Open Close
General Information
Symbol
Dmel\Adh
Species
D. melanogaster
Name
Alcohol dehydrogenase
Annotation Symbol
CG3481
Feature Type
FlyBase ID
FBgn0000055
Gene Model Status
Stock Availability
Enzyme Name (EC)
Alcohol dehydrogenase (1.1.1.1)
Acetaldehyde dehydrogenase (acetylating) (1.2.1.10)
Gene Snapshot
Alcohol dehydrogenase (Adh) encodes an alcohol and acetaldehyde dehydrogenase involved in alcohol and acetaldehyde metabolism. [Date last reviewed: 2019-09-12]
Also Known As

DmADH, BG:DS01486.8

Key Links
Genomic Location
Cytogenetic map
Sequence location
2L:14,615,552..14,618,902 [+]
Recombination map

2-50

RefSeq locus
NT_033779 REGION:14615552..14618902
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Gene Ontology (GO) Annotations (13 terms)
Molecular Function (4 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN002451415
(assigned by GO_Central )
Biological Process (7 terms)
Terms Based on Experimental Evidence (7 terms)
CV Term
Evidence
References
inferred from direct assay
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProt )
inferred from mutant phenotype
inferred from mutant phenotype
inferred from direct assay
inferred from direct assay
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN002451415
(assigned by GO_Central )
Cellular Component (2 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN002451415
(assigned by GO_Central )
Protein Family (UniProt)
Belongs to the short-chain dehydrogenases/reductases (SDR) family. (P00334)
Catalytic Activity (EC)
Experimental Evidence
(1) A primary alcohol + NAD(+) = an aldehyde + NADH (1.1.1.1)
(2) A secondary alcohol + NAD(+) = a ketone + NADH (1.1.1.1)
Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH (1.2.1.10)
Predictions / Assertions
-
Summaries
Gene Group (FlyBase)
ALCOHOL DEHYDROGENASES -
Alcohol dehydrogenases are NAD dependent oxidoreductases that are involved in the interconversion between alcohols and aldehydes or ketones. (Adapted from FBrf0096056).
ALDEHYDE OR OXO OXIDOREDUCTASES, NAD OR NADP AS ACCEPTOR -
Aldehyde or oxo oxidoreductases with NAD or NADP as acceptor, include dehydrogenases that oxidize an aldehyde or ketone (oxo) group with the reduction of NAD or NADP.
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
Adh: Alcohol dehydrogenase (M. Ashburner)
Structural gene for alcohol dehydrogenase [ADH (EC 1.1.1.1)]. Natural populations are polymorphic for three electrophoretic alleles (AdhF, AdhS, AdhF-ChD) and for three rarer electrophoretic alleles (AdhUS, AdhF', AdhUF). The frequency of the AdhF allele increases, at the expense of AdhS, with increasing latitude in both northern and southern hemispheres [Johnson and Schaffer, 1973, Biochem. Genet. 10: 149-63; Vigue and Johnson, 1973, Biochem. Genet. 9: 213-27; Wilks, Gibson, Oakeshott and Chambers, 1980, Aust. J. Biol. Sci. 33: 575-85; Anderson, 1981, Genetic Studies of Drosophila Populations (Gibson and Oakes, eds.). Australian National University Press, pp. 237-50; Anderson and Chambers, 1982, Evolution 36: 86-96]. Confers resistance to ethanol; flies lacking ADH rapidly become intoxicated and eventually die on exposure to ethanol (Grell, Jacobson and Murphy, 1968, Ann. N.Y. Acad. Sci 151: 441-45; Vigue and Sofer, 1976, Biochem. Genet. 14: 127-135; David, Bocquet, Arens and Fouillet, 1976, Biochem. Genet. 14: 989-97). However, ethanol sensitivity is complex since even Adh nulls are more resistant to ethanol when young than when old (Vigue and Sofer, 1976; Tsubota). Adh+ flies are killed by low concentrations of unsaturated secondary alcohols (e.g. 1-penten-3-ol; 1-pentyn-3-ol) but not by unsaturated primary alcohols (e.g. 1-penten-1-ol) (Sofer and Hatkoff, 1972, Genetics 72: 545-49), presumably due to the formation of toxic ketones. This allows the chemical selection of Adh nulls (Sofer and Hatkoff, 1972; O'Donnell, Gerace, Leister and Sofer, 1975, Genetics 79: 73-83). ADH may play a metabolic role independent of alcohol detoxication, i.e. in the metabolism of higher alcohols (see Winberg, Thatcher and McKinley-McKee, 1982, Biochem. Biophys. Acta 704: 7-16). ADH also catalyses the oxidation of acetaldehyde to acetate (Heinstra, Eisses, Schoonen, Aben, de Winter, van de Horst, van Marrewijk, Beenakkers, Scharloo and Thorig, 1983, Genetica 60: 129-37; Moxon, Holmes, Parsons, Irving, and Doddrell, 1985, Comp. Biochem. Physiol. 80B: 525-35). Specific activity of ADH changes with development, with peaks at the end of the third larval instar and about four days after eclosion (Ursprung, Sofer and Burroughs, 1970, Wilhelm Roux's Arch. Entwicklungsmech. Org. 164: 201-08; Dunn, Wilson and Jacobson, 1969, J. Exp. Zool. 171: 185-90; Leibenguth, Rammo and Dubiczky, 1979, Wilhelm Roux's Arch. Dev. Biol. 187: 81-88; Maroni and Stamey, 1983, DIS 59: 77-79; Anderson and McDonald, 1981, Canad. J. Genet. Cytol. 23: 305-13). Most of the activity is in the larval fat body and gut and the adult fat body (Ursprung, Sofer and Burroughs). Maternal inheritance of ADH by embryos and larvae (O'Donnell et al.; Leibenguth et al.). Half life of ADH-F in vivo estimated as 55.3 hours (Anderson and McDonald, 1981, Biochem. Genet. 19: 411-19). Not expressed in SL2 tissue culture cells, but transfected cloned gene is (Benyajati and Dray, 1984, Proc. Nat. Acad. Sci. 1701-05). Ethanol tolerance usually correlated with ADH activity and polymorphic experimental populations exposed to ethanol usually show an increase in the frequency AdhF (McDonald and Avise, 1976, Biochem. Genet. 14: 347-55; Cavener and Clegg, 1978, Genetics 90: 629-44; van Delden, Kamping and van Dijk, 1975, Experientia 31: 418-19; Oakeshott, Gibson, Anderson and Champ, 1980, Aust. J. Biol. Sci. 33: 105-14; McDonald, Chambers, David and Ayala, 1977, Proc. Nat. Acad. Sci. USA 74: 4562-66). Flies carrying AdhF tend to be more resistant than those carrying only AdhS to ethanol [Kamping and van Delden, 1978, Biochem. Genet. 16: 541-55; Ainsley and Kitto, 1975, Isozymes (C. Markert, ed.). Academic Press, Vol. II, pp. 733-43; Briscoe, Robertson and Malpica, 1975, Nature (London) 253: 148-49]. Electrophoresis of homozygous genotypes usually reveals three interconvertable isozymes [Ursprung and Leone; Johnson and Denniston; Grell et al., 1965; Ursprung and Carlin, 1968, Ann. N.Y. Acad. Sci. 151: 456-75; Jacobson, Murphy and Hartmann, 1970, J. Biol. Chem. 245: 1075-83; Jacobson and Pfuderer, 1970, J. Biol. Chem. 245: 3938-44; Jacobson, Murphy and Ortiz, 1972, Arch. Biochem. Biophys. 149: 22-35; Knopp and Jacobson, 1972, Arch. Biochem. Biophys. 149: 36-41; Schwartz, Gerace, O'Donnell and Sofer, 1975, Isoenzymes (C. Markert, ed.). Academic Press, Vol. I, pp. 725-51]. These vary in activity and stability, the most cathodal being more active, but less stable, than the more anodal forms. They probably result from the binding of 0, 1 or 2 moles per mole of a NAD+ addition complex with a carbonyl compound [Schwartz and Sofer, 1976, Nature (London) 263: 129-31; Schwartz, O'Donnell and Sofer, 1979, Arch. Biochem. Biophys. 194: 365-78; Winberg, Thatcher and McKinley-McKee, 1983, Biochem. Genet. 21: 63-80]. Feeding flies acetone, propan-2-ol, or 3-hydroxy-butanone, for example, converts isozymes to most anodal form and results in loss of enzyme activity in vitro and in vivo (Schwartz and Sofer, 1976; Papel, Henderson, van Herrewege, David and Sofer, 1979, Biochem. Genet. 17: 533-63). ADH has been purified (Sofer and Ursprung, 1968, J. Biol. Chem. 243: 3118-25; Schwartz et al., 1975; Thatcher, 1977, Biochem. J. 163: 317-23; Leigh Brown and Lee, 1979, Biochem. J. 179: 479-82; Juan and Gonzalez-Duarte, 1980, Biochem. J. 189: 105-10; Elliot and Knopp, 1975, Methods Enzymol. 41: 374-79; Chambers, 1984, Biochem. Genet. 22: 529-50). It is a homodimer with monomeric subunit molecular weight of 27500 daltons (Thatcher, 1980, Biochem. J. 187: 875-83); molecular extinction coefficient 4.8 X 104 liter/mol/cm (Juan and Gonzalez-Duarte, for ADH-S). Complete amino acid sequence determined by Thatcher (1980; see also Schwartz and Jornvall, 1976, Europ. J. Biochem. 68: 159-68; Auffret, Williams and Thatcher, 1978, FEBS Lett. 90: 324-26; Benyajati, Place, Powers, and Sofer, 1981, Proc. Nat. Acad. Sci. USA 78: 2317-21; Chambers, Laver, Campbell and Gibson, 1981, Proc. Nat. Acad. Sci. USA 78: 3103-07) with secondary structure predictions (Thatcher and Sawyer, 1980, Biochem J. 187: 884-86; Benyajati et al., 1981). Limited homology in supposed catalytic region with ribitol dehydrogenase of Klebsiella (Jornvall, Persson and Jeffry, 1981, Proc. Nat. Acad. Sci. USA 78: 4226-30). ADH shows a broad substrate specificity but is more active (by at least a factor of 5) with secondary than primary alcohols and shows highest activity to 3-6 carbon alcohols (Sofer and Ursprung; Thatcher and Camfield, 1977, Winberg et al., 1982, Chambers et al.). Differences in substrate specificity, kinetic constants and stability of different electrophoretic variants often reported (Anderson and McDonald, 1983, Proc. Nat. Acad. Sci. USA 80: 4798-802). Considerable heterogeneity in the specific activity of ADH within and between different AdhF and AdhS strains, though AdhS strains tend to be lower than AdhF [Day, Hillier and Clarke, 1974, Biochem. Genet. 11: 141-53, 155-65; Day and Needham, 1974, Biochem. Genet. 11: 167-75; Gibson, 1970, Nature (London) 227: 959-61; Gibson, Chambers, Wilkes and Oakeshott, 1980, Aust. J. Biol. Sci. 33: 479-89; Gibson and Miklovitch, 1971, Experientia 27: 99-100; Kreitman, 1980, Genetics 95: 467-75; Oakeshott, 1976, Aust. J. Biol. Sci. 29: 365-73; Sampsell, 1977, Biochem. Genet. 15: 971-88; Sampsell and Sims, 1982, Nature (London) 296: 853-55; Thorig, Schoone and Scharloo, 1975; Biochem. Genet. 13: 721-31; Vigue and Johnson; Hewitt, Pipkin, Williams and Chakrabartty, 1974, J. Hered. 65: 141-44; Ward, 1974, Biochem. Genet. 12: 449-58; Ward, 1975, Genet. Res. 26: 81-93; Maroni, Laurie-Ahlberg, Adams and Wilton, 1982, Genetics 101: 431-66; Rasmuson, Nilson and Zeppezauer, 1966, Hereditas 56: 313-16; Clarke, Camfield, Garvin and Pitts, 1979, Nature (London) 180: 517-18; Laurie-Ahlberg, Maroni, Bewley, Lucchesi and Weil, 1980, Proc. Nat. Acad. Sci. USA 77: 1073-77; Barnes and Birley, 1978, Heredity 40: 51-57; Barnes and Birley, 1978, Biochem. Genet. 16: 155-65; McDonald and Ayala, 1978, Genetics 89: 371-88; McDonald et al., 1980; Lewis and Gibson, 1978, Biochem. Genet. 16: 159-70]. With the exception of the studies by Thatcher and Sheik (1981, Biochem. J. 197: 111-17), Winberg et al. (1982), McDonald, Anderson and Santos (1980, Genetics 95: 1013-22); Eisses, Schoonen, Aben, Scharloo, and Thorig (1985, Mol. Gen. Genet. 199: 76-81) and Moxon et al. (1985), these were all done with crude extracts and not purified enzyme. Thatcher and Sheikh find the relative thermostabilities to be ADH-S > ADH-F > ADH-n5 > ADH-D. ADH-S shows slower dissociation of NADH from NADN-enzyme complex than ADH-F (Winberg, Hovik, and McKinley-McKee, 1985, Biochem. Genet. 23: 205-16). ADH is not a metalloenzyme (Place, Powers and Sofer, 1980, Fed. Proc. 39: 1640); but, paradoxically, is inhibited by certain metal ion chelators, e.g. pyrazole (Place, Powers and Sofer; Winberg et al., 1982; Moxon et al., 1985). Utilization of ethanol as an energy source (van Herrewege and David, 1974, C. Rend. Acad. Sci. Paris 279D: 335-38; van Herrewege, David and Grantham, 1980, Experientia 36: 846-47; Libion-Mannaert, Delcour, Deltombe-Lietaert, Lenelle-Montfort and Elens, 1976, Experentia 32: 22-23) depends on ADH activity (David, Bocquet, van Herrewege, Fouillet and Arens, 1978, Biochem. Genet. 16: 203-11). AdhF homozygotes usually show a better ability to survive on ethanol as a sole energy source than AdhS homozygotes (Daly and Clarke, 1981, Heredity 46: 219-26; Anderson, McDonald and Santos, 1981, Experientia 37: 463-64). AdhF and AdhS homozygotes also show behavioural differences in their response to ethanol (Parsons, 1977 Oecologia 30: 141-46; Cavener, 1979, Behav. Genet. 9: 359-65; Gelan and McDonald, 1980, Behav. Genet. 10: 237-49; Hougonto, Lietaert, Libion-Mannaert, Feytmans and Elens, 1982, Genetica 58: 121-28; Parsons, 1980, Behav. Genet. 10: 183-90; Parsons, 1980, Experientia 36: 1070-71). D. simulans enzyme monomers form heterodimers with those of D. melanogaster (E.H. Grell); D. simulans enzyme purified (Juan and Gonzalez-Duarte, 1981, Biochem. J. 195: 61-69). Sequence of D. simulans ADH (from DNA) similar to that of AdhS with following changes: ser1 -> ala1; gln82 -> lys82; ile184 -> val184 (Bodmer and Ashburner, 1984, Nature 309: 425-30). D. simulans and D. melanogaster enzymes differentially regulated in hybrids (Dickenson, Rowan, and Brennan, 1984, Heredity 52: 215-25). The Adh genes from D. orena and D. mauritiana have also been sequenced (Bodmer and Ashburner), and those of D. erecta, D. teissieri and D. yakuba mapped with restriction enzymes (Langley, Montgomery and Quattlebaum, 1982, Proc. Nat. Acad. Sci. USA 79: 5631-35).
Gene Model and Products
Number of Transcripts
5
Number of Unique Polypeptides
1

