A Database of Drosophila Genes & Genomes

FB2012_01, released January 20th, 2012
 

Gene Dmel\Adh

General Information
SymbolDmel\AdhSpeciesD. melanogaster
NameAlcohol dehydrogenaseAnnotation symbolCG3481
Feature typeprotein_coding_geneFlyBase IDFBgn0000055
Gene Model StatusCurrent Stock availability 263 publicly available
Also Known AsCG32954, BG:DS01486.8
Genomic Location
Chromosome (arm)2LRecombination map2-50.1
Cytogenetic map35B3-35B3Sequence location2L:14,615,555..14,618,902 [+]

Genomic Maps

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Automatically generated summary

See sections below for more information
The gene Alcohol dehydrogenase is referred to in FlyBase by the symbol Dmel\Adh (CG3481, FBgn0000055). It is a protein_coding_gene from Drosophila melanogaster. There is experimental evidence that it has the molecular function: protein homodimerization activity; alcohol dehydrogenase (NAD) activity; acetaldehyde dehydrogenase (acetylating) activity. There is experimental evidence that it is involved in the biological process: alcohol catabolic process; alcohol metabolic process; ethanol oxidation; behavioral response to ethanol; acetaldehyde metabolic process; ethanol metabolic process. 587 alleles are reported. No phenotypic data is available. It has 5 annotated transcripts and 5 annotated polypeptides. Protein features are: Alcohol dehydrogenase, Drosophila-type; Alcohol dehydrogenase, insect-type; NAD(P)-binding domain; Short-chain dehydrogenase/reductase SDR; Short-chain dehydrogenase/reductase, conserved site. Summary of modENCODE Temporal Expression Profile: Temporal profile ranges from a peak of extremely high expression to a trough of low expression. Peak expression observed at stages throughout the larval period, in adult male stages. This gene is annotated by FlyBase as a dicistronic gene, meaning that some or all of its transcripts encode two or more polypeptide-coding open reading frames (ORFs) , with each ORF assigned to a different gene. The distribution of RNA-Seq coverage data amongst the different encoded genes cannot be determined. Summary of FlyAtlas Anatomical Expression Data: Two or more Affy2 ProbeSets identify exons of this gene. This is a summary of the tissue expression peaks exhibited in at least one of these ProbeSets. Expression at high levels in the following post-embryonic organs or tissues: adult head, adult eye, adult central nervous system, adult crop, larval/adult midgut, larval/adult hindgut, larval/adult Malpighian tubules, adult heart, larval/adult fat body, adult salivary gland, larval trachea, adult female reproductive system, adult male accessory gland, larval/adult carcass. Expression at moderate levels in the following post-embryonic organs or tissues: larval salivary gland, adult testis. Gene sequence location is 2L:14615555..14618902.

