AL1A7_MOUSE
ID AL1A7_MOUSE Reviewed; 501 AA.
AC O35945; Q80ZX7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aldehyde dehydrogenase, cytosolic 1;
DE EC=1.2.1.3;
DE AltName: Full=ALDH class 1;
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A7;
DE AltName: Full=Aldehyde dehydrogenase phenobarbital-inducible;
GN Name=Aldh1a7 {ECO:0000312|MGI:MGI:1347050}; Synonyms=Aldh-pb;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=10191271; DOI=10.1042/bj3390387;
RA Hsu L.C., Chang W.C., Hoffmann I., Duester G.;
RT "Molecular analysis of two closely related mouse aldehyde dehydrogenase
RT genes: identification of a role for Aldh1, but not Aldh-pb, in the
RT biosynthesis of retinoic acid.";
RL Biochem. J. 339:387-395(1999).
RN [2] {ECO:0000312|EMBL:AAH46315.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAH46315.2};
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Pancreas;
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).
CC -!- FUNCTION: Can oxidize benzaldehyde, propionaldehyde and acetaldehyde
CC (By similarity). No detectable activity with retinal. {ECO:0000250,
CC ECO:0000269|PubMed:10191271}.
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;
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P13601}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13601}.
CC -!- TISSUE SPECIFICITY: Highest level in liver, high level in lung, low
CC level in kidney and testis. {ECO:0000269|PubMed:10191271}.
CC -!- MISCELLANEOUS: Xenopus embryos injected with Aldh1a7 mRNA failed to
CC produce retinoic acid in contrast to embryos injected with Aldh1a1.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255}.
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DR EMBL; U96401; AAB64411.1; -; mRNA.
DR EMBL; BC046315; AAH46315.2; -; mRNA.
DR CCDS; CCDS29696.1; -.
DR RefSeq; NP_036051.1; NM_011921.2.
DR AlphaFoldDB; O35945; -.
DR SMR; O35945; -.
DR BioGRID; 204918; 1.
DR STRING; 10090.ENSMUSP00000025656; -.
DR iPTMnet; O35945; -.
DR PhosphoSitePlus; O35945; -.
DR SwissPalm; O35945; -.
DR jPOST; O35945; -.
DR MaxQB; O35945; -.
DR PaxDb; O35945; -.
DR PRIDE; O35945; -.
DR ProteomicsDB; 281962; -.
DR DNASU; 26358; -.
DR Ensembl; ENSMUST00000025656; ENSMUSP00000025656; ENSMUSG00000024747.
DR GeneID; 26358; -.
DR KEGG; mmu:26358; -.
DR UCSC; uc008gyn.1; mouse.
DR CTD; 26358; -.
DR MGI; MGI:1347050; Aldh1a7.
DR VEuPathDB; HostDB:ENSMUSG00000024747; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000154609; -.
DR HOGENOM; CLU_005391_0_2_1; -.
DR InParanoid; O35945; -.
DR OMA; ENCSATS; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; O35945; -.
DR TreeFam; TF300455; -.
DR BRENDA; 1.2.1.3; 3474.
DR UniPathway; UPA00780; UER00768.
DR BioGRID-ORCS; 26358; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Aldh1a7; mouse.
DR PRO; PR:O35945; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O35945; protein.
DR Bgee; ENSMUSG00000024747; Expressed in epithelium of lens and 170 other tissues.
DR ExpressionAtlas; O35945; baseline and differential.
DR Genevisible; O35945; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISO:MGI.
DR GO; GO:0106373; F:3-deoxyglucosone dehydrogenase activity; ISO:MGI.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:MGI.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; ISO:MGI.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; ISO:MGI.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030392; P:fructosamine catabolic process; ISO:MGI.
DR GO; GO:0006001; P:fructose catabolic process; IDA:MGI.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT CHAIN 2..501
FT /note="Aldehyde dehydrogenase, cytosolic 1"
FT /id="PRO_0000291264"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P51977,
FT ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-
FT ProRule:PRU10008"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P51977,
FT ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-
FT ProRule:PRU10008"
FT BINDING 246..251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q28399"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
SQ SEQUENCE 501 AA; 54588 MW; 42DE97962799237B CRC64;
MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSSKKFPV LNPATEEVIC HVEEGDKADV
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATMESMN AGKVFAHAYL
LDVEISIKAL QYFAGWADKI HGQTIPSDGN IFTYTRREPI GVCGQIIPWN GPLIIFTWKL
GPALSCGNTV VVKPAEQTPL TALHMASLIK EAGFPPGVVN IVPGYGPTAG GAISSHMDID
KVSFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDSAVEF AHQGVFFHQG
QICVAASRLF VEESIYDEFV RRSVERAKKY ILGNPLNSGI NQGPQIDKEQ HNKILGLIES
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSMDDVIKR
ANNTTYGLAA GVFTKDLDKA ITVSSALQAG MVWVNCYLAV PVQCPFGGFK MSGNGRELGE
HGLYEYTELK TVAMQISQKN S
