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Q9QYY9

- ADH4_MOUSE

UniProt

Q9QYY9 - ADH4_MOUSE

Protein

Alcohol dehydrogenase 4

Gene

Adh4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 4 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Involved in the reduction of benzoquinones.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Zinc 1; catalytic
    Binding sitei49 – 491NAD1 Publication
    Metal bindingi68 – 681Zinc 1; catalytic
    Metal bindingi98 – 981Zinc 2
    Metal bindingi101 – 1011Zinc 2
    Metal bindingi104 – 1041Zinc 2
    Metal bindingi112 – 1121Zinc 2
    Metal bindingi179 – 1791Zinc 1; catalytic
    Binding sitei228 – 2281NAD1 Publication
    Binding sitei233 – 2331NAD1 Publication
    Binding sitei372 – 3721NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi204 – 2096NAD1 Publication
    Nucleotide bindingi297 – 2993NAD1 Publication
    Nucleotide bindingi320 – 3223NAD1 Publication

    GO - Molecular functioni

    1. alcohol dehydrogenase (NAD) activity Source: MGI
    2. alcohol dehydrogenase activity, zinc-dependent Source: MGI
    3. alditol:NADP+ 1-oxidoreductase activity Source: MGI
    4. all-trans retinal binding Source: Ensembl
    5. benzaldehyde dehydrogenase activity Source: Ensembl
    6. ethanol binding Source: InterPro
    7. NAD binding Source: Ensembl
    8. NADPH:quinone reductase activity Source: MGI
    9. retinol binding Source: Ensembl
    10. retinol dehydrogenase activity Source: Ensembl
    11. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. alcohol catabolic process Source: MGI
    2. cellular aldehyde metabolic process Source: MGI
    3. ethanol metabolic process Source: MGI
    4. ethanol oxidation Source: Ensembl
    5. quinone metabolic process Source: MGI
    6. retinol metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    SABIO-RKQ9QYY9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase 4 (EC:1.1.1.1)
    Alternative name(s):
    ADH2
    Alcohol dehydrogenase class II
    Short name:
    Alcohol dehydrogenase II
    Gene namesi
    Name:Adh4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1349472. Adh4.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule cytoskeleton Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481P → H: Strongly increases enzyme activity, serves as proton acceptor. 1 Publication
    Mutagenesisi52 – 521N → H: No effect. 1 Publication
    Mutagenesisi183 – 1831S → T: Strongly increases activity towards ethanol, increases KM for benzoquinone 10-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Alcohol dehydrogenase 4PRO_0000160682Add
    BLAST

    Proteomic databases

    MaxQBiQ9QYY9.
    PaxDbiQ9QYY9.
    PRIDEiQ9QYY9.

    PTM databases

    PhosphoSiteiQ9QYY9.

    Expressioni

    Tissue specificityi

    Liver specific.1 Publication

    Gene expression databases

    BgeeiQ9QYY9.
    GenevestigatoriQ9QYY9.

    Interactioni

    Subunit structurei

    Dimer.1 Publication

    Protein-protein interaction databases

    IntActiQ9QYY9. 1 interaction.
    MINTiMINT-4087269.
    STRINGi10090.ENSMUSP00000013458.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 158
    Beta strandi23 – 297
    Beta strandi36 – 4510
    Helixi48 – 525
    Beta strandi62 – 643
    Beta strandi69 – 779
    Beta strandi89 – 924
    Beta strandi99 – 1013
    Helixi102 – 1054
    Helixi121 – 1233
    Beta strandi134 – 1374
    Beta strandi140 – 1434
    Turni146 – 1483
    Beta strandi151 – 1588
    Helixi159 – 1613
    Beta strandi162 – 1643
    Helixi171 – 1744
    Helixi175 – 1784
    Helixi180 – 18910
    Turni190 – 1923
    Beta strandi199 – 2035
    Helixi207 – 21812
    Beta strandi222 – 2276
    Helixi231 – 2333
    Helixi234 – 2396
    Beta strandi243 – 2464
    Helixi248 – 2503
    Helixi255 – 2628
    Beta strandi267 – 2748
    Helixi277 – 2859
    Turni289 – 2913
    Beta strandi293 – 2964
    Beta strandi300 – 3078
    Helixi308 – 3125
    Beta strandi316 – 3194
    Helixi322 – 3243
    Helixi327 – 33913
    Helixi345 – 3484
    Beta strandi349 – 3546
    Helixi355 – 3573
    Helixi358 – 3669
    Beta strandi371 – 3766

