AL3A1_HUMAN
ID AL3A1_HUMAN Reviewed; 453 AA.
AC P30838; A8K828; Q9BT37;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Aldehyde dehydrogenase, dimeric NADP-preferring;
DE EC=1.2.1.5 {ECO:0000269|PubMed:1737758, ECO:0000269|PubMed:22021038};
DE AltName: Full=ALDHIII;
DE AltName: Full=Aldehyde dehydrogenase 3;
DE AltName: Full=Aldehyde dehydrogenase family 3 member A1;
GN Name=ALDH3A1; Synonyms=ALDH3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-134.
RC TISSUE=Stomach;
RA Schuuring E.M.D., Verhoeven E., Eckey R., Vos H.L., Michalides R.J.A.;
RT "Cloning and complete nucleotide sequence of a cDNA encoding the full-
RT length open reading frame of the human aldehyde dehydrogenase type III
RT gene.";
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Stomach;
RX PubMed=1737758; DOI=10.1016/s0021-9258(19)50690-1;
RA Hsu L.C., Chang W.-C., Shibuya A., Yoshida A.;
RT "Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary
RT structure, and expression in Escherichia coli.";
RL J. Biol. Chem. 267:3030-3037(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach;
RX PubMed=8493892; DOI=10.1007/978-1-4615-2904-0_16;
RA Hsu L.C., Yoshida A.;
RT "Human stomach aldehyde dehydrogenase, ALDH3.";
RL Adv. Exp. Med. Biol. 328:141-152(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-134.
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 [LARGE SCALE MRNA], AND VARIANT ALA-134.
RC TISSUE=Cervix, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-134.
RA Mural R.J., Istrail S., Sutton 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], AND VARIANT ALA-134.
RC TISSUE=Pancreas;
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 PROTEIN SEQUENCE OF 62-453.
RC TISSUE=Stomach;
RX PubMed=2037078; DOI=10.1016/0014-5793(91)80559-l;
RA Yin S.-J., Vagelopoulos N., Wang S.-L., Joernvall H.;
RT "Structural features of stomach aldehyde dehydrogenase distinguish dimeric
RT aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant'
RT enzymes within the alcohol and aldehyde dehydrogenase families.";
RL FEBS Lett. 283:85-88(1991).
RN [10]
RP CHARACTERIZATION.
RX PubMed=1905102; DOI=10.1007/978-1-4684-5901-2_6;
RA Eckey R., Timmann R., Hempel J., Agarwal D.P., Goedde H.W.;
RT "Biochemical, immunological, and molecular characterization of a 'high Km'
RT aldehyde dehydrogenase.";
RL Adv. Exp. Med. Biol. 284:43-52(1991).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-178 AND LYS-194, AND
RP IDENTIFICATION BY MASS 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 [12]
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 [13]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITOR, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF CYS-244, AND ACTIVE SITE.
RX PubMed=22021038; DOI=10.1074/jbc.m111.293597;
RA Khanna M., Chen C.H., Kimble-Hill A., Parajuli B., Perez-Miller S.,
RA Baskaran S., Kim J., Dria K., Vasiliou V., Mochly-Rosen D., Hurley T.D.;
RT "Discovery of a novel class of covalent inhibitor for aldehyde
RT dehydrogenases.";
RL J. Biol. Chem. 286:43486-43494(2011).
RN [15]
RP VARIANT ALA-329.
RX PubMed=9250352; DOI=10.1046/j.1469-1809.1997.6130235.x;
RA Tsukamoto N., Chang C., Yoshida A.;
RT "Mutations associated with Sjogren-Larsson syndrome.";
RL Ann. Hum. Genet. 61:235-242(1997).
CC -!- FUNCTION: ALDHs play a major role in the detoxification of alcohol-
CC derived acetaldehyde (Probable). They are involved in the metabolism of
CC corticosteroids, biogenic amines, neurotransmitters, and lipid
CC peroxidation (Probable). Oxidizes medium and long chain aldehydes into
CC non-toxic fatty acids (PubMed:1737758). Preferentially oxidizes
CC aromatic aldehyde substrates (PubMed:1737758). Comprises about 50
CC percent of corneal epithelial soluble proteins (By similarity). May
CC play a role in preventing corneal damage caused by ultraviolet light
CC (By similarity). {ECO:0000250|UniProtKB:P47739,
CC ECO:0000269|PubMed:1737758, ECO:0000305}.
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=1.2.1.5; Evidence={ECO:0000269|PubMed:1737758,
CC ECO:0000269|PubMed:22021038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P47739};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Has a high Km for acetaldehyde.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22021038}.
CC -!- INTERACTION:
CC P30838; O75344: FKBP6; NbExp=3; IntAct=EBI-3905126, EBI-744771;
CC P30838; Q9NUX5: POT1; NbExp=2; IntAct=EBI-3905126, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47739}.
CC -!- TISSUE SPECIFICITY: High levels in stomach, esophagus and lung; low
CC level in the liver and kidney.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M74542; AAA51696.1; -; mRNA.
DR EMBL; M77477; AAB46377.1; -; mRNA.
DR EMBL; S61044; AAB26658.1; -; mRNA.
DR EMBL; BT007102; AAP35766.1; -; mRNA.
DR EMBL; AK292193; BAF84882.1; -; mRNA.
DR EMBL; AK314584; BAG37160.1; -; mRNA.
DR EMBL; AC005722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471212; EAW50909.1; -; Genomic_DNA.
DR EMBL; BC004370; AAH04370.1; -; mRNA.
DR EMBL; BC008892; AAH08892.1; -; mRNA.
