ID   AL3A1_MOUSE             Reviewed;         453 AA.
AC   P47739; B1ATI7; Q9R203;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Aldehyde dehydrogenase, dimeric NADP-preferring;
DE            EC=1.2.1.5 {ECO:0000269|PubMed:25286108};
DE   AltName: Full=Aldehyde dehydrogenase 4;
DE   AltName: Full=Aldehyde dehydrogenase family 3 member A1;
DE   AltName: Full=Dioxin-inducible aldehyde dehydrogenase 3;
GN   Name=Aldh3a1; Synonyms=Ahd-4, Ahd4, Aldh3, Aldh4;
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 [MRNA].
RC   STRAIN=C3H/HeJ;
RX   PubMed=8148869; DOI=10.1097/00008571-199312000-00002;
RA   Vasiliou V., Reuter S.F., Kozak C.A., Nebert D.W.;
RT   "Mouse dioxin-inducible cytosolic aldehyde dehydrogenase-3: AHD4 cDNA
RT   sequence, genetic mapping, and differences in mRNA levels.";
RL   Pharmacogenetics 3:281-290(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Vasiliou V., Reuter S.F., Nebert D.W.;
RT   "Organization and characterization of the murine cytosolic TCDD-inducible
RT   aldehyde dehydrogenase gene (ahd4).";
RL   Toxicologist 14:410-410(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
RP   ALD3A1C ASN-154; ARG-305 AND VAL-352.
RC   STRAIN=DBA/2J, and SWR/J;
RX   PubMed=10376761;
RA   Shiao T., Tran P., Siegel D., Lee J., Vasiliou V.;
RT   "Four amino acid changes are associated with the Aldh3a1 locus polymorphism
RT   in mice which may be responsible for corneal sensitivity to ultraviolet
RT   light.";
RL   Pharmacogenetics 9:145-153(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   FUNCTION.
RC   STRAIN=CD-1;
RX   PubMed=11784860; DOI=10.1128/mcb.22.3.849-855.2002;
RA   Nees D.W., Wawrousek E.F., Robison W.G. Jr., Piatigorsky J.;
RT   "Structurally normal corneas in aldehyde dehydrogenase 3a1-deficient
RT   mice.";
RL   Mol. Cell. Biol. 22:849-855(2002).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=25286108; DOI=10.1042/bj20140624;
RA   Kitamura T., Takagi S., Naganuma T., Kihara A.;
RT   "Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via
RT   two C-terminal tryptophan residues and lipid modification.";
RL   Biochem. J. 465:79-87(2015).
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:25286108). Preferentially oxidizes
CC       aromatic aldehyde substrates (PubMed:11784860). Comprises about 50
CC       percent of corneal epithelial soluble proteins (PubMed:11784860). May
CC       play a role in preventing corneal damage caused by ultraviolet light
CC       (PubMed:10376761). {ECO:0000250|UniProtKB:P30838,
CC       ECO:0000269|PubMed:10376761, ECO:0000269|PubMed:11784860,
CC       ECO:0000269|PubMed:25286108, 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;
CC         Evidence={ECO:0000269|PubMed:25286108};
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:0000269|PubMed:25286108};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30838}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25286108}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in cornea, stomach, skin,
CC       bladder and lungs. Lowest expression levels in lungs and bladder.
CC       {ECO:0000269|PubMed:10376761}.
CC   -!- POLYMORPHISM: There are two alleles, Ald3a1a and Ald3a1c. Ald3a1c codes
CC       for a low activity enzyme and is associated with extensive corneal
CC       clouding after exposure to ultraviolet light. Ald3a1a encodes the high
CC       activity enzyme. {ECO:0000269|PubMed:10376761}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U12785; AAA20670.1; -; mRNA.
DR   EMBL; AF072815; AAD15964.1; -; mRNA.
DR   EMBL; AL646093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS24808.1; -.
DR   RefSeq; NP_001106196.1; NM_001112725.1.
DR   RefSeq; NP_031462.2; NM_007436.2.
DR   RefSeq; XP_006532089.1; XM_006532026.1.
DR   RefSeq; XP_006532090.1; XM_006532027.3.
DR   AlphaFoldDB; P47739; -.
DR   SMR; P47739; -.
DR   BioGRID; 198065; 2.
DR   STRING; 10090.ENSMUSP00000019246; -.
DR   SwissLipids; SLP:000001745; -.
DR   PhosphoSitePlus; P47739; -.
DR   SwissPalm; P47739; -.
DR   jPOST; P47739; -.
DR   MaxQB; P47739; -.
DR   PaxDb; 10090-ENSMUSP00000019246; -.
DR   PeptideAtlas; P47739; -.
DR   ProteomicsDB; 296165; -.
DR   Antibodypedia; 26030; 522 antibodies from 40 providers.
DR   DNASU; 11670; -.
DR   Ensembl; ENSMUST00000019246.4; ENSMUSP00000019246.4; ENSMUSG00000019102.11.
DR   Ensembl; ENSMUST00000108716.8; ENSMUSP00000104356.2; ENSMUSG00000019102.11.
DR   GeneID; 11670; -.
DR   KEGG; mmu:11670; -.
DR   UCSC; uc007jhd.2; mouse.
DR   AGR; MGI:1353451; -.
DR   CTD; 218; -.
DR   MGI; MGI:1353451; Aldh3a1.
DR   VEuPathDB; HostDB:ENSMUSG00000019102; -.
DR   eggNOG; KOG2456; Eukaryota.
DR   GeneTree; ENSGT00940000162101; -.
DR   HOGENOM; CLU_005391_3_0_1; -.
DR   InParanoid; P47739; -.
DR   OMA; EPCIQGQ; -.
