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Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (Aldehyde dehydrogenase 4) (Aldehyde dehydrogenase family 3 member A1) (Dioxin-inducible aldehyde dehydrogenase 3)

 AL3A1_MOUSE             Reviewed;         453 AA.
P47739; B1ATI7; Q9R203;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 145.
RecName: Full=Aldehyde dehydrogenase, dimeric NADP-preferring;
EC=1.2.1.5 {ECO:0000269|PubMed:25286108};
AltName: Full=Aldehyde dehydrogenase 4;
AltName: Full=Aldehyde dehydrogenase family 3 member A1;
AltName: Full=Dioxin-inducible aldehyde dehydrogenase 3;
Name=Aldh3a1; Synonyms=Ahd-4, Ahd4, Aldh3, Aldh4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeJ;
PubMed=8148869;
Vasiliou V., Reuter S.F., Kozak C.A., Nebert D.W.;
"Mouse dioxin-inducible cytosolic aldehyde dehydrogenase-3: AHD4 cDNA
sequence, genetic mapping, and differences in mRNA levels.";
Pharmacogenetics 3:281-290(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Vasiliou V., Reuter S.F., Nebert D.W.;
"Organization and characterization of the murine cytosolic TCDD-
inducible aldehyde dehydrogenase gene (ahd4).";
Toxicologist 14:410-410(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
ALD3A1C ASN-154; ARG-305 AND VAL-352.
STRAIN=DBA/2J, and SWR/J;
PubMed=10376761;
Shiao T., Tran P., Siegel D., Lee J., Vasiliou V.;
"Four amino acid changes are associated with the Aldh3a1 locus
polymorphism in mice which may be responsible for corneal sensitivity
to ultraviolet light.";
Pharmacogenetics 9:145-153(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
FUNCTION.
STRAIN=CD-1;
PubMed=11784860; DOI=10.1128/MCB.22.3.849-855.2002;
Nees D.W., Wawrousek E.F., Robison W.G. Jr., Piatigorsky J.;
"Structurally normal corneas in aldehyde dehydrogenase 3a1-deficient
mice.";
Mol. Cell. Biol. 22:849-855(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=25286108; DOI=10.1042/BJ20140624;
Kitamura T., Takagi S., Naganuma T., Kihara A.;
"Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets
via two C-terminal tryptophan residues and lipid modification.";
Biochem. J. 465:79-87(2015).
-!- FUNCTION: ALDHs play a major role in the detoxification of
alcohol-derived acetaldehyde (Probable). They are involved in the
metabolism of corticosteroids, biogenic amines, neurotransmitters,
and lipid peroxidation (Probable). Oxidizes medium and long chain
aldehydes into non-toxic fatty acids (PubMed:25286108).
Preferentially oxidizes aromatic aldehyde substrates
(PubMed:11784860). Comprises about 50 percent of corneal
epithelial soluble proteins (PubMed:11784860). May play a role in
preventing corneal damage caused by ultraviolet light
(PubMed:10376761). {ECO:0000250|UniProtKB:P30838,
ECO:0000269|PubMed:10376761, ECO:0000269|PubMed:11784860,
ECO:0000269|PubMed:25286108, ECO:0000305}.
-!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = a
carboxylate + NAD(P)H. {ECO:0000269|PubMed:25286108}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30838}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25286108}.
-!- TISSUE SPECIFICITY: Constitutively expressed in cornea, stomach,
skin, bladder and lungs. Lowest expression levels in lungs and
bladder. {ECO:0000269|PubMed:10376761}.
-!- POLYMORPHISM: There are two alleles, Ald3a1a and Ald3a1c. Ald3a1c
codes for a low activity enzyme and is associated with extensive
corneal clouding after exposure to ultraviolet light. Ald3a1a
encodes the high activity enzyme. {ECO:0000269|PubMed:10376761}.
-!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U12785; AAA20670.1; -; mRNA.
EMBL; AF072815; AAD15964.1; -; mRNA.
EMBL; AL646093; CAI25900.1; -; Genomic_DNA.
CCDS; CCDS24808.1; -.
RefSeq; NP_001106196.1; NM_001112725.1.
RefSeq; NP_031462.2; NM_007436.2.
RefSeq; XP_006532089.1; XM_006532026.1.
RefSeq; XP_006532090.1; XM_006532027.3.
UniGene; Mm.4257; -.
ProteinModelPortal; P47739; -.
SMR; P47739; -.
BioGrid; 198065; 1.
IntAct; P47739; 1.
MINT; MINT-4087533; -.
STRING; 10090.ENSMUSP00000019246; -.
SwissLipids; SLP:000001745; -.
PhosphoSitePlus; P47739; -.
MaxQB; P47739; -.
PaxDb; P47739; -.
PeptideAtlas; P47739; -.
PRIDE; P47739; -.
Ensembl; ENSMUST00000019246; ENSMUSP00000019246; ENSMUSG00000019102.
Ensembl; ENSMUST00000108716; ENSMUSP00000104356; ENSMUSG00000019102.
GeneID; 11670; -.
KEGG; mmu:11670; -.
UCSC; uc007jhd.2; mouse.
CTD; 218; -.
MGI; MGI:1353451; Aldh3a1.
eggNOG; KOG2456; Eukaryota.
eggNOG; COG1012; LUCA.
GeneTree; ENSGT00390000002825; -.
HOVERGEN; HBG050483; -.
InParanoid; P47739; -.
KO; K00129; -.
OMA; TIQPMVG; -.
OrthoDB; EOG091G05HC; -.
TreeFam; TF314264; -.
BRENDA; 1.2.1.5; 3474.
Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
PRO; PR:P47739; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000019102; -.
CleanEx; MM_ALDH3A1; -.
ExpressionAtlas; P47739; baseline and differential.
Genevisible; P47739; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI.
GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; ISS:UniProtKB.
GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:MGI.
GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; ISO:MGI.
GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
Gene3D; 3.40.605.10; -; 1.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR016160; Ald_DH_CS_CYS.
InterPro; IPR029510; Ald_DH_CS_GLU.
InterPro; IPR016162; Ald_DH_N.
InterPro; IPR015590; Aldehyde_DH_dom.
InterPro; IPR012394; Aldehyde_DH_NAD(P).
Pfam; PF00171; Aldedh; 1.
PIRSF; PIRSF036492; ALDH; 1.
SUPFAM; SSF53720; SSF53720; 1.
PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase;
Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P30838}.
CHAIN 2 453 Aldehyde dehydrogenase, dimeric NADP-
preferring.
/FTId=PRO_0000056471.
NP_BIND 188 193 NAD or NADP. {ECO:0000250}.
ACT_SITE 210 210 {ECO:0000250}.
ACT_SITE 244 244 {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P30838}.
MOD_RES 178 178 N6-acetyllysine.
{ECO:0000250|UniProtKB:P30838}.
MOD_RES 194 194 N6-acetyllysine.
{ECO:0000250|UniProtKB:P30838}.
VARIANT 154 154 I -> N (in allele Ald3a1c).
{ECO:0000269|PubMed:10376761}.
VARIANT 305 305 H -> R (in allele Ald3a1c).
{ECO:0000269|PubMed:10376761}.
VARIANT 352 352 I -> V (in allele Ald3a1c).
{ECO:0000269|PubMed:10376761}.
CONFLICT 88 88 A -> G (in Ref. 1; AAA20670).
{ECO:0000305}.
CONFLICT 88 88 A -> R (in Ref. 3; AAD15964).
{ECO:0000305}.
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


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