hide Phenotypic Description from the Red Book (Lindsley & Zimm 1992)
Gene/Allele symbols may differ from current usage
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).
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FB2011_10
References
FB2012_01
References
All updates Click here to see a list of all updates to this record from FB2010_08 and on.
hide Detailed Mapping Data
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)  
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
Location
Left of (cM)
Right of (cM)
Notes
Maps to the left of Tp(2;2)Sco. Extremely close to Tp(2;2)Sco.
Maps 0.12cM to the left of Tp(2;2)Sco.
hide Gene Model & Products
Please see the GBrowse view of Dmel\Adh for information on other features
To submit a correction to a gene model please use the Contact FlyBase form
detailed view FBtr0308753 FBtr0006151 FBtr0100589 FBtr0100594 FBtr0100591 FBtr0100590 FBtr0100593 FBtr0100187 FBtr0114465 FBtr0301495 FBtr0301496 FBtr0301494 FBpp0100047 FBpp0100048 FBpp0100050 FBpp0100045 FBpp0100051 FBpp0099544 FBpp0099545 FBpp0290710 FBpp0290709 FBpp0290711 FBpp0112957 FBti0015071 FBti0051096 FBti0014084 FBti0057324 FBti0110062 FBti0025816 FBti0018409 FBti0023167 FBti0056239
Comments on Gene Model
gene_with_dicistronic_mRNA ; SO:0000722
hide Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Associated CDS (aa)
FBtr0100589
  1071
  256
FBtr0100590
  1016
  256
FBtr0100591
  2077
  256
FBtr0100593
  2022
  256
FBtr0100594
  1245
  256
Additional Transcript Data & Comments
Reported size (kB)
1.150 (northern blot)
1.120 (northern blot)
1.5 (northern blot)
1.0 (northern blot)
0.760 (sequence analysis)
Comments
External Data
Crossreferences
hide Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank protein
Adh-PC  
FBpp0100045  
27.7  
256  
7.57  
Adh-PE  
FBpp0100047  
27.7  
256  
7.57  
Adh-PF  
FBpp0100048  
27.7  
256  
7.57  
Adh-PH  
FBpp0100050  
27.7  
256  
7.57  
Adh-PI  
FBpp0100051  
27.7  
256  
7.57  
Additional Polypeptide Data & 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
Linkouts
Crossreferences
InterPro domains - A database of protein families, domains, and functional sites
hide Sequences Consistent with the Gene Model
DDBJ /
EMBL /
GenBank
DNA sequence
Protein sequence
Name
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
UniProtKB/Swiss-Prot
UniProtKB/TrEMBL
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Mapped Features have been reorganized, please see this article for details.
Additional mapped features and mutations can be found on GBrowse or related reports.
Type
Symbol & Location
Additional Notes
References
protein binding site
bound_moiety=Trl-XP
evidence=experimental
protein binding site
protein binding site
protein binding site
bound_moiety=Trl-XP
evidence=experimental
protein binding site
protein binding site
protein binding site
protein binding site
protein binding site
protein binding site
bound_moiety=Adf1-XP
evidence=experimental
protein binding site
protein binding site
protein binding site
protein binding site
protein binding site
bound_moiety=Adf1-XP
evidence=experimental
protein binding site
bound_moiety=srp-XP
evidence=experimental
protein binding site
protein binding site
protein binding site
protein binding site
protein binding site
bound_moiety=Aef1-XP
evidence=experimental
protein binding site
protein binding site
bound_moiety=Aef1-XP
evidence=experimental
protein binding site
protein binding site
hide External Data
Linkouts
Crossreferences
EPD - Eukarytoic Promoter Database, an annotated collection of POL II promoters
hide Expression Data
hideTranscript Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
Comment:all cells of cell layer
northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
Marker for
Subcellular Localization
CV Term
Notes
hidePolypeptide 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
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.
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.
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.
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.
Marker for
Subcellular Localization
CV Term
Notes
hide High-Throughput Expression Data
or
Untitled Document detailed view Adhr-RA Adh-RC Adh-RI Adh-RF Adh-RE Adh-RH Adhr-RB osp-RC osp-RE osp-RF osp-RD
See Gelbart and Emmert, 2010.10.13 for analysis details and data files for all genes.

modENCODE Temporal Expression Data for FBgn0000055


   Styles
Linear
Logarithmic
Heatmap
   Scales
max expr for FBgn0000055
Very low expression bin max
Moderate expression bin max
High expression bin max
Extremely high expression bin max

Summary of modENCODE Temporal Expression Profile: Temporal profile ranges from a peak of extremely high expression to a trough of low expression. Peak expression observed at stages throughout the larval period, in adult male stages. This gene is annotated by FlyBase as a dicistronic gene, meaning that some or all of its transcripts encode two or more polypeptide-coding open reading frames (ORFs) , with each ORF assigned to a different gene. The distribution of RNA-Seq coverage data amongst the different encoded genes cannot be determined.
[download data (TSV)]

Guide to modENCODE expression level colors
 
No expression (0 - 0)
 
