ID   ADH1_RAT                Reviewed;         376 AA.
AC   P06757;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 78.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase A subunit;
GN   Name=Adh1; Synonyms=Adh-1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=87163532; PubMed=2881847; DOI=10.1016/0378-1119(86)90087-9;
RA   Crabb D.W., Edenberg H.J.;
RT   "Complete amino acid sequence of rat liver alcohol dehydrogenase
RT   deduced from the cDNA sequence.";
RL   Gene 48:287-291(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=90077433; PubMed=2591969; DOI=10.1016/0888-7543(89)90133-X;
RA   Crabb D.W., Stein P.M., Dipple K.M., Hittle J.B., Sidhu R., Qulali M.,
RA   Zhang K., Edenberg H.J.;
RT   "Structure and expression of the rat class I alcohol dehydrogenase
RT   gene.";
RL   Genomics 5:906-914(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [4]
RP   ACETYLATION AT SER-2.
RX   MEDLINE=73031732; PubMed=4673366;
RX   DOI=10.1111/j.1432-1033.1972.tb01971.x;
RA   Jornvall H., Markovic O.;
RT   "Structural studies of alcohol dehydrogenase from rat liver.";
RL   Eur. J. Biochem. 29:167-174(1972).
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   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-I subfamily.
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DR   EMBL; M29523; AAA85462.1; -; Genomic_DNA.
DR   EMBL; M29516; AAA85462.1; JOINED; Genomic_DNA.
DR   EMBL; M29517; AAA85462.1; JOINED; Genomic_DNA.
DR   EMBL; M29518; AAA85462.1; JOINED; Genomic_DNA.
DR   EMBL; M29519; AAA85462.1; JOINED; Genomic_DNA.
DR   EMBL; M29520; AAA85462.1; JOINED; Genomic_DNA.
DR   EMBL; M29521; AAA85462.1; JOINED; Genomic_DNA.
DR   EMBL; M29522; AAA85462.1; JOINED; Genomic_DNA.
DR   EMBL; M15327; AAA40681.1; -; mRNA.
DR   EMBL; BC062403; AAH62403.1; -; mRNA.
DR   PIR; A26468; A26468.
DR   RefSeq; NP_062159.3; -.
DR   UniGene; Rn.40222; -.
DR   HSSP; P00326; 1HT0.
DR   SMR; P06757; 2-376.
DR   Ensembl; ENSRNOG00000012464; Rattus norvegicus.
DR   GeneID; 24172; -.
DR   KEGG; rno:24172; -.
DR   RGD; 2044; Adh1.
DR   HOVERGEN; P06757; -.
DR   NextBio; 602493; -.
DR   ArrayExpress; P06757; -.
DR   GermOnline; ENSRNOG00000012464; Rattus norvegicus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    376       Alcohol dehydrogenase 1.
FT                                /FTId=PRO_0000160669.
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       176    176       Zinc 1; catalytic.
FT   MOD_RES       2      2       N-acetylserine.
FT   CONFLICT    143    143       I -> L (in Ref. 1; AAA40681).
SQ   SEQUENCE   376 AA;  39645 MW;  3C7026C6D7C0ED76 CRC64;
     MSTAGKVIKC KAAVLWEPHK PFTIEDIEVA PPKAHEVRIK MVATGVCRSD DHAVSGSLFT
     PLPAVLGHEG AGIVESIGEG VTCVKPGDKV IPLFSPQCGK CRICKHPESN LCCQTKNLTQ
     PKGALLDGTS RFSCRGKPIH HFISTSTFSQ YTVVDDIAVA KIDAAAPLDK VCLIGCGFST
     GYGSAVQVAK VTPGSTCAVF GLGGVGLSVV IGCKTAGAAK IIAVDINKDK FAKAKELGAT
     DCINPQDYTK PIQEVLQEMT DGGVDFSFEV IGRLDTMTSA LLSCHSACGV SVIVGVPPSA
     QSLSVNPMSL LLGRTWKGAI FGGFKSKDAV PKLVADFMAK KFPLEPLITH VLPFEKINEA
     FDLLRAGKSI RTVLTF
//