DR EMBL; BC021194; AAH21194.1; -; mRNA.
DR CCDS; CCDS11212.1; -.
DR PIR; A42584; A42584.
DR RefSeq; NP_000682.3; NM_000691.4.
DR RefSeq; NP_001128639.1; NM_001135167.1.
DR RefSeq; NP_001128640.1; NM_001135168.1.
DR PDB; 3SZA; X-ray; 1.48 A; A/B=1-453.
DR PDB; 3SZB; X-ray; 1.51 A; A/B=1-453.
DR PDB; 4H80; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-453.
DR PDB; 4L1O; X-ray; 2.30 A; A/B=1-453.
DR PDB; 4L2O; X-ray; 1.94 A; A/B/E/G=1-453.
DR PDBsum; 3SZA; -.
DR PDBsum; 3SZB; -.
DR PDBsum; 4H80; -.
DR PDBsum; 4L1O; -.
DR PDBsum; 4L2O; -.
DR AlphaFoldDB; P30838; -.
DR SMR; P30838; -.
DR BioGRID; 106720; 89.
DR IntAct; P30838; 16.
DR STRING; 9606.ENSP00000411821; -.
DR BindingDB; P30838; -.
DR ChEMBL; CHEMBL3578; -.
DR DrugBank; DB00157; NADH.
DR GlyGen; P30838; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30838; -.
DR PhosphoSitePlus; P30838; -.
DR BioMuta; ALDH3A1; -.
DR DMDM; 311033473; -.
DR EPD; P30838; -.
DR jPOST; P30838; -.
DR MassIVE; P30838; -.
DR MaxQB; P30838; -.
DR PaxDb; P30838; -.
DR PeptideAtlas; P30838; -.
DR PRIDE; P30838; -.
DR ProteomicsDB; 54741; -.
DR Antibodypedia; 26030; 484 antibodies from 40 providers.
DR DNASU; 218; -.
DR Ensembl; ENST00000225740.11; ENSP00000225740.6; ENSG00000108602.18.
DR Ensembl; ENST00000444455.5; ENSP00000388469.1; ENSG00000108602.18.
DR Ensembl; ENST00000457500.6; ENSP00000411821.2; ENSG00000108602.18.
DR GeneID; 218; -.
DR KEGG; hsa:218; -.
DR MANE-Select; ENST00000225740.11; ENSP00000225740.6; NM_000691.5; NP_000682.3.
DR UCSC; uc002gwj.4; human.
DR CTD; 218; -.
DR DisGeNET; 218; -.
DR GeneCards; ALDH3A1; -.
DR HGNC; HGNC:405; ALDH3A1.
DR HPA; ENSG00000108602; Tissue enhanced (esophagus, salivary gland, stomach).
DR MIM; 100660; gene.
DR neXtProt; NX_P30838; -.
DR OpenTargets; ENSG00000108602; -.
DR PharmGKB; PA24697; -.
DR VEuPathDB; HostDB:ENSG00000108602; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000162101; -.
DR InParanoid; P30838; -.
DR OMA; RHGKRWM; -.
DR OrthoDB; 646662at2759; -.
DR PhylomeDB; P30838; -.
DR TreeFam; TF314264; -.
DR BRENDA; 1.2.1.5; 2681.
DR PathwayCommons; P30838; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; P30838; -.
DR SignaLink; P30838; -.
DR BioGRID-ORCS; 218; 14 hits in 1078 CRISPR screens.
DR ChiTaRS; ALDH3A1; human.
DR EvolutionaryTrace; P30838; -.
DR GeneWiki; Aldehyde_dehydrogenase_3_family,_member_A1; -.
DR GenomeRNAi; 218; -.
DR Pharos; P30838; Tchem.
DR PRO; PR:P30838; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P30838; protein.
DR Bgee; ENSG00000108602; Expressed in nasal cavity epithelium and 149 other tissues.
DR ExpressionAtlas; P30838; baseline and differential.
DR Genevisible; P30838; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; TAS:Reactome.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:CACAO.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 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; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..453
FT /note="Aldehyde dehydrogenase, dimeric NADP-preferring"
FT /id="PRO_0000056470"
FT ACT_SITE 210
FT /evidence="ECO:0000269|PubMed:22021038"
FT ACT_SITE 244
FT /evidence="ECO:0000269|PubMed:22021038"
FT BINDING 188..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 178
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 134
FT /note="S -> A (in dbSNP:rs887241)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT /id="VAR_018981"
FT VARIANT 309
FT /note="G -> E (in dbSNP:rs3744692)"
FT /id="VAR_018982"
FT VARIANT 329
FT /note="P -> A (in allele ALDH3A1*2; dbSNP:rs2228100)"
FT /evidence="ECO:0000269|PubMed:9250352"
FT /id="VAR_011303"
FT MUTAGEN 244
FT /note="C->S: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:22021038"
FT CONFLICT 12
FT /note="R -> P (in Ref. 2; AAB46377 and 3; AAB26658)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="I -> F (in Ref. 1; AAA51696)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="V -> L (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="D -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:3SZA"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 64..82
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4L2O"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3SZA"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:3SZA"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 257..272
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3SZA"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 416..421
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 423..430
FT /evidence="ECO:0007829|PDB:3SZA"
FT HELIX 437..442
FT /evidence="ECO:0007829|PDB:3SZA"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:3SZA"
SQ SEQUENCE 453 AA; 50395 MW; D35C488A022FAACA CRC64;
MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY
YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL
TIQPMVGAIA AGNSVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER
FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS
GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG
QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVL PIVCVRSLEE AIQFINQREK
PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE
TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH
