ADH1_RAT
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 03-AUG-2022, entry version 171.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX 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 deduced
RT from the cDNA sequence.";
RL Gene 48:287-291(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX 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 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ACETYLATION AT SER-2.
RX PubMed=4673366; DOI=10.1111/j.1432-1033.1972.tb01971.x;
RA Joernvall H., Markovic O.;
RT "Structural studies of alcohol dehydrogenase from rat liver.";
RL Eur. J. Biochem. 29:167-174(1972).
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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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; NM_019286.4.
DR AlphaFoldDB; P06757; -.
DR SMR; P06757; -.
DR STRING; 10116.ENSRNOP00000016346; -.
DR ChEMBL; CHEMBL4862; -.
DR iPTMnet; P06757; -.
DR PhosphoSitePlus; P06757; -.
DR jPOST; P06757; -.
DR PaxDb; P06757; -.
DR PRIDE; P06757; -.
DR Ensembl; ENSRNOT00000085067; ENSRNOP00000069797; ENSRNOG00000012436.
DR GeneID; 24172; -.
DR KEGG; rno:24172; -.
DR CTD; 11522; -.
DR RGD; 2044; Adh1.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155234; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P06757; -.
DR OMA; RVKMIAT; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P06757; -.
DR Reactome; R-RNO-2161541; Abacavir metabolism.
DR Reactome; R-RNO-5365859; RA biosynthesis pathway.
DR Reactome; R-RNO-71384; Ethanol oxidation.
DR SABIO-RK; P06757; -.
DR PRO; PR:P06757; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012436; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; P06757; baseline and differential.
DR Genevisible; P06757; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0035276; F:ethanol binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:RGD.
DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046186; P:acetaldehyde biosynthetic process; IDA:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0048149; P:behavioral response to ethanol; ISO:RGD.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:RGD.
DR GO; GO:0006069; P:ethanol oxidation; IDA:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; ISO:RGD.
DR GO; GO:0048545; P:response to steroid hormone; ISO:RGD.
DR GO; GO:0033574; P:response to testosterone; ISO:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR GO; GO:0001523; P:retinoid metabolic process; ISO:RGD.
DR GO; GO:0042572; P:retinol metabolic process; ISO:RGD.
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:0000269|PubMed:4673366"
FT CHAIN 2..376
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160669"
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 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 201..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 294..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4673366"
FT MOD_RES 235
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00329"
FT MOD_RES 341
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00329"
FT CONFLICT 143
FT /note="I -> L (in Ref. 1; AAA40681)"
FT /evidence="ECO:0000305"
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
