ADH1_MOUSE
ID ADH1_MOUSE Reviewed; 375 AA.
AC P00329;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=ADH-A2;
DE AltName: Full=Alcohol dehydrogenase A subunit;
GN Name=Adh1; Synonyms=Adh-1;
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].
RX PubMed=3157987; DOI=10.1073/pnas.82.8.2262;
RA Edenberg H.J., Zhang K., Fong K., Bosron W.F., Li T.-K.;
RT "Cloning and sequencing of cDNA encoding the complete mouse liver alcohol
RT dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2262-2266(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2893758; DOI=10.1016/0378-1119(87)90325-8;
RA Ceci J.D., Zheng Y.W., Felder M.R.;
RT "Molecular analysis of mouse alcohol dehydrogenase: nucleotide sequence of
RT the Adh-1 gene and genetic mapping of a related nucleotide sequence to
RT chromosome 3.";
RL Gene 59:171-182(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3428612; DOI=10.1016/0378-1119(87)90173-9;
RA Zhang K., Bosron W.F., Edenberg H.J.;
RT "Structure of the mouse Adh-1 gene and identification of a deletion in a
RT long alternating purine-pyrimidine sequence in the first intron of strains
RT expressing low alcohol dehydrogenase activity.";
RL Gene 57:27-36(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-51.
RX PubMed=7937138; DOI=10.1093/nar/22.20.4132;
RA Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L.,
RA Zaballos A.;
RT "Isolation of genomic DNA fragments corresponding to genes modulated in
RT vivo by a transcription factor.";
RL Nucleic Acids Res. 22:4132-4138(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-375.
RC STRAIN=SWR/J; TISSUE=Liver;
RX PubMed=3011597; DOI=10.1016/0378-1119(86)90101-0;
RA Ceci J.D., Lawther R., Duester G., Hatfield G.W., Smith M., O'Malley M.P.,
RA Felder M.R.;
RT "Androgen induction of alcohol dehydrogenase in mouse kidney. Studies with
RT a cDNA probe confirmed by nucleotide sequence analysis.";
RL Gene 41:217-224(1986).
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=FVB/N;
RX PubMed=7738026; DOI=10.1074/jbc.270.18.10868;
RA Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.;
RT "Cloning of the mouse class IV alcohol dehydrogenase (retinol
RT dehydrogenase) cDNA and tissue-specific expression patterns of the murine
RT ADH gene family.";
RL J. Biol. Chem. 270:10868-10877(1995).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Testis;
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 [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-234 AND LYS-340, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBUNIT: Dimer of identical or non-identical chains of three types (A,
CC B, C), which are coded by 3 separate genes at different loci.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the liver, small
CC intestine and eye, at moderate levels in kidney, ovary and uterus, and
CC at low levels in the spinal cord, thymus, heart, stomach mucosa, skin
CC and testis. {ECO:0000269|PubMed:7738026}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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DR EMBL; M18480; AAA37178.1; -; Genomic_DNA.
DR EMBL; M18472; AAA37178.1; JOINED; Genomic_DNA.
DR EMBL; M18473; AAA37178.1; JOINED; Genomic_DNA.
DR EMBL; M18474; AAA37178.1; JOINED; Genomic_DNA.
DR EMBL; M18475; AAA37178.1; JOINED; Genomic_DNA.
DR EMBL; M18476; AAA37178.1; JOINED; Genomic_DNA.
DR EMBL; M18477; AAA37178.1; JOINED; Genomic_DNA.
DR EMBL; M18478; AAA37178.1; JOINED; Genomic_DNA.
DR EMBL; M22679; AAA37179.1; -; Genomic_DNA.
DR EMBL; M22671; AAA37179.1; JOINED; Genomic_DNA.
DR EMBL; M22672; AAA37179.1; JOINED; Genomic_DNA.
DR EMBL; M22673; AAA37179.1; JOINED; Genomic_DNA.
