ProtInc.
DR   GO; GO:0110095; P:cellular detoxification of aldehyde; IMP:UniProtKB.
DR   GO; GO:0030392; P:fructosamine catabolic process; IDA:UniProtKB.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0036438; P:maintenance of lens transparency; ISS:UniProtKB.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
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; Cell projection; Cytoplasm;
KW   Direct protein sequencing; Lipid metabolism; NAD; Nucleotide-binding;
KW   Oxidoreductase; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6723659,
FT                   ECO:0007744|PubMed:22223895"
FT   CHAIN           2..501
FT                   /note="Aldehyde dehydrogenase 1A1"
FT                   /id="PRO_0000056415"
FT   REGION          336..501
FT                   /note="Mediates interaction with PRMT3"
FT                   /evidence="ECO:0000269|PubMed:33495566"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008,
FT                   ECO:0000269|PubMed:3676276"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008,
FT                   ECO:0000269|PubMed:3676276"
FT   BINDING         167..170
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:25450233,
FT                   ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT                   ECO:0007744|PDB:4X4L"
FT   BINDING         193..196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:25450233,
FT                   ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT                   ECO:0007744|PDB:4X4L"
FT   BINDING         226..227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:25450233,
FT                   ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT                   ECO:0007744|PDB:4X4L"
FT   BINDING         246..247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:25450233,
FT                   ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT                   ECO:0007744|PDB:4X4L"
FT   BINDING         269..271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:25450233,
FT                   ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT                   ECO:0007744|PDB:4X4L"
FT   BINDING         349..353
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:25450233,
FT                   ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT                   ECO:0007744|PDB:4X4L"
FT   BINDING         400..402
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:25450233,
FT                   ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT                   ECO:0007744|PDB:4X4L"
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:0000269|PubMed:6723659,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         128
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         252
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         337
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         353
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         367
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         410
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         419
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         435
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         495
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         121
FT                   /note="N -> S (in dbSNP:rs1049981)"
FT                   /evidence="ECO:0000269|PubMed:8214422"
FT                   /id="VAR_048901"
FT   VARIANT         125
FT                   /note="G -> R (in dbSNP:rs11554423)"
FT                   /id="VAR_048902"
FT   VARIANT         177
FT                   /note="I -> F (in dbSNP:rs8187929)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_017778"
FT   MUTAGEN         302
FT                   /note="C->A,S: Does not prevent inhibition by duocarmycin
FT                   analogs."
FT                   /evidence="ECO:0000269|PubMed:26373694"
FT   MUTAGEN         458
FT                   /note="G->N: No significant effect on aldehyde
FT                   dehydrogenase activity. Prevents the inhibition by ALDH1A1-
FT                   specific inhibitors."
FT                   /evidence="ECO:0000269|PubMed:25634381"
FT   CONFLICT        162
FT                   /note="V -> I (in Ref. 11; AAA35518 and 12; AAA51695)"
FT                   /evidence="ECO:0000305"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           57..70
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           76..79
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           82..98
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           100..111
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           115..120
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           122..136
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:5L2O"
FT   STRAND          148..159
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           172..185
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           200..212
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           226..234
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          241..246
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           248..260
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          265..269
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          275..278
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           284..296
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           297..300
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          308..312
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           313..327
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           348..363
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          367..370
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          373..379
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          385..389
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          403..412
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           414..422
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          428..433
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           437..446
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          450..455
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           470..472
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          473..475
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           479..483
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   HELIX           484..486
FT                   /evidence="ECO:0007829|PDB:7JWS"
FT   STRAND          487..495
FT                   /evidence="ECO:0007829|PDB:7JWS"
SQ   SEQUENCE   501 AA;  54862 MW;  B26464DC7168348E CRC64;
     MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV
     DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL
     NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI
     GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID
     KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG
     QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES
     GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR
     ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE
     YGFHEYTEVK TVTVKISQKN S
 
 
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