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E3EX-ray2.12A/B2-377[»]
    1E3IX-ray2.08A/B2-377[»]
    1E3LX-ray2.50A/B2-377[»]
    ProteinModelPortaliQ9QYY9.
    SMRiQ9QYY9. Positions 2-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QYY9.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1062.
    GeneTreeiENSGT00430000030800.
    HOGENOMiHOG000294674.
    HOVERGENiHBG000195.
    InParanoidiQ3V0P5.
    KOiK13980.
    OMAiPLTNLCG.
    TreeFamiTF300429.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. 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]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PTHR11695:SF308. PTHR11695:SF308. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QYY9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTQGKVIKC KAAIAWKTGS PLCIEEIEVS PPKACEVRIQ VIATCVCPTD    50
    INATDPKKKA LFPVVLGHEC AGIVESVGPG VTNFKPGDKV IPFFAPQCKR 100
    CKLCLSPLTN LCGKLRNFKY PTIDQELMED RTSRFTCKGR SIYHFMGVSS 150
    FSQYTVVSEA NLARVDDEAN LERVCLIGCG FSSGYGAAIN TAKVTPSSTC 200
    AVFGLGCVGL SAIIGCKIAG ASRIIAIDIN GEKFPKAKAL GATDCLNPRE 250
    LDKPVQDVIT ELTAGGVDYS LDCAGTAQTL KAAVDCTVLG WGSCTVVGAK 300
    VDKMTIPTVD VILGRSINGT FFGGWKSVDS VPNLVSDYKN KKFDLDLLVT 350
    HALPFESIND AIDLMKEGKS IRTILTF 377
    Length:377
    Mass (Da):40,211
    Last modified:June 28, 2011 - v4
    Checksum:i5B527E48BB745E14
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti197 – 1971S → G in CAB57455. (PubMed:10514444)Curated
    Sequence conflicti303 – 3031K → E in CAB57455. (PubMed:10514444)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ245750 mRNA. Translation: CAB57455.1.
    AK132994 mRNA. Translation: BAE21459.1.
    CCDSiCCDS38653.1.
    RefSeqiNP_036126.2. NM_011996.2.
    UniGeneiMm.158750.

    Genome annotation databases

    EnsembliENSMUST00000013458; ENSMUSP00000013458; ENSMUSG00000037797.
    GeneIDi26876.
    KEGGimmu:26876.
    UCSCiuc008rnj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ245750 mRNA. Translation: CAB57455.1 .
    AK132994 mRNA. Translation: BAE21459.1 .
    CCDSi CCDS38653.1.
    RefSeqi NP_036126.2. NM_011996.2.
    UniGenei Mm.158750.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E3E X-ray 2.12 A/B 2-377 [» ]
    1E3I X-ray 2.08 A/B 2-377 [» ]
    1E3L X-ray 2.50 A/B 2-377 [» ]
    ProteinModelPortali Q9QYY9.
    SMRi Q9QYY9. Positions 2-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9QYY9. 1 interaction.
    MINTi MINT-4087269.
    STRINGi 10090.ENSMUSP00000013458.

    PTM databases

    PhosphoSitei Q9QYY9.

    Proteomic databases

    MaxQBi Q9QYY9.
    PaxDbi Q9QYY9.
    PRIDEi Q9QYY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000013458 ; ENSMUSP00000013458 ; ENSMUSG00000037797 .
    GeneIDi 26876.
    KEGGi mmu:26876.
    UCSCi uc008rnj.1. mouse.

    Organism-specific databases

    CTDi 127.
    MGIi MGI:1349472. Adh4.

    Phylogenomic databases

    eggNOGi COG1062.
    GeneTreei ENSGT00430000030800.
    HOGENOMi HOG000294674.
    HOVERGENi HBG000195.
    InParanoidi Q3V0P5.
    KOi K13980.
    OMAi PLTNLCG.
    TreeFami TF300429.

    Enzyme and pathway databases

    SABIO-RK Q9QYY9.

    Miscellaneous databases

    EvolutionaryTracei Q9QYY9.
    NextBioi 304683.
    PROi Q9QYY9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QYY9.
    Genevestigatori Q9QYY9.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. 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 ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    PTHR11695:SF308. PTHR11695:SF308. 1 hit.
    Pfami PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 2 hits.
    PROSITEi PS00059. ADH_ZINC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiADH4_MOUSE
    AccessioniPrimary (citable) accession number: Q9QYY9
    Secondary accession number(s): Q3V0P5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 114 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3