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

 ADH4_MOUSE              Reviewed;         377 AA.
Q9QYY9; Q3V0P5;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 4.
22-NOV-2017, entry version 137.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ZINC-BINDING, MUTAGENESIS OF
PRO-48; ASN-52 AND SER-183, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10514444; DOI=10.1074/jbc.274.42.29712;
Svensson S., Stroemberg P., Hoeoeg J.-O.;
"A novel subtype of class II alcohol dehydrogenase in rodents. Unique
Pro(47) and Ser(182) modulates hydride transfer in the mouse enzyme.";
J. Biol. Chem. 274:29712-29719(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH
NADH AND INHIBITOR AND OF MUTANT HIS-48 IN COMPLEX WITH NADH.
PubMed=10970744; DOI=10.1006/jmbi.2000.4039;
Svensson S., Hoeoeg J.-O., Schneider G., Sandalova T.;
"Crystal structures of mouse class II alcohol dehydrogenase reveal
determinants of substrate specificity and catalytic efficiency.";
J. Mol. Biol. 302:441-453(2000).
-!- FUNCTION: Involved in the reduction of benzoquinones.
{ECO:0000269|PubMed:10514444}.
-!- 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;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- SUBUNIT: Dimer. {ECO:0000269|PubMed:10970744}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:10514444}.
-!- 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; AJ245750; CAB57455.1; -; mRNA.
EMBL; AK132994; BAE21459.1; -; mRNA.
CCDS; CCDS38653.1; -.
RefSeq; NP_036126.2; NM_011996.2.
UniGene; Mm.158750; -.
PDB; 1E3E; X-ray; 2.12 A; A/B=2-377.
PDB; 1E3I; X-ray; 2.08 A; A/B=2-377.
PDB; 1E3L; X-ray; 2.50 A; A/B=2-377.
PDBsum; 1E3E; -.
PDBsum; 1E3I; -.
PDBsum; 1E3L; -.
ProteinModelPortal; Q9QYY9; -.
SMR; Q9QYY9; -.
BioGrid; 205034; 1.
IntAct; Q9QYY9; 1.
MINT; MINT-4087269; -.
STRING; 10090.ENSMUSP00000013458; -.
SwissLipids; SLP:000000496; -.
iPTMnet; Q9QYY9; -.
PhosphoSitePlus; Q9QYY9; -.
MaxQB; Q9QYY9; -.
PaxDb; Q9QYY9; -.
PRIDE; Q9QYY9; -.
Ensembl; ENSMUST00000013458; ENSMUSP00000013458; ENSMUSG00000037797.
GeneID; 26876; -.
KEGG; mmu:26876; -.
UCSC; uc008rnj.1; mouse.
CTD; 127; -.
MGI; MGI:1349472; Adh4.
eggNOG; KOG0022; Eukaryota.
eggNOG; COG1062; LUCA.
GeneTree; ENSGT00430000030800; -.
HOGENOM; HOG000294674; -.
HOVERGEN; HBG000195; -.
InParanoid; Q9QYY9; -.
KO; K13980; -.
OMA; MKAALDC; -.
OrthoDB; EOG091G08N3; -.
TreeFam; TF300429; -.
BRENDA; 1.1.1.1; 3474.
Reactome; R-MMU-5365859; RA biosynthesis pathway.
Reactome; R-MMU-71384; Ethanol oxidation.
SABIO-RK; Q9QYY9; -.
EvolutionaryTrace; Q9QYY9; -.
PRO; PR:Q9QYY9; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000037797; -.
ExpressionAtlas; Q9QYY9; baseline and differential.
Genevisible; Q9QYY9; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:MGI.
GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:MGI.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:MGI.
GO; GO:0005503; F:all-trans retinal binding; ISO:MGI.
GO; GO:0019115; F:benzaldehyde dehydrogenase activity; ISO:MGI.
GO; GO:0051287; F:NAD binding; ISO:MGI.
GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:MGI.
GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; ISO:MGI.
GO; GO:0019841; F:retinol binding; ISO:MGI.
GO; GO:0004745; F:retinol dehydrogenase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0046164; P:alcohol catabolic process; IDA:MGI.
GO; GO:0006066; P:alcohol metabolic process; ISO:MGI.
GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:MGI.
GO; GO:0006067; P:ethanol metabolic process; IDA:MGI.
GO; GO:0006069; P:ethanol oxidation; ISO:MGI.
GO; GO:1901661; P:quinone metabolic process; IDA:MGI.
GO; GO:0001523; P:retinoid metabolic process; ISO:MGI.
GO; GO:0042572; P:retinol metabolic process; ISO:MGI.
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; IPR028632; Zinc_ADH_II.
PANTHER; PTHR43880:SF14; PTHR43880:SF14; 1.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SUPFAM; SSF50129; SSF50129; 2.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00059; ADH_ZINC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Metal-binding; NAD;
Oxidoreductase; Reference proteome; Zinc.
CHAIN 1 377 Alcohol dehydrogenase 4.
/FTId=PRO_0000160682.
NP_BIND 204 209 NAD. {ECO:0000269|PubMed:10970744}.
NP_BIND 297 299 NAD. {ECO:0000269|PubMed:10970744}.
NP_BIND 320 322 NAD. {ECO:0000269|PubMed:10970744}.