Extremely low expression (1 - 10)
 
Very low expression (11 - 100)
 
Low expression (101 - 400)
 
Moderate expression (401 - 1400)
 
Moderately high expression (1401 - 4000)
 
High expression (4001 - 10000)
 
Very high expression (10001 - 100000)
 
Extremely high expression (100001 - 2000000)

Linear, scaled to maximum FBgn0000055 expression level
Developmental Stage   Expression Level
embryo 00-02hr
 
 8270
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 
 4499
embryo 16-18hr
 
 7464
embryo 18-20hr
 
 18128
embryo 20-22hr
 
 36780
embryo 22-24hr
 
 59599
larva L1
 
 77050
larva L2
 
 118789
larva L3 12hr old
 
 180270
larva L3 puffstage 1-2
 
 106979
larva L3 puffstage 3-6
 
 49757
larva L3 puffstage 7-9
 
 9000
white prepupae new
 
 3936
white prepupae 12hr
 
 5619
white prepupae 24hr
 
 3604
pupae 2d postWPP
 
 3710
pupae 3d postWPP
 
 4854
pupae 4d postWPP
 
 48907
adult male 01day
 
 172892
adult male 05day
 
 174623
adult male 30day
 
 104458
adult female 01day
 
 97642
adult female 05day
 
 64019
adult female 30day
 
 65715
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
 Extremely high 
Linear, scaled to Very low expression
Developmental Stage   Expression Level
embryo 00-02hr
 (8270)
embryo 02-04hr
 (306)
embryo 04-06hr
 (168)
embryo 06-08hr
 (187)
embryo 08-10hr
 (275)
embryo 10-12hr
 (431)
embryo 12-14hr
 (857)
embryo 14-16hr
 (4499)
embryo 16-18hr
 (7464)
embryo 18-20hr
 (18128)
embryo 20-22hr
 (36780)
embryo 22-24hr
 (59599)
larva L1
 (77050)
larva L2
 (118789)
larva L3 12hr old
 (180270)
larva L3 puffstage 1-2
 (106979)
larva L3 puffstage 3-6
 (49757)
larva L3 puffstage 7-9
 (9000)
white prepupae new
 (3936)
white prepupae 12hr
 (5619)
white prepupae 24hr
 (3604)
pupae 2d postWPP
 (3710)
pupae 3d postWPP
 (4854)
pupae 4d postWPP
 (48907)
adult male 01day
 (172892)
adult male 05day
 (174623)
adult male 30day
 (104458)
adult female 01day
 (97642)
adult female 05day
 (64019)
adult female 30day
 (65715)
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
Linear, scaled to Moderate expression
Developmental Stage   Expression Level
embryo 00-02hr
 (8270)
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 (4499)
embryo 16-18hr
 (7464)
embryo 18-20hr
 (18128)
embryo 20-22hr
 (36780)
embryo 22-24hr
 (59599)
larva L1
 (77050)
larva L2
 (118789)
larva L3 12hr old
 (180270)
larva L3 puffstage 1-2
 (106979)
larva L3 puffstage 3-6
 (49757)
larva L3 puffstage 7-9
 (9000)
white prepupae new
 (3936)
white prepupae 12hr
 (5619)
white prepupae 24hr
 (3604)
pupae 2d postWPP
 (3710)
pupae 3d postWPP
 (4854)
pupae 4d postWPP
 (48907)
adult male 01day
 (172892)
adult male 05day
 (174623)
adult male 30day
 (104458)
adult female 01day
 (97642)
adult female 05day
 (64019)
adult female 30day
 (65715)
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
Linear, scaled to High expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 8270
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 
 4499
embryo 16-18hr
 
 7464
embryo 18-20hr
 (18128)
embryo 20-22hr
 (36780)
embryo 22-24hr
 (59599)
larva L1
 (77050)
larva L2
 (118789)
larva L3 12hr old
 (180270)
larva L3 puffstage 1-2
 (106979)
larva L3 puffstage 3-6
 (49757)
larva L3 puffstage 7-9
 
 9000
white prepupae new
 
 3936
white prepupae 12hr
 
 5619
white prepupae 24hr
 
 3604
pupae 2d postWPP
 
 3710
pupae 3d postWPP
 
 4854
pupae 4d postWPP
 (48907)
adult male 01day
 (172892)
adult male 05day
 (174623)
adult male 30day
 (104458)
adult female 01day
 (97642)
adult female 05day
 (64019)
adult female 30day
 (65715)
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
Linear, scaled to Extremely high expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 8270
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 
 4499
embryo 16-18hr
 
 7464
embryo 18-20hr
 
 18128
embryo 20-22hr
 
 36780
embryo 22-24hr
 
 59599
larva L1
 
 77050
larva L2
 
 118789
larva L3 12hr old
 
 180270
larva L3 puffstage 1-2
 
 106979
larva L3 puffstage 3-6
 
 49757
larva L3 puffstage 7-9
 
 9000
white prepupae new
 
 3936
white prepupae 12hr
 
 5619
white prepupae 24hr
 
 3604
pupae 2d postWPP
 
 3710
pupae 3d postWPP
 
 4854
pupae 4d postWPP
 
 48907
adult male 01day
 
 172892
adult male 05day
 
 174623
adult male 30day
 
 104458
adult female 01day
 
 97642
adult female 05day
 
 64019
adult female 30day
 
 65715
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
 Extremely high 
log, scaled to maximum FBgn0000055 expression level
Developmental Stage   Expression Level
embryo 00-02hr
 
 8270
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 
 4499
embryo 16-18hr
 
 7464
embryo 18-20hr
 
 18128
embryo 20-22hr
 
 36780
embryo 22-24hr
 
 59599
larva L1
 
 77050
larva L2
 
 118789
larva L3 12hr old
 
 180270
larva L3 puffstage 1-2
 
 106979
larva L3 puffstage 3-6
 
 49757
larva L3 puffstage 7-9
 
 9000
white prepupae new
 
 3936
white prepupae 12hr
 
 5619
white prepupae 24hr
 
 3604
pupae 2d postWPP
 
 3710
pupae 3d postWPP
 
 4854
pupae 4d postWPP
 
 48907
adult male 01day
 
 172892
adult male 05day
 
 174623
adult male 30day
 
 104458
adult female 01day
 
 97642
adult female 05day
 
 64019
adult female 30day
 
 65715
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
 Extremely high 
log, scaled to Very low expression
Developmental Stage   Expression Level
embryo 00-02hr
 (8270)
embryo 02-04hr
 (306)
embryo 04-06hr
 (168)
embryo 06-08hr
 (187)
embryo 08-10hr
 (275)
embryo 10-12hr
 (431)
embryo 12-14hr
 (857)
embryo 14-16hr
 (4499)
embryo 16-18hr
 (7464)
embryo 18-20hr
 (18128)
embryo 20-22hr
 (36780)
embryo 22-24hr
 (59599)
larva L1
 (77050)
larva L2
 (118789)
larva L3 12hr old
 (180270)
larva L3 puffstage 1-2
 (106979)
larva L3 puffstage 3-6
 (49757)
larva L3 puffstage 7-9
 (9000)
white prepupae new
 (3936)
white prepupae 12hr
 (5619)
white prepupae 24hr
 (3604)
pupae 2d postWPP
 (3710)
pupae 3d postWPP
 (4854)
pupae 4d postWPP
 (48907)
adult male 01day
 (172892)
adult male 05day
 (174623)
adult male 30day
 (104458)
adult female 01day
 (97642)
adult female 05day
 (64019)
adult female 30day
 (65715)
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
log, scaled to Moderate expression
Developmental Stage   Expression Level
embryo 00-02hr
 (8270)
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 (4499)
embryo 16-18hr
 (7464)
embryo 18-20hr
 (18128)
embryo 20-22hr
 (36780)
embryo 22-24hr
 (59599)
larva L1
 (77050)
larva L2
 (118789)
larva L3 12hr old
 (180270)
larva L3 puffstage 1-2
 (106979)
larva L3 puffstage 3-6
 (49757)
larva L3 puffstage 7-9
 (9000)
white prepupae new
 (3936)
white prepupae 12hr
 (5619)
white prepupae 24hr
 (3604)
pupae 2d postWPP
 (3710)
pupae 3d postWPP
 (4854)
pupae 4d postWPP
 (48907)
adult male 01day
 (172892)
adult male 05day
 (174623)
adult male 30day
 (104458)
adult female 01day
 (97642)
adult female 05day
 (64019)
adult female 30day
 (65715)
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
log, scaled to High expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 8270
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 
 4499
embryo 16-18hr
 
 7464
embryo 18-20hr
 18128
embryo 20-22hr
 (36780)
embryo 22-24hr
 (59599)
larva L1
 (77050)
larva L2
 (118789)
larva L3 12hr old
 (180270)
larva L3 puffstage 1-2
 (106979)
larva L3 puffstage 3-6
 (49757)
larva L3 puffstage 7-9
 
 9000
white prepupae new
 
 3936
white prepupae 12hr
 
 5619
white prepupae 24hr
 
 3604
pupae 2d postWPP
 
 3710
pupae 3d postWPP
 
 4854
pupae 4d postWPP
 (48907)
adult male 01day
 (172892)
adult male 05day
 (174623)
adult male 30day
 (104458)
adult female 01day
 (97642)
adult female 05day
 (64019)
adult female 30day
 (65715)
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
log, scaled to Extremely high expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 8270
embryo 02-04hr
 
 306
embryo 04-06hr
 
 168
embryo 06-08hr
 
 187
embryo 08-10hr
 
 275
embryo 10-12hr
 
 431
embryo 12-14hr
 
 857
embryo 14-16hr
 
 4499
embryo 16-18hr
 
 7464
embryo 18-20hr
 
 18128
embryo 20-22hr
 
 36780
embryo 22-24hr
 
 59599
larva L1
 
 77050
larva L2
 
 118789
larva L3 12hr old
 
 180270
larva L3 puffstage 1-2
 
 106979
larva L3 puffstage 3-6
 
 49757
larva L3 puffstage 7-9
 
 9000
white prepupae new
 
 3936
white prepupae 12hr
 
 5619
white prepupae 24hr
 
 3604
pupae 2d postWPP
 
 3710
pupae 3d postWPP
 
 4854
pupae 4d postWPP
 
 48907
adult male 01day
 
 172892
adult male 05day
 
 174623
adult male 30day
 
 104458
adult female 01day
 
 97642
adult female 05day
 
 64019
adult female 30day
 
 65715
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
 Extremely high 
Heatmap
Developmental Stage   Expression Level
embryo 00-02hr
 
 
embryo 02-04hr
 
 
embryo 04-06hr
 
 
embryo 06-08hr
 
 
embryo 08-10hr
 
 
embryo 10-12hr
 
 
embryo 12-14hr
 
 
embryo 14-16hr
 
 
embryo 16-18hr
 
 
embryo 18-20hr
 
 
embryo 20-22hr
 
 
embryo 22-24hr
 
 
larva L1
 
 
larva L2
 
 
larva L3 12hr old
 
 
larva L3 puffstage 1-2
 
 
larva L3 puffstage 3-6
 
 
larva L3 puffstage 7-9
 
 
white prepupae new
 
 
white prepupae 12hr
 
 
white prepupae 24hr
 
 
pupae 2d postWPP
 
 
pupae 3d postWPP
 
 
pupae 4d postWPP
 
 
adult male 01day
 
 
adult male 05day
 
 
adult male 30day
 
 
adult female 01day
 
 
adult female 05day
 
 
adult female 30day
 
 

FlyAtlas Anatomical Expression Data for FBgn0000055


   Styles
Linear
Logarithmic
Heatmap
Back-to-back
   Scales
max expr for FBgn0000055
Moderate expression bin max
High level expression bin max
Very high expression bin max

Summary of FlyAtlas Anatomical Expression Data: Two or more Affy2 ProbeSets identify exons of this gene. This is a summary of the tissue expression peaks exhibited in at least one of these ProbeSets. Expression at high levels in the following post-embryonic organs or tissues: adult head, adult eye, adult central nervous system, adult crop, larval/adult midgut, larval/adult hindgut, larval/adult Malpighian tubules, adult heart, larval/adult fat body, adult salivary gland, larval trachea, adult female reproductive system, adult male accessory gland, larval/adult carcass. Expression at moderate levels in the following post-embryonic organs or tissues: larval salivary gland, adult testis.
[download data (TSV)]

Guide to FlyAtlas expression level colors
 
No expression (0 - 9.999)
 
Low expression (10 - 99.999)
 
Moderate expression (100 - 499.999)
 
High level expression (500 - 999.999)
 
Very high expression (1000 - 25000)

Heatmap
Tissue   Expression Level
Larval Central Nervous System no informative data
Larval Midgut no informative data
Larval Hindgut no informative data
Larval Malpighian Tubules no informative data
Larval Fat Body no informative data
Larval Salivary Gland no informative data
Larval Trachea no informative data
Larval Carcass no informative data
Adult Head no informative data
Adult Eye no informative data
Adult Brain no informative data
Adult Thoracic-Abdominal Ganglion no informative data
Adult Crop no informative data
Adult Midgut no informative data
Adult Hindgut no informative data
Adult Malpighian Tubules no informative data
Adult Fat Body no informative data
Adult Salivary Gland no informative data
Adult Heart no informative data
Adult VirginFemale Spermatheca no informative data
Adult InseminatedFemale Spermatheca no informative data
Adult Ovary no informative data
Adult Testis no informative data
Adult Male Accessory Gland no informative data
Adult Carcass no informative data

modENCODE Temporal Expression Data (Graveley et al., 2011)
FlyAtlas Anatomical Expression Data (Chintapalli et al., 2007)
hide Expression Clusters
A cluster of genes with similar mRNA expression dynamics across development.
hide External Data & Images
Linkouts
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
FlyExpress - Embryonic expression images (BDGP data)
hide Alleles & Phenotypes
hide Summary of Allele Phenotypes
Other Phenotypes
Allele
Phenotype manifest in
Allele
hide Classical Alleles ( 191 )
For All Classical Alleles Show

Allele of AdhClassMutagenStocksKnown lesion
AdhnBloss of function allele55 Yes
Adhfn23loss of function allele, amorphic allele - genetic evidence31 Yes
AdhUF26 Yes
Adhn4amorphic allele - genetic evidence, loss of function allele18 Yes
Adhn2loss of function allele, amorphic allele - genetic evidence14 Yes
AdhD10 Yes
Adhn7loss of function allele, amorphic allele - genetic evidence8 Yes
AdhF8 Yes
Adhn11amorphic allele - genetic evidence, hypomorphic allele - genetic evidence6 Yes
Adhn1loss of function allele, amorphic allele - genetic evidence6 Yes
AdhnC16 --
AdhS6 Yes
Adhn5amorphic allele - genetic evidence, hypomorphic allele - genetic evidence5 --
Adhfn6loss of function allele, amorphic allele - genetic evidence4 Yes
Adhn10amorphic allele - genetic evidence, loss of function allele2 Yes
AdhBG010491 Yes
AdhF'1 Yes
AdhKG053451 Yes
AdhUS1 Yes
AdhAC14amorphic allele - genetic evidence
0 --
AdhAC22amorphic allele - genetic evidence
0 --
AdhAC53amorphic allele - genetic evidence
0 --
AdhAC80amorphic allele - genetic evidence
0 --
AdhAC95amorphic allele - genetic evidence
0 --
AdhAH108amorphic allele - genetic evidence
0 --
AdhAH26amorphic allele - genetic evidence
0 --
AdhAH36amorphic allele - genetic evidence
0 --
AdhAH41amorphic allele - genetic evidence
0 --
AdhAH52amorphic allele - genetic evidence
0 --
AdhAH70amorphic allele - genetic evidence
0 --
AdhAH77amorphic allele - genetic evidence
0 --
AdhAH98amorphic allele - genetic evidence
0 --
AdhAH9amorphic allele - genetic evidence
0 --
AdhAP81amorphic allele - genetic evidence
0 --
AdhAT240amorphic allele - genetic evidence
0 --
AdhAT265amorphic allele - genetic evidence
0 --
AdhAT33amorphic allele - genetic evidence
0 --
AdhAT340amorphic allele - genetic evidence
0 --
Adhfn4loss of function allele, amorphic allele - genetic evidence0 Yes
Adhn12loss of function allele, amorphic allele - genetic evidence0 --
Adhn13amorphic allele - genetic evidence, loss of function allele0 --
Adhn14amorphic allele - genetic evidence, loss of function allele0 Yes
Adhn3loss of function allele, amorphic allele - genetic evidence0 --
Adhn6amorphic allele - genetic evidence, loss of function allele0 --
Adhn8loss of function allele, amorphic allele - genetic evidence0 --
Adhn9loss of function allele, amorphic allele - genetic evidence0 --
AdhnAC14amorphic allele - genetic evidence
0 Yes
AdhnAC22amorphic allele - genetic evidence
0 Yes
AdhnAC95amorphic allele - genetic evidence
0 Yes
AdhnACH105amorphic allele - genetic evidence
0 Yes
AdhnACH449amorphic allele - genetic evidence
0 Yes
AdhnAH144amorphic allele - genetic evidence
0 Yes
AdhnAH52loss of function allele, amorphic allele - genetic evidence0 Yes
AdhnAH9amorphic allele - genetic evidence
0 Yes
AdhnAP81amorphic allele - genetic evidence
0 Yes
AdhnAT33amorphic allele - genetic evidence
0 Yes
AdhnAT340amorphic allele - genetic evidence
0 Yes
AdhnBR108loss of function allele, amorphic allele - genetic evidence0 Yes
AdhnBR112amorphic allele - genetic evidence0 Yes
AdhnBR114amorphic allele - genetic evidence0 Yes
AdhnBR28amorphic allele - genetic evidence, loss of function allele0 Yes
AdhnBR43loss of function allele, amorphic allele - genetic evidence0 Yes