Please see the JBrowse view of Dmel\Adh for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model

Dicistronic transcript isoform(s) appear to be relatively rare based on RNA-Seq and/or EST data.

Gene model reviewed during 5.52

Low-frequency RNA-Seq exon junction(s) not annotated.

gene_with_dicistronic_mRNA ; SO:0000722

Gene model reviewed during 5.55

Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0100589
1057
256
FBtr0100590
1001
256
FBtr0100591
2080
256
FBtr0100593
2024
256
FBtr0100594
1231
256
Additional Transcript Data and Comments
Reported size (kB)

1.0 (northern blot)

1.150 (northern blot)

1.5 (northern blot)

0.760 (sequence analysis)

1.120 (northern blot)

Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0100045
27.7
256
7.57
FBpp0100047
27.7
256
7.57
FBpp0100048
27.7
256
7.57
FBpp0100050
27.7
256
7.57
FBpp0100051
27.7
256
7.57
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

256 aa isoforms: Adh-PC, Adh-PE, Adh-PF, Adh-PH, Adh-PI
Additional Polypeptide Data and Comments
Reported size (kDa)
Comments

In vitro transcribed protein from a genomic Adh clone (gAC1 and sAC1) which was bound by an immobilized Adh antibody was run on a gel to show one protein product with an approximate size of 24kD. No Adh protein was recovered from an Actin clone or without the addition of DNA.

External Data
Subunit Structure (UniProtKB)

Homodimer.

(UniProt, P00334)
Linkouts
Sequences Consistent with the Gene Model
Nucleotide / Polypeptide Records
 
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Adh using the Feature Mapper tool.

