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Q9QYY9 (ADH4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 4

EC=1.1.1.1
Alternative name(s):
ADH2
Alcohol dehydrogenase class II
Short name=Alcohol dehydrogenase II
Gene names
Name:Adh4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the reduction of benzoquinones. Ref.1

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Dimer.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Liver specific. Ref.1

Miscellaneous

Has much lower enzymatic activity towards alcohols and aldehydes compared to human class II ADH. Strongly inhibited by omega-hydroxy fatty acids.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-II subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalcohol catabolic process

Inferred from direct assay Ref.1. Source: MGI

cellular aldehyde metabolic process

Inferred from direct assay Ref.1. Source: MGI

ethanol metabolic process

Inferred from direct assay PubMed 518534. Source: MGI

ethanol oxidation

Inferred from electronic annotation. Source: Ensembl

quinone metabolic process

Inferred from direct assay Ref.1. Source: MGI

retinol metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule cytoskeleton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: Ensembl

NADPH:quinone reductase activity

Inferred from direct assay Ref.1. Source: MGI

alcohol dehydrogenase (NAD) activity

Inferred from direct assay PubMed 518534. Source: MGI

alcohol dehydrogenase activity, zinc-dependent

Inferred from direct assay Ref.1. Source: MGI

alditol:NADP+ 1-oxidoreductase activity

Inferred from direct assay Ref.1. Source: MGI

all-trans retinal binding

Inferred from electronic annotation. Source: Ensembl

benzaldehyde dehydrogenase activity

Inferred from electronic annotation. Source: Ensembl

ethanol binding

Inferred from electronic annotation. Source: InterPro

retinol binding

Inferred from electronic annotation. Source: Ensembl

retinol dehydrogenase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Alcohol dehydrogenase 4
PRO_0000160682

Regions

Nucleotide binding204 – 2096NAD
Nucleotide binding297 – 2993NAD
Nucleotide binding320 – 3223NAD

Sites

Metal binding471Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1791Zinc 1; catalytic
Binding site491NAD
Binding site2281NAD
Binding site2331NAD
Binding site3721NAD

Experimental info

Mutagenesis481P → H: Strongly increases enzyme activity, serves as proton acceptor. Ref.1
Mutagenesis521N → H: No effect. Ref.1
Mutagenesis1831S → T: Strongly increases activity towards ethanol, increases KM for benzoquinone 10-fold. Ref.1
Sequence conflict1971S → G in CAB57455. Ref.1
Sequence conflict3031K → E in CAB57455. Ref.1

Secondary structure

........................................................................... 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QYY9 [UniParc].

Last modified June 28, 2011. Version 4.
Checksum: 5B527E48BB745E14

FASTA37740,211
        10         20         30         40         50         60 
MGTQGKVIKC KAAIAWKTGS PLCIEEIEVS PPKACEVRIQ VIATCVCPTD INATDPKKKA 

        70         80         90        100        110        120 
LFPVVLGHEC AGIVESVGPG VTNFKPGDKV IPFFAPQCKR CKLCLSPLTN LCGKLRNFKY 

       130        140        150        160        170        180 
PTIDQELMED RTSRFTCKGR SIYHFMGVSS FSQYTVVSEA NLARVDDEAN LERVCLIGCG 

       190        200        210        220        230        240 
FSSGYGAAIN TAKVTPSSTC AVFGLGCVGL SAIIGCKIAG ASRIIAIDIN GEKFPKAKAL 

       250        260        270        280        290        300 
GATDCLNPRE LDKPVQDVIT ELTAGGVDYS LDCAGTAQTL KAAVDCTVLG WGSCTVVGAK 

       310        320        330        340        350        360 
VDKMTIPTVD VILGRSINGT FFGGWKSVDS VPNLVSDYKN KKFDLDLLVT HALPFESIND 

       370 
AIDLMKEGKS IRTILTF 

« Hide

References

« Hide 'large scale' references
[1]"A novel subtype of class II alcohol dehydrogenase in rodents. Unique Pro(47) and Ser(182) modulates hydride transfer in the mouse enzyme."
Svensson S., Stroemberg P., Hoeoeg J.-O.
J. Biol. Chem. 274:29712-29719(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ZINC-BINDING, MUTAGENESIS OF PRO-48; ASN-52 AND SER-183, TISSUE SPECIFICITY.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[3]"Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency."
Svensson S., Hoeoeg J.-O., Schneider G., Sandalova T.
J. Mol. Biol. 302:441-453(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH NADH AND INHIBITOR AND OF MUTANT HIS-48 IN COMPLEX WITH NADH.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ245750 mRNA. Translation: CAB57455.1.
AK132994 mRNA. Translation: BAE21459.1.
CCDSCCDS38653.1.
RefSeqNP_036126.2. NM_011996.2.
UniGeneMm.158750.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E3EX-ray2.12A/B2-377[»]
1E3IX-ray2.08A/B2-377[»]
1E3LX-ray2.50A/B2-377[»]
ProteinModelPortalQ9QYY9.
SMRQ9QYY9. Positions 2-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QYY9. 1 interaction.
MINTMINT-4087269.
STRING10090.ENSMUSP00000013458.

PTM databases

PhosphoSiteQ9QYY9.

Proteomic databases

MaxQBQ9QYY9.
PaxDbQ9QYY9.
PRIDEQ9QYY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000013458; ENSMUSP00000013458; ENSMUSG00000037797.
GeneID26876.
KEGGmmu:26876.
UCSCuc008rnj.1. mouse.

Organism-specific databases

CTD127.
MGIMGI:1349472. Adh4.

Phylogenomic databases

eggNOGCOG1062.
GeneTreeENSGT00430000030800.
HOGENOMHOG000294674.
HOVERGENHBG000195.
InParanoidQ3V0P5.
KOK13980.
OMAPLTNLCG.
TreeFamTF300429.

Enzyme and pathway databases

SABIO-RKQ9QYY9.

Gene expression databases

BgeeQ9QYY9.
GenevestigatorQ9QYY9.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR028632. Zinc_ADH_II.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PTHR11695:SF308. PTHR11695:SF308. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 2 hits.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9QYY9.
NextBio304683.
PROQ9QYY9.
SOURCESearch...

Entry information

Entry nameADH4_MOUSE
AccessionPrimary (citable) accession number: Q9QYY9
Secondary accession number(s): Q3V0P5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 113 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot