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Alcohol dehydrogenase 4 (EC 1.1.1.1) (ADH2) (Alcohol dehydrogenase class II) (Alcohol dehydrogenase II)

 ADH4_RAT                Reviewed;         377 AA.
Q64563;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 117.
RecName: Full=Alcohol dehydrogenase 4;
EC=1.1.1.1;
AltName: Full=ADH2;
AltName: Full=Alcohol dehydrogenase class II;
Short=Alcohol dehydrogenase II;
Name=Adh4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7635195; DOI=10.1016/0014-5793(95)00707-G;
Hoeoeg J.-O.;
"Cloning and characterization of a novel rat alcohol dehydrogenase of
class II type.";
FEBS Lett. 368:445-448(1995).
-!- FUNCTION: Involved in the reduction of benzoquinones.
-!- CATALYTIC ACTIVITY: A primary alcohol + NAD(+) = an aldehyde +
NADH.
-!- CATALYTIC ACTIVITY: A secondary alcohol + NAD(+) = a ketone +
NADH.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBUNIT: Dimer.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Liver specific.
-!- MISCELLANEOUS: Has much lower enzymatic activity towards alcohols
and aldehydes compared to human class II ADH. Strongly inhibited
by omega-hydroxy fatty acids.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. Class-II subfamily. {ECO:0000305}.
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EMBL; X90710; CAA62241.1; -; mRNA.
PIR; S66286; S66286.
UniGene; Rn.98159; -.
ProteinModelPortal; Q64563; -.
SMR; Q64563; -.
STRING; 10116.ENSRNOP00000016891; -.
PaxDb; Q64563; -.
PRIDE; Q64563; -.
RGD; 71028; Adh4.
eggNOG; KOG0022; Eukaryota.
eggNOG; COG1062; LUCA.
HOGENOM; HOG000294674; -.
HOVERGEN; HBG000195; -.
InParanoid; Q64563; -.
PRO; PR:Q64563; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:RGD.
GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; ISO:RGD.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; ISO:RGD.
GO; GO:0005503; F:all-trans retinal binding; ISO:RGD.
GO; GO:0019115; F:benzaldehyde dehydrogenase activity; ISO:RGD.
GO; GO:0035276; F:ethanol binding; IDA:RGD.
GO; GO:0051287; F:NAD binding; IDA:RGD.
GO; GO:0003960; F:NADPH:quinone reductase activity; ISO:RGD.
GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; ISO:RGD.
GO; GO:0019841; F:retinol binding; ISO:RGD.
GO; GO:0004745; F:retinol dehydrogenase activity; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0046164; P:alcohol catabolic process; ISO:RGD.
GO; GO:0006066; P:alcohol metabolic process; ISO:RGD.
GO; GO:0006081; P:cellular aldehyde metabolic process; ISO:RGD.
GO; GO:0006067; P:ethanol metabolic process; ISO:RGD.
GO; GO:0006069; P:ethanol oxidation; IDA:RGD.
GO; GO:0042698; P:ovulation cycle; IEP:RGD.
GO; GO:1901661; P:quinone metabolic process; ISO:RGD.
GO; GO:0001523; P:retinoid metabolic process; ISO:RGD.
GO; GO:0042572; P:retinol metabolic process; ISO:RGD.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR002328; ADH_Zn_CS.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020843; PKS_ER.
InterPro; IPR028632; Zinc_ADH_II.
PANTHER; PTHR43880:SF14; PTHR43880:SF14; 1.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SMART; SM00829; PKS_ER; 1.
SUPFAM; SSF50129; SSF50129; 2.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00059; ADH_ZINC; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
Reference proteome; Zinc.
CHAIN 1 377 Alcohol dehydrogenase 4.
/FTId=PRO_0000160683.
NP_BIND 48 49 NAD. {ECO:0000250}.
NP_BIND 204 209 NAD. {ECO:0000250}.
NP_BIND 297 299 NAD. {ECO:0000250}.
NP_BIND 320 322 NAD. {ECO:0000250}.
METAL 47 47 Zinc 1; catalytic. {ECO:0000250}.
METAL 68 68 Zinc 1; catalytic. {ECO:0000250}.
METAL 98 98 Zinc 2. {ECO:0000250}.
METAL 101 101 Zinc 2. {ECO:0000250}.
METAL 104 104 Zinc 2. {ECO:0000250}.
METAL 112 112 Zinc 2. {ECO:0000250}.
METAL 179 179 Zinc 1; catalytic. {ECO:0000250}.
BINDING 228 228 NAD. {ECO:0000250}.
BINDING 233 233 NAD. {ECO:0000250}.
BINDING 372 372 NAD. {ECO:0000250}.
SEQUENCE 377 AA; 40277 MW; 9944E04A86868CBF CRC64;
MGTQGKVITC KAAIAWKTDS PLCIEEIEVS PPKAHEVRIK VIATCVCPTD INATNPKKKA
LFPVVLGHEC AGIVESVGPG VTNFKPGDKV IPFFAPQCKK CKLCLSPLTN LCGKLRNFKY
PTIDQELMED RTSRFTSKER SIYHFMGVSS FSQYTVVSEA NLARVDDEAN LERVCLIGCG
FTSGYGAAIN TAKVTPGSAC AVFGLGCVGL SAVIGCKIAG ASRIIAIDIN SEKFPKAKAL
GATDCLNPRD LDKPVQDVIT ELTGGGVDFS LDCAGTAQTL KAAVDCTVVG WGSCTVVGAK
VDEMNISTVD MILGRSVKGT FFGGWKSVDS VPNLVTDYKN KKFDLDLLVT HALPFDKIND
AIDLMNQGKS IRTILTF


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