External Data
Crossreferences
Linkouts
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
expression microarray
Stage
Tissue/Position (including subcellular localization)
Reference
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
cell

Comment: all cells of cell layer

northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
Marker for
Subcellular Localization
CV Term
Polypeptide Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
enzyme assay or biochemical detection
Stage
Tissue/Position (including subcellular localization)
Reference
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

As the concentration of ethanol in the diet is increased, the amount of Adh protein in the midgut increases. None is observed in the foregut or hindgut.

Monoclonal antibodies MMBB8 and LLBE8 were used to analyse the temporal and tissue-specific patterns of Adh gene expression. In the early stages of oogenesis, small amounts of Adh protein are detectable in the cystocytes. At the beginning of vitellogenesis, Adh protein is located mainly in the nurse cells. During late oogenesis, multiple Adh protein-positive bodies of varying size appear in the ooplasm. Adh protein is compartmentalized within the yolk or β-spheres.

In tissues such as fat body, gastric caeca, and adult cardiac valve the patterns of Adh RNA and protein expression are identical. Other tissues such as oocytes, nurse cells, imaginal discs, and brain have the same or lower levels of RNA but little or no Adh protein.

The amount of Adh protein was maximal for fat body, intermediate for intestinal duct, minimal for Malpighian tubules and carcass, and non-detectable in the brain.

Marker for
 
Subcellular Localization
CV Term
Evidence
References
Expression Deduced from Reporters
Reporter: P{AdhALEhs}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{AdhD-5000}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{Adh-GAL4.E2}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{AP-2} P{AP-5}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{GAL4-Adh.Dmul}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{hs-Adh.C}
Stage
Tissue/Position (including subcellular localization)
Reference
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\Adh in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Flygut - An atlas of the Drosophila adult midgut
Images
FlyExpress - Embryonic expression images (BDGP data)
  • Stages(s) 1-3
  • Stages(s) 4-6
  • Stages(s) 11-12
  • Stages(s) 13-16
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 196 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 282 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of Adh
Transgenic constructs containing regulatory region of Adh
Deletions and Duplications ( 226 )
Disrupted in
Not disrupted in
Phenotypes
Orthologs
Human Orthologs (via DIOPT v8.0)
Homo sapiens (Human) (1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
6 of 15
Yes
No
Model Organism Orthologs (via DIOPT v8.0)
Mus musculus (laboratory mouse) (1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
6 of 15
Yes
No
Rattus norvegicus (Norway rat) (1)
7 of 13
Yes
No
Xenopus tropicalis (Western clawed frog) (1)
4 of 12
Yes
No
Danio rerio (Zebrafish) (2)
7 of 15
Yes
No
6 of 15
No
No
Caenorhabditis elegans (Nematode, roundworm) (1)
1 of 15
Yes
No
Arabidopsis thaliana (thale-cress) (1)
1 of 9
Yes
Yes
Saccharomyces cerevisiae (Brewer's yeast) (2)
1 of 15
Yes
No
1 of 15
Yes
No
Schizosaccharomyces pombe (Fission yeast) (1)
1 of 12
Yes
No
Ortholog(s) in Drosophila Species (via OrthoDB v9.1) ( EOG09190EAD )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila pseudoobscura pseudoobscura
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila virilis
Drosophila mojavensis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( None identified )
No non-Drosophilid orthologies identified
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( None identified )
No non-Dipteran orthologies identified
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( None identified )
No non-Insect Arthropod orthologies identified
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( EOG091G0OC9 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strongylocentrotus purpuratus
Purple sea urchin
Gallus gallus
Domestic chicken
Paralogs
Paralogs (via DIOPT v8.0)
Drosophila melanogaster (Fruit fly) (5)
5 of 10
5 of 10
5 of 10
5 of 10
4 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
    Disease Model Summary Ribbon
    Disease Ontology (DO) Annotations
    Models Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Evidence
    References
    Potential Models Based on Orthology ( 1 )
    Modifiers Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Interaction
    References
    Disease Associations of Human Orthologs (via DIOPT v8.0 and OMIM)
    Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
    Functional Complementation Data
    Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
    Interactions
    Summary of Physical Interactions
    esyN Network Diagram
    Show neighbor-neighbor interactions:
    Select Layout:
    Legend:
    Protein
    RNA
    Selected Interactor(s)
    Interactions Browser

    Please see the Physical Interaction reports below for full details
    protein-protein
    Physical Interaction
    Assay
    References
    Summary of Genetic Interactions
    esyN Network Diagram
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    External Data
    Subunit Structure (UniProtKB)
    Homodimer.
    (UniProt, P00334 )
    Linkouts
    DroID - A comprehensive database of gene and protein interactions.
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Pathways
    Genomic Location and Detailed Mapping Data
    Chromosome (arm)
    2L
    Recombination map

    2-50

    Cytogenetic map
    Sequence location
    2L:14,615,552..14,618,902 [+]
    FlyBase Computed Cytological Location
    Cytogenetic map
    Evidence for location
    35B3-35B3
    Limits computationally determined from genome sequence between P{EP}elBEP2039&P{PZ}osprJ571 and P{lacW}Su(H)k07904
    Experimentally Determined Cytological Location
    Cytogenetic map
    Notes
    References
    35B-35B
    (determined by in situ hybridisation)
    35B3-35B3
    (determined by in situ hybridisation)
    35B3-35B5
    (determined by in situ hybridisation)
    Experimentally Determined Recombination Data
    Notes

    Maps 0.12cM to the left of Tp(2;2)Sco.

    Maps to the left of Tp(2;2)Sco. Extremely close to Tp(2;2)Sco.

    Stocks and Reagents
    Stocks (198)
    Genomic Clones (18)
     

    Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete

    cDNA Clones (269)
     

    Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.

    cDNA clones, fully sequenced
    BDGP DGC clones
    Other clones
      Drosophila Genomics Resource Center cDNA clones

      For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

      cDNA Clones, End Sequenced (ESTs)
      Other clones
      RNAi and Array Information
      Linkouts
      DRSC - Results frm RNAi screens
      GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
      Antibody Information
      Laboratory Generated Antibodies
       

      monoclonal

      Commercially Available Antibodies
       
      Other Information
      Relationship to Other Genes
      Source for database identify of

      Source for identity of: Adh CG3481

      Source for database merge of
      Additional comments

      Dicistronic annotation CG32954 split out into separate annotations for each open reading frame, CG3481 and CG3484, in release 4.2 of the genome annotation. CG3481 corresponds to Adh and CG3484 corresponds to Adhr.