METAL 47 47 Zinc 1; catalytic.
METAL 68 68 Zinc 1; catalytic.
METAL 98 98 Zinc 2.
METAL 101 101 Zinc 2.
METAL 104 104 Zinc 2.
METAL 112 112 Zinc 2.
METAL 179 179 Zinc 1; catalytic.
BINDING 49 49 NAD. {ECO:0000269|PubMed:10970744}.
BINDING 228 228 NAD. {ECO:0000269|PubMed:10970744}.
BINDING 233 233 NAD. {ECO:0000269|PubMed:10970744}.
BINDING 372 372 NAD. {ECO:0000269|PubMed:10970744}.
MUTAGEN 48 48 P->H: Strongly increases enzyme activity,
serves as proton acceptor.
{ECO:0000269|PubMed:10514444}.
MUTAGEN 52 52 N->H: No effect.
{ECO:0000269|PubMed:10514444}.
MUTAGEN 183 183 S->T: Strongly increases activity towards
ethanol, increases KM for benzoquinone
10-fold. {ECO:0000269|PubMed:10514444}.
CONFLICT 197 197 S -> G (in Ref. 1; CAB57455).
{ECO:0000305}.
CONFLICT 303 303 K -> E (in Ref. 1; CAB57455).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:1E3I}.
STRAND 23 29 {ECO:0000244|PDB:1E3I}.
STRAND 36 45 {ECO:0000244|PDB:1E3I}.
HELIX 48 52 {ECO:0000244|PDB:1E3I}.
STRAND 62 64 {ECO:0000244|PDB:1E3I}.
STRAND 69 77 {ECO:0000244|PDB:1E3I}.
STRAND 89 92 {ECO:0000244|PDB:1E3I}.
STRAND 99 101 {ECO:0000244|PDB:1E3I}.
HELIX 102 105 {ECO:0000244|PDB:1E3I}.
HELIX 121 123 {ECO:0000244|PDB:1E3I}.
STRAND 134 137 {ECO:0000244|PDB:1E3I}.
STRAND 140 143 {ECO:0000244|PDB:1E3I}.
TURN 146 148 {ECO:0000244|PDB:1E3I}.
STRAND 151 158 {ECO:0000244|PDB:1E3I}.
HELIX 159 161 {ECO:0000244|PDB:1E3I}.
STRAND 162 164 {ECO:0000244|PDB:1E3I}.
HELIX 171 174 {ECO:0000244|PDB:1E3I}.
HELIX 175 178 {ECO:0000244|PDB:1E3I}.
HELIX 180 189 {ECO:0000244|PDB:1E3I}.
TURN 190 192 {ECO:0000244|PDB:1E3E}.
STRAND 199 203 {ECO:0000244|PDB:1E3I}.
HELIX 207 218 {ECO:0000244|PDB:1E3I}.
STRAND 222 227 {ECO:0000244|PDB:1E3I}.
HELIX 231 233 {ECO:0000244|PDB:1E3I}.
HELIX 234 239 {ECO:0000244|PDB:1E3I}.
STRAND 243 246 {ECO:0000244|PDB:1E3I}.
HELIX 248 250 {ECO:0000244|PDB:1E3I}.
HELIX 255 262 {ECO:0000244|PDB:1E3I}.
STRAND 267 274 {ECO:0000244|PDB:1E3I}.
HELIX 277 285 {ECO:0000244|PDB:1E3I}.
TURN 289 291 {ECO:0000244|PDB:1E3I}.
STRAND 293 296 {ECO:0000244|PDB:1E3I}.
STRAND 300 307 {ECO:0000244|PDB:1E3I}.
HELIX 308 312 {ECO:0000244|PDB:1E3I}.
STRAND 316 319 {ECO:0000244|PDB:1E3I}.
HELIX 322 324 {ECO:0000244|PDB:1E3I}.
HELIX 327 339 {ECO:0000244|PDB:1E3I}.
HELIX 345 348 {ECO:0000244|PDB:1E3I}.
STRAND 349 354 {ECO:0000244|PDB:1E3I}.
HELIX 355 357 {ECO:0000244|PDB:1E3I}.
HELIX 358 366 {ECO:0000244|PDB:1E3I}.
STRAND 371 376 {ECO:0000244|PDB:1E3I}.
SEQUENCE 377 AA; 40211 MW; 5B527E48BB745E14 CRC64;
MGTQGKVIKC KAAIAWKTGS PLCIEEIEVS PPKACEVRIQ VIATCVCPTD INATDPKKKA
LFPVVLGHEC AGIVESVGPG VTNFKPGDKV IPFFAPQCKR CKLCLSPLTN LCGKLRNFKY
PTIDQELMED RTSRFTCKGR SIYHFMGVSS FSQYTVVSEA NLARVDDEAN LERVCLIGCG
FSSGYGAAIN TAKVTPSSTC AVFGLGCVGL SAIIGCKIAG ASRIIAIDIN GEKFPKAKAL
GATDCLNPRE LDKPVQDVIT ELTAGGVDYS LDCAGTAQTL KAAVDCTVLG WGSCTVVGAK
VDKMTIPTVD VILGRSINGT FFGGWKSVDS VPNLVSDYKN KKFDLDLLVT HALPFESIND
AIDLMKEGKS IRTILTF


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