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Q64437 (ADH7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 class 4 mu/sigma chain

EC=1.1.1.1
Alternative name(s):
ADH-C2
Alcohol dehydrogenase 7
Alcohol dehydrogenase class IV mu/sigma chain
Gastric alcohol dehydrogenase
Retinol dehydrogenase
Gene names
Name:Adh7
Synonyms:Adh-3, Adh3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

High expression in the stomach mucosa. Lower expression in eye, thymus, skin and ovary. Very low expression in small intestine, liver and uterus.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processethanol catabolic process

Inferred from mutant phenotype PubMed 10358022. Source: MGI

ethanol oxidation

Inferred from electronic annotation. Source: Ensembl

extracellular negative regulation of signal transduction

Inferred from electronic annotation. Source: Ensembl

fatty acid omega-oxidation

Inferred from electronic annotation. Source: Ensembl

response to bacterium

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

retinoic acid metabolic process

Inferred from mutant phenotype PubMed 10358022PubMed 10402668. Source: MGI

retinol metabolic process

Inferred from mutant phenotype PubMed 10358022PubMed 10402668. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: Ensembl

intracellular

Inferred from direct assay PubMed 9002638. Source: MGI

nucleolus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionalcohol dehydrogenase (NAD) activity

Inferred from direct assay PubMed 518534PubMed 6372555PubMed 7026729. Source: MGI

alcohol dehydrogenase activity, zinc-dependent

Inferred from electronic annotation. Source: Ensembl

aldehyde oxidase activity

Inferred from electronic annotation. Source: Ensembl

ethanol binding

Inferred from electronic annotation. Source: Ensembl

oxidoreductase activity

Traceable author statement PubMed 12027900. Source: MGI

retinol binding

Inferred from electronic annotation. Source: Ensembl

retinol dehydrogenase activity

Inferred from direct assay PubMed 3663136. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 374374Alcohol dehydrogenase class 4 mu/sigma chain
PRO_0000160692

Regions

Nucleotide binding199 – 2046NAD By similarity
Nucleotide binding292 – 2943NAD By similarity

Sites

Metal binding471Zinc 1; catalytic By similarity
Metal binding681Zinc 1; catalytic By similarity
Metal binding981Zinc 2 By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1121Zinc 2 By similarity
Metal binding1741Zinc 1; catalytic By similarity
Binding site2231NAD By similarity
Binding site2281NAD By similarity
Binding site3691NAD By similarity

Experimental info

Sequence conflict1201R → C in AAA76735. Ref.1
Sequence conflict1201R → C in AAC53124. Ref.2
Sequence conflict2621I → V in AAA76735. Ref.1
Sequence conflict2621I → V in AAC53124. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q64437 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: D615119A23B41843

FASTA37439,904
        10         20         30         40         50         60 
MGTAGKVIKC KAAVLWGVNQ PFSIEEIEVA PPKAKEVRVK ILATGICRTD DHIIKGSMVS 

        70         80         90        100        110        120 
KFPVIVGHEA VGVVESVGEG VTTVRPGDKV IPLFLPQCRE CNACLNPEGN LCIRSDLTGR 

       130        140        150        160        170        180 
GVLADGTTRF TCKGKPVQHF MNTSTFTEYT VLDESSVAKV DGAAPPEKAC LIGCGFSTGY 

       190        200        210        220        230        240 
GAAVKTAKVT PGSTCVVFGL GGVGLSVIMG CKAAGASRII GIDINKDKFQ KALAVGATEC 

       250        260        270        280        290        300 
ISPKDSTKPI SEVLSDMTGN TIQYTFEVIG RLETMVDALS SCHMNYGTSV VVGAPPSAKM 

       310        320        330        340        350        360 
LTYDPMLLFT GRTWKGCVFG GWKSRDDVPK LVTEFLEKKF DLDQLITHTL PFNNINEGFE 

       370 
LLYSGKSIRT VLTF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the mouse class IV alcohol dehydrogenase (retinol dehydrogenase) cDNA and tissue-specific expression patterns of the murine ADH gene family."
Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.
J. Biol. Chem. 270:10868-10877(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FVB/N.
Tissue: Gastric mucosa.
[2]"Gene structure and promoter for Adh-3 encoding mouse class IV alcohol dehydrogenase (retinol dehydrogenase)."
Zgombic-Knight M., Deltour L., Haselbeck R.J., Foglio M.H., Duester G.
Genomics 41:105-109(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20257 mRNA. Translation: AAA76735.1.
U76734 expand/collapse EMBL AC list , U76728, U76729, U76730, U76727, U76731, U76733, U76732 Genomic DNA. Translation: AAC53124.1.
AC079682 Genomic DNA. No translation available.
CCDSCCDS38651.1.
PIRA56436.
RefSeqNP_033756.2. NM_009626.4.
XP_006500982.1. XM_006500919.1.
UniGeneMm.8473.

3D structure databases

ProteinModelPortalQ64437.
SMRQ64437. Positions 2-374.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ64437.

Proteomic databases

MaxQBQ64437.
PaxDbQ64437.
PRIDEQ64437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090171; ENSMUSP00000087633; ENSMUSG00000055301.
GeneID11529.
KEGGmmu:11529.
UCSCuc008rnd.2. mouse.

Organism-specific databases

CTD131.
MGIMGI:87926. Adh7.

Phylogenomic databases

eggNOGCOG1062.
HOGENOMHOG000294674.
HOVERGENHBG000195.
InParanoidQ64437.
KOK13951.
OMAPFKQINE.
OrthoDBEOG72NRQ6.
TreeFamTF300429.

Gene expression databases

ArrayExpressQ64437.
BgeeQ64437.
GenevestigatorQ64437.

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.
IPR028635. Zinc_ADH_IV.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PTHR11695:SF406. PTHR11695:SF406. 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

NextBio278964.
PROQ64437.
SOURCESearch...

Entry information

Entry nameADH7_MOUSE
AccessionPrimary (citable) accession number: Q64437
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 122 of the entry and version 2 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

MGD cross-references

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