DR   OrthoDB; 606537at2759; -.
DR   PhylomeDB; P47739; -.
DR   TreeFam; TF314264; -.
DR   BRENDA; 1.2.1.5; 3474.
DR   Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR   BioGRID-ORCS; 11670; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Aldh3a2; mouse.
DR   PRO; PR:P47739; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P47739; Protein.
DR   Bgee; ENSMUSG00000019102; Expressed in substantia propria of cornea and 83 other cell types or tissues.
DR   ExpressionAtlas; P47739; baseline and differential.
DR   Genevisible; P47739; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:MGI.
DR   GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; ISO:MGI.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR   GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   CDD; cd07132; ALDH_F3AB; 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; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF15; ALDEHYDE DEHYDROGENASE, DIMERIC NADP-PREFERRING; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 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   Acetylation; Cytoplasm; Lipid metabolism; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P30838"
FT   CHAIN           2..453
FT                   /note="Aldehyde dehydrogenase, dimeric NADP-preferring"
FT                   /id="PRO_0000056471"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250"
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:0000250|UniProtKB:P30838"
FT   MOD_RES         178
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30838"
FT   MOD_RES         194
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30838"
FT   VARIANT         154
FT                   /note="I -> N (in allele Ald3a1c)"
FT                   /evidence="ECO:0000269|PubMed:10376761"
FT   VARIANT         305
FT                   /note="H -> R (in allele Ald3a1c)"
FT                   /evidence="ECO:0000269|PubMed:10376761"
FT   VARIANT         352
FT                   /note="I -> V (in allele Ald3a1c)"
FT                   /evidence="ECO:0000269|PubMed:10376761"
FT   CONFLICT        88
FT                   /note="A -> G (in Ref. 1; AAA20670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="A -> R (in Ref. 3; AAD15964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   453 AA;  50481 MW;  7B4EA1CC56B5FAA1 CRC64;
     MSNISSIVNR ARDAFNSGKT RPLQFRVEQL EALQRMINEN LKGISKALAS NLRKNEWTSY
     YEEVAHVLDE IDFTIKGLSD WAEDEPVAKT RQTQEDDLYI HSEPLGVVLV IGAWNYPFNL
     TIQPMVGAIA AGNAVVLKPS EVSDHMADLL STLIPQYMDK DLYPVIKGGV PETTELLKEK
     FDHIMYTGST AVGKIVMAAA AKHLTPVTLE LGGKSPCYVD KDCDLDVACR RIAWGKFMNS
     GQTCVAPDYI LCDPSIQNEI VEKLKKSLKD FYGEDAKQSH DYGRIINDRH FQRVINLIDS
     KKVAHGGTWD QPSRYIAPTI LVDVDPQSPV MQEEIFGPVM PIVCVRSLDE AIKFINQREK
     PLALYVFSNN DKVIKKMIAE TSSGGVTAND VIVHITVPTL PFGGVGNSGM GAYHGKKSFE
     TFSHRRSCLV RSLRNEEANK ARYPPSPAKM PRH
//

ID   Q3UNF5_MOUSE            Unreviewed;       453 AA.
AC   Q3UNF5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   Name=Aldh3a1 {ECO:0000313|EMBL:AAI50678.1,
GN   ECO:0000313|MGI:MGI:1353451};
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 {ECO:0000313|EMBL:BAE25792.1};
RN   [1] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:AAI50678.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI50678.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [7] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAE25792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Colon {ECO:0000313|EMBL:BAE25792.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
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:0000256|ARBA:ARBA00000589};
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00036150};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC150677; AAI50678.1; -; mRNA.
DR   EMBL; AK144241; BAE25792.1; -; mRNA.
DR   RefSeq; NP_001106196.1; NM_001112725.1.
DR   RefSeq; NP_031462.2; NM_007436.2.
DR   AlphaFoldDB; Q3UNF5; -.
DR   DNASU; 11670; -.
DR   GeneID; 11670; -.
DR   KEGG; mmu:11670; -.
DR   AGR; MGI:1353451; -.
DR   CTD; 218; -.
DR   MGI; MGI:1353451; Aldh3a1.
DR   OrthoDB; 606537at2759; -.
DR   BRENDA; 1.2.1.3; 3474.
DR   BioGRID-ORCS; 11670; 2 hits in 77 CRISPR screens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProt.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07132; ALDH_F3AB; 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; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF15; ALDEHYDE DEHYDROGENASE, DIMERIC NADP-PREFERRING; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          3..425
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   453 AA;  50501 MW;  A64EB83B56155C7F CRC64;
     MSNISSIVNR ARDAFNSGKT RPLQFRVEQL EALQRMINEN LKGISKALAS NLRKNEWTSY
     YEEVAHVLDE IDFTIKGLSD WAEDEPVAKT RQTQEDDLYI HSEPLGVVLV IGAWNYPFNL
     TIQPMVGAIA AGNAVVLKPS EVSDHMADLL STLNPQYMDK DLYPVIKGGV PETTELLKEK
     FDHIMYTGST AVGKIVMAAA AKHLTPVTLE LGGKSPCYVD KDCDLDVACR RIAWGKFMNS
     GQTCVAPDYI LCDPSIQNEI VEKLKKSLKD FYGEDAKQSH DYGRIINDRH FQRVINLIDS
     KKVARGGTWD QPSRYIAPTI LVDVDPQSPV MQEEIFGPVM PIVCVRSLDE AIKFINQREK
     PLALYVFSNN DKVIKKMIAE TSSGGVTAND VIVHITVPTL PFGGVGNSGM GAYHGKKSFE
     TFSHRRSCLV RSLRNEEANK ARYPPSPAKM PRH
//