      One or more of the processed transcripts for this gene contain(s) two non-overlapping open reading frames (ORFs). The non-overlapping ORFs are represented by Adh and Adhr.

      Other Comments

      Full-length Adh transgenes are silenced post-transcriptionally at high copy number or by a pulsed increase over a threshold. Production of 21-25 bp length sense and antisense RNAs homologous to Adh is correlated with this process.

      A non-transcribed segment in the Adh regulatory region was found to be one of the sequences required for homology recognition in the phenomenon of cosuppression.

      Aef1 protein binds with high affinity to the Inr region of the proximal Adh promoter, and inhibits transcription both in vivo and in vitro.

      Transgene coplacement studies indicate that the correlation in specific activity between D.melanogaster and D.affinidisjuncta Adh genes that occupy the same position is high in both larvae and adults.

      5' end RACE of the Adhr transcript from adults indicates that Adhr is transcribed as a dicistronic mRNA from the Adh distal promoter. RACE experiment with total RNA from embryos showed the embryonic Adhr transcript is also dicistronic and is transcribed from the proximal Adh promoter. Mutations that affect Adh transcripts also affect Adhr transcripts. Sedimentation profiles of polysomes and RNA analysis indicates the Adhr open reading frame of the dicistronic transcript is being translated and strongly suggests that Adhr translation is initiated by internal initiation in the intergenic region between Adh and Adhr coding regions. Adhr protein can be detected and is shown to co-localise with Adh. The level of Adh and Adhr transcripts in su(f) mutant and wild type background demonstrates the accumulation of the dicistronic messenger is controlled by a temperature-sensitive post-transcriptional mechanism.

      Molecular replacement and data from crystallographically refined 3D determination structures confirm the position of Ser 139. Results suggest Ser 139 is directly involved in the catalytic reaction.

      Adh activity is not primarily involved in oviposition site preference behaviour.

      NS1 region is located approximately 300bp upstream of the larval cap site and acts like an enhancer. Adh protein is not expressed when the sequence is deleted, expression is restored by placing a second Adh gene with an intact enhancer elsewhere on the same plasmid. The interactions between the enhancer and expression from a proximal and distal promoter are investigated.

      The excision reactions of P1\cre/P1\loxP and the related Scer\FLP1/Scer\FRT system are used to create lines in which transgenes, Adh and Daff\Adh, are at exactly allelic sites in homologous chromosomes.

      A 3D model of Adh using the tertiary structures has been generated, using molecular information about mutant alleles, to provide additional information about Adh catalysis and the stability of Adh dimers.

      mRNA levels do not increase at adult day 5 in strain showing extended longevity phenotype (ELP).

      Except for flies lacking Adh activity altogether there is a correlation between Adh activity and acute tolerance to acetic acid.

      The tandem Adh promoters are differentially transcribed in the embryo owing to critical differences in the core promoter elements. Reconstituted differential Adh promoter transcription in vitro provides evidence that selective Adh promoter utilization is mediated by a specific Tbp-TAF complex in combination with TfIIA. TAFs in the Tbp complex are required for discrimination between the Adh distal and proximal initiator elements.

      Adh enzyme activity has been measured in D.melanogaster lines in which spontaneous mutations have accumulated over approximately 300 generations.

      Adh catalyses a rapid aldehyde dismutation at physiological pH.

      Wild type larvae are most tolerant to ethanol, then methanol, n-propanol and n-butanol in descending order. For Adh-deficient larvae the toxicity of methanol was least, then ethanol, n-propanol and n-butanol in that order. Toxicity for this stage of the larval period is related to chain length of the alcohol, if the alcohol could not be degraded by the Adh system.

      Bending of DNA can inhibit transcription by affecting the binding of at least one of the general transcription factors. A tight bend present in a 245bp minicircular DNA reduces transcription from the Adh distal promoter. Repression occurs, at least in part, because the general factor TFIID is unable to bind to this bent DNA.

      Isolated as a rhythmically expressed transcript in fly heads. Transcript shows a single daily peak and a single daily trough in expression, highest expression is in the 'morning'. Adh expression oscillation is dependent on a light-dark cycle, on timed feeding and on the function of the per gene.

      The homologous genomic region containing Adh and Adhr is analysed. Ka and Ks values are determined (Ks values for Adh are significantly lower than values for Adhr) and amino acid comparisons reveal conserved regions shared by Adh and Adhr which have been assigned to known functional domains.

      A range of Adh substrates and inhibitors are used to study the effect of the Ser substitution in Adh mutants, how it affects their activity and kinetic parameters.

      Adh serves as a terminal fat cell differentiation marker.

      Somatic transformation of Daff\Adh in D.melanogaster flies identifies cis-acting elements that are highly conserved between the D.melanogaster and D.affinidisjuncta genes.

      Adh activity in 71 Drosophila species is assayed to determine if the protein plays a key role in the adaptation of species to substrates undergoing alcoholic fermentation.

      The in situ localization of Adh transcripts in different species reveals evolved regulatory differences in spatially restricted expression.

      In vivo crosslinking studies demonstrate that endogenous eve and ftz protein significantly interacts with the promoter region, although this is not an expected target gene.

      The srp gene encodes a transcription factor that binds a conserved sequence element of the larval promoter of the Adh gene. The srp-binding sites of the D.melanogaster and D.mulleri Adh larval promoters function as positive control elements.

      Ecdysteroid-regulated gene.

      Adh adult enhancer contains site that binds both activator ftz-f1 and repressor Hr39.