DR EMBL; M22674; AAA37179.1; JOINED; Genomic_DNA.
DR EMBL; M22675; AAA37179.1; JOINED; Genomic_DNA.
DR EMBL; M22676; AAA37179.1; JOINED; Genomic_DNA.
DR EMBL; M22677; AAA37179.1; JOINED; Genomic_DNA.
DR EMBL; M11307; AAA37180.1; -; mRNA.
DR EMBL; BC013477; AAH13477.1; -; mRNA.
DR EMBL; BC054467; AAH54467.1; -; mRNA.
DR EMBL; Z32540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M22611; AAA37181.1; -; mRNA.
DR CCDS; CCDS17867.1; -.
DR PIR; A27322; DEMSAA.
DR RefSeq; NP_031435.1; NM_007409.2.
DR AlphaFoldDB; P00329; -.
DR SMR; P00329; -.
DR BioGRID; 197984; 1.
DR STRING; 10090.ENSMUSP00000004232; -.
DR iPTMnet; P00329; -.
DR PhosphoSitePlus; P00329; -.
DR SwissPalm; P00329; -.
DR jPOST; P00329; -.
DR PaxDb; P00329; -.
DR PeptideAtlas; P00329; -.
DR PRIDE; P00329; -.
DR ProteomicsDB; 296067; -.
DR DNASU; 11522; -.
DR Ensembl; ENSMUST00000004232; ENSMUSP00000004232; ENSMUSG00000074207.
DR GeneID; 11522; -.
DR KEGG; mmu:11522; -.
DR UCSC; uc008rnf.1; mouse.
DR CTD; 11522; -.
DR MGI; MGI:87921; Adh1.
DR VEuPathDB; HostDB:ENSMUSG00000074207; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155234; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P00329; -.
DR OMA; RVKMIAT; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P00329; -.
DR TreeFam; TF300429; -.
DR Reactome; R-MMU-2161541; Abacavir metabolism.
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR Reactome; R-MMU-71384; Ethanol oxidation.
DR SABIO-RK; P00329; -.
DR BioGRID-ORCS; 11522; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Adh1; mouse.
DR PRO; PR:P00329; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P00329; protein.
DR Bgee; ENSMUSG00000074207; Expressed in conjunctival fornix and 212 other tissues.
DR ExpressionAtlas; P00329; baseline and differential.
DR Genevisible; P00329; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; ISO:MGI.
DR GO; GO:0035276; F:ethanol binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0051287; F:NAD binding; ISO:MGI.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISO:MGI.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0046186; P:acetaldehyde biosynthetic process; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:MGI.
DR GO; GO:0006069; P:ethanol oxidation; ISO:MGI.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
DR GO; GO:0048545; P:response to steroid hormone; IDA:MGI.
DR GO; GO:0033574; P:response to testosterone; IDA:MGI.
DR GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; IMP:MGI.
DR GO; GO:0042572; P:retinol metabolic process; IMP:MGI.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06757"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160666"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 370
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:P06757"
FT MOD_RES 234
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 340
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 375 AA; 39771 MW; 7B8AF94C95D35108 CRC64;
MSTAGKVIKC KAAVLWELHK PFTIEDIEVA PPKAHEVRIK MVATGVCRSD DHVVSGTLVT
PLPAVLGHEG AGIVESVGEG VTCVKPGDKV IPLFSPQCGE CRICKHPESN FCSRSDLLMP
RGTLREGTSR FSCKGKQIHN FISTSTFSQY TVVDDIAVAK IDGASPLDKV CLIGCGFSTG
YGSAVKVAKV TPGSTCAVFG LGGVGLSVII GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYSKP IQEVLQEMTD GGVDFSFEVI GRLDTMTSAL LSCHAACGVS VVVGVPPNAQ
NLSMNPMLLL LGRTWKGAIF GGFKSKDSVP KLVADFMAKK FPLDPLITHV LPFEKINEAF
DLLRSGKSIR TVLTF
