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   25-NOV-2008, entry version 88.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase A subunit;
DE   AltName: Full=ADH-A2;
GN   Name=Adh1; Synonyms=Adh-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=85190477; PubMed=3157987;
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
RT   alcohol dehydrogenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:2262-2266(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88137953; 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
RT   sequence of the Adh-1 gene and genetic mapping of a related nucleotide
RT   sequence to chromosome 3.";
RL   Gene 59:171-182(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88112859; 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
RT   a long alternating purine-pyrimidine sequence in the first intron of
RT   strains 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-51.
RX   MEDLINE=95023181; 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
RT   in 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   MEDLINE=86221702; PubMed=3011597; DOI=10.1016/0378-1119(86)90101-0;
RA   Ceci J.D., Lawther R., Duester G., Hatfield G.W., Smith M.,
RA   O'Malley M.P., Felder M.R.;
RT   "Androgen induction of alcohol dehydrogenase in mouse kidney. Studies
RT   with a cDNA probe confirmed by nucleotide sequence analysis.";
RL   Gene 41:217-224(1986).
RN   [7]
RP   TISSUE SPECIFICITY.
RC   STRAIN=FVB/N;
RX   MEDLINE=95256259; 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
RT   murine ADH gene family.";
RL   J. Biol. Chem. 270:10868-10877(1995).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit.
CC   -!- SUBUNIT: Dimer of identical or non-identical chains of three types
CC       (A, 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,
CC       and at low levels in the spinal cord, thymus, heart, stomach
CC       mucosa, skin and testis.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-I subfamily.
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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   PIR; A27322; DEMSAA.
DR   RefSeq; NP_031435.1; -.
DR   UniGene; Mm.2409; -.
DR   UniGene; Mm.412004; -.
DR   HSSP; P00326; 1HT0.
DR   SMR; P00329; 2-375.
DR   PhosphoSite; P00329; -.
DR   Ensembl; ENSMUSG00000074207; Mus musculus.
DR   GeneID; 11522; -.
DR   KEGG; mmu:11522; -.
DR   MGI; MGI:87921; Adh1.
DR   HOGENOM; P00329; -.
DR   HOVERGEN; P00329; -.
DR   NextBio; 278960; -.
DR   ArrayExpress; P00329; -.
DR   CleanEx; MM_ADH1; -.
DR   GermOnline; ENSMUSG00000074207; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004022; F:alcohol dehydrogenase activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR   GO; GO:0006068; P:ethanol catabolic process; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
DR   GO; GO:0033574; P:response to testosterone stimulus; IDA:MGI.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI.
DR   GO; GO:0042572; P:retinol metabolic process; IMP:MGI.
DR   InterPro; IPR013154; AlcDHase_GroES-like.
DR   InterPro; IPR002085; AlcDHase_SF_Zn.
DR   InterPro; IPR013149; AlcDHase_Zn-bd.
DR   InterPro; IPR002328; AlcDHase_Zn_CS.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    375       Alcohol dehydrogenase 1.
FT                                /FTId=PRO_0000160666.
FT   METAL        47     47       Zinc 1; catalytic.
FT   METAL        68     68       Zinc 1; catalytic.
FT   METAL        98     98       Zinc 2.
FT   METAL       101    101       Zinc 2.
FT   METAL       104    104       Zinc 2.
FT   METAL       112    112       Zinc 2.
FT   METAL       175    175       Zinc 1; catalytic.
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
//