      The function of residues Tyr152 and Lys156 has been studied and the enzymatic properties of the mutants determined.

      Mutation of the Adh gene suggests that Tyr152 and Lys156 are involved in catalysis and Gly130, Gly133 and Gly184 contribute substantially to the structure of the active form.

      Adh protein either copurifies with a subtilisin type protease or may have protease activity per se.

      The effect of dietary ethanol on the ultrastructure of wild type and Adh mutant larvae was studied. The midgut and hindgut showed ethanol-induced subcellular damage, disrupting mitochondria and endoplasmic reticulum, reducing glycogen rosettes and protein granules, increasing autophagic vacuoles and causing unusual myelin whorls, with Adh mutant having greater sensitivity to ethanol.

      Accessible chromatin structures are found in the Adh proximal promoter, distal promoter and adult enhancer region just prior to and during Adh transcription in the fat body. A nucleosome positioning element between the distal promoter and the Adh adult enhancer can function via DNA-core histone interactions alone.

      Aldehyde dehydrogenase activities from Adh and Aldh gene products are selectively inhibited by cyanimide or acetone, respectively. Although larvae and adults use different aldehyde dehydrogenase activities to detoxify acetaldehyde (from Adh and Aldh encoded enzymes, respectively) both activities are cytosolic.

      Results are opposed to those of Lietaert, Experientia 38:651 and Lietaert, Experientia 41:57 , who concluded that the aldehyde dehydrogenase activity was mainly in the mitochondria.

      Adh can be rendered glucose-repressible by engineering the 5' region of Amy-p upstream of the Adh coding region.

      Phylogenetic relationships in Drosophila are studied using the Alcohol dehydrogenase locus in several species.

      CrebA protein binds to the fat body specific enhancers of Dmul\Adh1, Adh, Yp1 and Yp2 and may be an important component of tissue specific regulation.

      The tyrosine at the invariant amino acid position 152 is essential for the activity of the Adh enzyme.

      To the contrary of what occurs in larvae, the short-term modulation of the enzyme activities involved in the metabolism of alcohols does not appear to be a major mechanism used by adults to respond to the presence of ethanol, 2-propanol and their respective in vivo oxidised derivatives in the medium. Adults ability to move to non-toxic feeding sites seems to be successful enough to avoid the toxic effects of alcohols.

      A sequence specific DNA binding factor, Trl, has binding sites that flank the distal promoter elements of Adh involved in transcription initiation. Trl acts as a repressor of expression acting at transcription initiation and binding requires an intact 10bp motif.

      flies lacking Adh protein rapidly become intoxicated and eventually die on exposure to ethanol.

      Four alleles, AdhF, AdhS, Adhn4 and Adh71k were tested for oviposition site preference and first instar larval food preference in multiple choice tests between different media. Strains showed significantly different patterns.

      A negative regulatory element in the AAE binds the adult enhancer factor 1 (Aef1). The Aef1 binding site, Dmul\Adh1 AAE and Yp1 gene fat body enhancer are related to a sequence recognised by the mammalian transcription factor C/EBP and a liver specific regulatory element of the human Adh gene. DNase I footprinting experiments reveal that Aef1 and C/EBP compete for adjacent binding sites in the fat body enhancers, Aef1 can displace bound C/EBP from its sites.

      Aef1 protein binds specifically to fat body enhancers of Adh and Yp1.

      Adh null activity alleles extracted from a number of natural populations in Tasmania are molecularly similar.

      High resolution analysis of chromatin structure and helix distortion around regions required for distal transcription of Adh revealed apparent coordinate assembly of a large cooperative complex of proteins interacting with the distal promoter, the positioned nucleosome, the enhancer of the distal promoter and each other.

      A wild type 3.2 kb Adh gene fragment has been inserted into an Adh- strain in multiple chromosomal locations by P-element mediated transformation, identifying tissue specific position effects that possibly reflect differing chromatin organization.

      Limited regions of Adh are especially sensitive to proteolysis, results suggest the possibility of an association between the enzyme active site and the sensitive site(s).

      The reducing activity of the Adh enzyme, which transforms acetaldehyde into ethanol, plays an essential role in the detoxification of acetaldehyde.

      D.simulans enzyme monomers form heterodimers with those of D.melanogaster (E.H. Grell).

      Analysis of a number of different isogenic lines containing the natural polymorphism 'upside down triangle 2' suggests an association with the polymorphism and higher levels of Adh protein.

      Comparison of CpG distribution in the coding region of 121 genes from six species supports the mCpG mutational hotspot explanation of CpG suppression in methylated species at position II-III and III-I.

      A plasmid containing the proximal Adh promoter has been used in vitro transcription assays to study TfIIB activity.

      Adh, Aldh and Aldox-1 play a role in alcohol/aldehyde metabolism in D.melanogaster.

      Adh has been used as a marker for transgenesis in quail muscle cell lines.

      Adaptation to ethanol may not be strictly a function of the level of Adh pprotein activity.

      Two enhancer sequences, AAE and ALE, are required for the efficient expression of the distal and proximal promoters, respectively. The ALE segment can be sub- divided into three segments which act synergistically. ALE is ineffective in adults because transcription takes place from the distal promoter: transcriptional interference. The interactions of transcriptional interference at the molecular level are unknown. The ALE is involved in the down regulation of the ethanol induction response, the AAE is unresponsive to ethanol.

      Previous site directed in vitro mutagenesis experiments have demonstrated the average difference in Adh protein level between the fast and slow allozymic classes may or may not be due to linkage disequilibrium between the amino acid replacement site and the polymorphism present in the insert fragment, a silent substitution at nucleotide 1443.

      Larval expression is dependent on a 53bp sequence located upstream of the larval transcription start site.

      Transcribed larval mRNA was measured from the autosomal Adh gene and the X chromosomal Dpse\Hsp83 gene, both carried on the same P-element construct. The compensation behaviour of both of the transposed genes was determined by their new chromosomal environment.

