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Q9QYY9

- ADH4_MOUSE

UniProt

Q9QYY9 - ADH4_MOUSE

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Protein
Alcohol dehydrogenase 4
Gene
Adh4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 491NAD
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 – 2281NAD
Binding sitei233 – 2331NAD
Binding sitei372 – 3721NAD

Regions

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

GO - Molecular functioni

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

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
Complete GO annotation...

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 4
PRO_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.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971S → G in CAB57455. 1 Publication
Sequence conflicti303 – 3031K → E in CAB57455. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 113 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

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