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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 – 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
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-KW
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 4PRO_0000160682Add
BLAST

Proteomic databases

MaxQBiQ9QYY9.
PaxDbiQ9QYY9.
PRIDEiQ9QYY9.

PTM databases

PhosphoSiteiQ9QYY9.

Expressioni

Tissue specificityi

Liver specific.1 Publication

Gene expression databases

BgeeiQ9QYY9.
ExpressionAtlasiQ9QYY9. baseline and differential.
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 – 158Combined sources
Beta strandi23 – 297Combined sources
Beta strandi36 – 4510Combined sources
Helixi48 – 525Combined sources
Beta strandi62 – 643Combined sources
Beta strandi69 – 779Combined sources
Beta strandi89 – 924Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 1054Combined sources
Helixi121 – 1233Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi140 – 1434Combined sources
Turni146 – 1483Combined sources
Beta strandi151 – 1588Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1643Combined sources
Helixi171 – 1744Combined sources
Helixi175 – 1784Combined sources
Helixi180 – 18910Combined sources
Turni190 – 1923Combined sources
Beta strandi199 – 2035Combined sources
Helixi207 – 21812Combined sources
Beta strandi222 – 2276Combined sources
Helixi231 – 2333Combined sources
Helixi234 – 2396Combined sources
Beta strandi243 – 2464Combined sources
Helixi248 – 2503Combined sources
Helixi255 – 2628Combined sources
Beta strandi267 – 2748Combined sources
Helixi277 – 2859Combined sources
Turni289 – 2913Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi300 – 3078Combined sources
Helixi308 – 3125Combined sources
Beta strandi316 – 3194Combined sources
Helixi322 – 3243Combined sources
Helixi327 – 33913Combined sources
Helixi345 – 3484Combined sources
Beta strandi349 – 3546Combined sources
Helixi355 – 3573Combined sources
Helixi358 – 3669Combined sources
Beta strandi371 – 3766Combined sources

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.
InParanoidiQ9QYY9.
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

        10         20         30         40         50
MGTQGKVIKC KAAIAWKTGS PLCIEEIEVS PPKACEVRIQ VIATCVCPTD
60 70 80 90 100
INATDPKKKA LFPVVLGHEC AGIVESVGPG VTNFKPGDKV IPFFAPQCKR
110 120 130 140 150
CKLCLSPLTN LCGKLRNFKY PTIDQELMED RTSRFTCKGR SIYHFMGVSS
160 170 180 190 200
FSQYTVVSEA NLARVDDEAN LERVCLIGCG FSSGYGAAIN TAKVTPSSTC
210 220 230 240 250
AVFGLGCVGL SAIIGCKIAG ASRIIAIDIN GEKFPKAKAL GATDCLNPRE
260 270 280 290 300
LDKPVQDVIT ELTAGGVDYS LDCAGTAQTL KAAVDCTVLG WGSCTVVGAK
310 320 330 340 350
VDKMTIPTVD VILGRSINGT FFGGWKSVDS VPNLVSDYKN KKFDLDLLVT
360 370
HALPFESIND AIDLMKEGKS IRTILTF
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 Q9QYY9.
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.
ExpressionAtlasi Q9QYY9. baseline and differential.
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: October 29, 2014
This is version 115 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