      A 15 bp positive cis-acting element nearly 500 bp upstream of the distal Adh RNA start site and a 61 bp negative cis-acting element upstream and adjacent to the enhancer behave as promoter elements in the tissue culture system.

      Flies trisomic for a quarter of the length of 2L have diploid Adh enzyme activity and mRNA levels. By subdividing the trisomic chromosome a region exerting an inverse regulatory effect and a region exerting a direct gene dosage response on Adh was found. When present simultaneously the regions cancel each other out to yield diploid levels of Adh enzyme activity and mRNA.

      Transcription from the Adh proximal promoter is regulated by a far upstream enhancer and at least two elements near the transcription start site. The enhancer is tissue specific, and includes at least two discrete regions. Each of the identified regulatory elements is sufficient for low levels of Adh gene expression in larval tissues, but maximal expression requires the entire set.

      Chromatin at the Adh distal promoter displays an ordered but different conformation in different cell types. In Adh- cells sequences between -40 to +30 of the distal RNA initiation site exist as a DNA linker between nucleosomes. In Adh+ cells a longer linker DNA, -140 to +30, is bound in a multi-protein transcription initiation complex. These mutually exclusive patterns of DNA- protein interactions suggest a model for organizing alternative chromatin structure associated with gene regulation.

      Analysis of ENU-induced Adh mutations demonstrates that ENU produces primarily GC to AT transitions, also transversions and multilocus deficiencies.

      The regions between +604bp and +634bp, and between -600bp and -5000bp significantly affect the induction of Adh by ethanol.

      The expression difference between D.melanogaster and Dsim\Adh gene is due to trans-acting not cis-acting modifiers within the Adh gene.

      The tissue specific expression of the D.orena Adh gene in D.melanogaster is similar to D.melanogaster but at lower levels. The Adh genes share conserved DNAse protected sequences with respect to position and sequence. Upstream regions show a mosaic of similar and dissimilar sequences.

      Northern blot analysis and gel electrophoresis of transformant D.melanogaster larvae carrying the D.affinidisjuncta and D.grimshawi Adh gene show comparable high levels of expression and broader tissue distribution of Adh expression, transformants carrying the D.hawaiiensis Adh gene show reduced levels of each.

      Results suggest the switch from Adh proximal to Adh distal promoter is regulated by the stage-specific activation of the distal promoter and the subsequent repression of the proximal promoter by transcriptional interference.

      Three Adh antibodies were characterized and immunoblotting assays found that they cross-react to Adh genes from D.melanogaster, D.bocqueti, D.erecta, D.teissieri and D.lebanonensis. Adh specific activity in different larval organs was found to be similar whereas protein distribution varies substantially.

      Studies of the flux of ethanol into lipid suggested that more than 75% of the oxidation of acetaldehyde in wild type larvae is catalysed by the Adh product, the remaining ethanol is oxidized by the Aldh product.

      Gene conversion and unequal crossover have been studied in flies carrying a construct that contains tandem copies of Adh- genes. Southern blots of Adh+ variants suggests that five were generated by gene conversion as the size of the P-element insert is unchanged and one was generated by unequal exchange as the size of the Adh cluster has been changed.

      Maternally inherited Adh transcripts decay rapidly. Zygotic expression of Adh RNA begins after germ band retraction. Distal and proximal promoters drive expression in the fat body. At 15 hours proximal promoter expression is seen in the gut, at this time distal expression in the fat body has ceased. Proximal transcript levels decline at the end of larval development, accompanied by a transient accumulation of distal transcripts predominantly in the fat body.

      Analysis of three populations by restiction mapping in Adh provides evidence of Founder effects in the most Northern populations. There are signs of population differentiation among the samples, but the similarities between the populations indicates extensive migration. This suggests natural selection plays a role in maintaining the cline.

      Daff\Adh is expressed at comparable levels in D.melanogaster and D.affinidisjuncta, and tissue and stage specificity of expression is similar in the two species. In some details expression of Daff\Adh in D.melanogaster resembles that of Daff\Adh in D.affinidisjuncta.

      Daff\Adh and Dhaw\Adh display markedly different levels of alcohol dehydrogenase in the larval midgut and Malpighian tubules. Comparison of the expression of Daff\Adh and Dhaw\Adh in transgenes in D.melanogaster demonstrates that the tissue specific levels of alcohol dehydrogenase are characteristic of the genes themselves. Demonstrable differences in cis-dominant regulatory information are sufficient to account for the observed regulatory variation.

      Adh injected into early Adh- embryos is expressed in the somatic tissues of larvae and adults. The expression is tissue-specific and dependent on the 5' DNA sequences flanking the gene.

      Adh shows alternative promoter use during development.

      The Adh product also catalyses the oxidation of acetaldehyde to acetate. The Adh product is not a metalloenzyme but, paradoxically, is inhibited by certain metal ion chelators, e.g. pyrazole.

      AdhS gene product shows slower dissociation of NADH from NADN-enzyme complex than AdhF gene product.

      Not expressed in SL2 tissue culture cells, but transfected cloned gene is.

      Dsim\Adh and Adh enzymes differentially regulated in hybrids.

      The Adh product also catalyses the oxidation of acetaldehyde to acetate.

      Specific activity of the Adh product changes with development, with peaks at the end of the third larval instar and about four days after eclosion.

      AdhF and AdhS homozygotes show behavioural differences in their response to ethanol.

      The Adh product is not a metalloenzyme but, paradoxically, is inhibited by certain metal ion chelators, e.g. pyrazole.

      Adh may play a metabolic role independent of alcohol detoxification, i.e. in the metabolism of higher alcohols.

      Specific activity of the Adh product changes with development, with peaks at the end of the third larval instar and about four days after eclosion. Half life of AdhF product in vivo estimated as 55.3 hours.

      AdhF homozygotes usually show a better ability to survive on ethanol as a sole energy source than AdhS homozygotes.

      The relative thermostabilities of the Adh products are to be AdhS > AdhF > Adhn5 > AdhD.

      Adh protein is maternally inherited by embryos and resulting larvae.

      Flies carrying AdhF tend to be more resistant than those carrying only AdhS to ethanol.

      flies lacking Adh protein rapidly become intoxicated and eventually die on exposure to ethanol. However, ethanol sensitivity is complex since even Adh nulls are more resistant to ethanol when young than when old.

      Adh+ flies are killed by low concentrations of unsaturated secondary alcohols (e.g. 1-penten-3-ol; 1-pentyn-3-ol) but not by unsaturated primary alcohols (e.g. 1-penten-1-ol), presumably due to the formation of toxic ketones. This allows the chemical selection of Adh nulls.

      Utilization of ethanol as an energy source depends on Adh activity.

      Specific activity of the Adh product changes with development, with peaks at the end of the third larval instar and about four days after eclosion. Most of the activity is in the larval fat body and gut and the adult fat body.

      Origin and Etymology
      Discoverer
      Etymology
      Identification
      External Crossreferences and Linkouts ( 145 )
      Sequence Crossreferences
      NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
      RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
      UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
      Other crossreferences
      BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
      Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
      Flygut - An atlas of the Drosophila adult midgut
      GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
      KEGG Genes - Molecular building blocks of life in the genomic space.
      modMine - A data warehouse for the modENCODE project
      Linkouts
      DroID - A comprehensive database of gene and protein interactions.
      DRSC - Results frm RNAi screens
      FLIGHT - Cell culture data for RNAi and other high-throughput technologies
      FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
      FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
      FlyMine - An integrated database for Drosophila genomics
      InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
      MIST (protein-protein) - An integrated Molecular Interaction Database
      Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
      Synonyms and Secondary IDs (19)
      Reported As
      Symbol Synonym
      Adh
      (Jorgensen et al., 2020, Vásquez-Procopio et al., 2020, Kapun and Flatt, 2019, Kopp and Park, 2019, Wang and Althoff, 2019, Zhang and Zhang, 2019, Gene Disruption Project members, 2018-, Zanini et al., 2018, Cogni et al., 2017, Siddiq et al., 2017, Barton, 2016, Bayliak et al., 2016, Bhadra et al., 2016, Elgart et al., 2016, Flatt, 2016, Loehlin and Carroll, 2016, Nelson et al., 2016, Zheng et al., 2016, Adrion et al., 2015, Aradska et al., 2015, Grotewiel and Bettinger, 2015, Lichtenstein et al., 2015, Waldron et al., 2015, Xie et al., 2015, Ashwal-Fluss et al., 2014, Chen et al., 2014, Mukherjee et al., 2014, Sha et al., 2014, Birchler, 2013, Colinet et al., 2013, Main et al., 2013, Wang et al., 2013, Chen et al., 2012, Commar et al., 2012, Frizzell et al., 2012, King et al., 2012, Larson et al., 2012, Muerdter et al., 2012, Pushpavalli et al., 2012, White-Cooper, 2012, Yampolsky et al., 2012, Friedman et al., 2011, Gao et al., 2011, Guo et al., 2011, Levis et al., 2011.12.16, Lott et al., 2011, Malaspinas et al., 2011, O'Keefe et al., 2011, Zera, 2011, Zheng et al., 2011, Hense et al., 2010, Jung et al., 2010, Lang and Juan, 2010, Ogueta et al., 2010, Soin et al., 2010, van der Linde et al., 2010, Eanes et al., 2009, Hollis et al., 2009, Li et al., 2009, Micale et al., 2009, Prokupek et al., 2009, Reumer et al., 2009, Roote, 2009.11.24, Zhang and Townsend, 2009, Dorus, 2008.10.28, Fisher et al., 2008, Holloway et al., 2008, Juven-Gershon et al., 2008, McDermott and Kliman, 2008, Ramanathan et al., 2008, Adryan et al., 2007, Casillas et al., 2007, Grönke et al., 2007, Laayouni et al., 2007, Lang et al., 2007, Ludwig and Loreto, 2007, Morozova et al., 2007, Ozsoy, 2007, Pérez-Farrerons and Juan, 2007, Stark et al., 2007, Akashi et al., 2006, Beller et al., 2006, Beller et al., 2006, Dorus et al., 2006, Glavan et al., 2006, Jensen et al., 2006, Kadener et al., 2006, Metzstein and Krasnow, 2006, Montooth et al., 2006, Negre et al., 2006, Pal Bhadra et al., 2006, Umina et al., 2006, Vasemagi, 2006, Vaulin and Zakharov, 2006, Walser et al., 2006, Jagadeeshan and Singh, 2005, Malherbe et al., 2005, Rehwinkel et al., 2005, Schlenke and McKean, 2005, Schmidt et al., 2005, Taraszka et al., 2005, Carlini, 2004, Deckert-Cruz et al., 2004, Geiger-Thornsberry and Mackay, 2004, Passananti et al., 2004, Ranz et al., 2004, Veuille et al., 2004, Wang et al., 2004, Chen and Stephan, 2003, Ko et al., 2003, Noor and Kliman, 2003, Powell et al., 2003, Albalat et al., 2001, Christophides et al., 2001, Gim et al., 2001, Bokor and Pecsenye, 2000, Gonzalez et al., 2000, Katoh et al., 2000, Singh and Heberlein, 2000, Wei and Brennan, 2000, Colon-Parrilla and Perez-Chiesa, 1999, Kovac and Marinkovic, 1999, Wu et al., 1998, Leal and Barbancho, 1992, Heinstra et al., 1983, Winberg et al., 1982)
      Reg-1
      Secondary FlyBase IDs
      • FBgn0016704
      • FBgn0052954
      Datasets (0)
      Study focus (0)
      Experimental Role
      Project
      Project Type
      Title
      References (1,168)