AdhnBR50amorphic allele - genetic evidence, loss of function allele0 Yes
AdhnBR51amorphic allele - genetic evidence0 Yes
AdhnBR52loss of function allele, amorphic allele - genetic evidence0 Yes
AdhnBR53amorphic allele - genetic evidence0 Yes
AdhnBR54amorphic allele - genetic evidence, loss of function allele0 Yes
AdhnBR56loss of function allele, amorphic allele - genetic evidence0 Yes
AdhnLA248loss of function allele, amorphic allele - genetic evidence0 Yes
AdhΔ25amorphic allele - molecular evidence0 Yes
Adh+D.2wild-type allele0 Yes
Adh+I.28wild-type allele0 Yes
Adh+I.35wild-type allele0 Yes
Adh+I.48wild-type allele0 Yes
Adh+I.4wild-type allele0 Yes
Adh+I.7wild-type allele0 Yes
Adh+I1.0wild-type allele0 Yes
Adh+I1.5wild-type allele0 Yes
Adh+I3.0wild-type allele0 Yes
Adh+I4.5wild-type allele0 Yes
Adh+I5.0wild-type allele0 Yes
Adh1Metloss of function allele0 Yes
Adh3intloss of function allele0 Yes
Adh71k0 Yes
AdhA146Vloss of function allele0 Yes
AdhA14Vloss of function allele0 Yes
AdhA158Vloss of function allele0 Yes
AdhA159Vloss of function allele0 Yes
AdhA10 Yes
AdhAAS440 Yes
AdhAC50 --
AdhAf-F0 Yes
AdhAf-S0 Yes
AdhAR720 Yes
AdhB70 Yes
AdhBG270 Yes
AdhCA-F10 --
AdhCA-S10 --
AdhChD120 Yes
AdhCr140 Yes
AdhCS470 Yes
AdhD.20 Yes
AdhDup0 Yes
AdhF(o)0 --
AdhF-ChD0 Yes
AdhFl-2S0 Yes
AdhFl-F0 Yes
AdhFl1-S0 Yes
AdhFm0 --
Adhfn24loss of function allele0 Yes
Adhfn45loss of function allele0 Yes
Adhfn46loss of function allele0 Yes
AdhFr-F0 Yes
AdhFr-S0 Yes
AdhFr0 --
AdhFs0 --
AdhG112Dloss of function allele0 Yes
AdhG139Eloss of function allele0 Yes
AdhG155Dloss of function allele0 Yes
AdhG150 --
AdhG17Eloss of function allele0 Yes
AdhG17Rloss of function allele0 Yes
AdhG184Closs of function allele0 Yes
AdhG184Dloss of function allele0 Yes
AdhG93Eloss of function allele0 Yes
AdhG93Rloss of function allele0 Yes
AdhGC-10 --
AdhH-R0 --
Adhh120 Yes
Adhh130 Yes
AdhH150 Yes
AdhH200 Yes
Adhh210 Yes
Adhh30 Yes
AdhI1.50 Yes
AdhI5.00 Yes
AdhJa-F0 Yes
AdhJa-S0 Yes
Adhjockey0 Yes
Adhk150 Yes
Adhk300 Yes
AdhKA120 Yes
AdhKA130 --
AdhKA160 --
AdhKA270 Yes
AdhMM-500 --
Adhn9670 --
AdhnAloss of function allele0 --
AdhnAChT
0 Yes
AdhnAus0 --
AdhnBR-167
0 Yes
AdhnBR18
0 Yes
AdhnBR4
0 Yes
AdhNC160 Yes
AdhnC2hypomorphic allele - genetic evidence0 --
AdhnCA14loss of function allele0 Yes
AdhnCh
0 --
Adhnf3
0 --
AdhnLA249loss of function allele0 Yes
AdhnLA252loss of function allele0 Yes
AdhnLA2loss of function allele0 Yes
AdhnLA319loss of function allele0 Yes
AdhnLA378loss of function allele0 --
AdhnLA3790 --
AdhnLA405loss of function allele0 --
AdhnLA73loss of function allele0 Yes
AdhnLA74loss of function allele0 Yes
AdhnLA80loss of function allele0 Yes
AdhnNC1loss of function allele0 --
AdhP183Lloss of function allele0 Yes
AdhQ101stoploss of function allele0 Yes
AdhRI-420 Yes
AdhRI320 Yes
AdhRI370 --
AdhS140Floss of function allele0 Yes
AdhS154Floss of function allele0 Yes
AdhS166Floss of function allele0 Yes
AdhSf10 Yes
AdhSi440 --
AdhSL
0 Yes
AdhSm0 --
AdhSs0 --
AdhT186Iloss of function allele0 Yes
AdhW124stoploss of function allele0 Yes
AdhW236stoploss of function allele0 Yes
AdhW0 Yes
AdhWa-F0 Yes
AdhWa-S0 Yes
AdhWI080 --
AdhWI090 --
AdhΔ170 Yes
hide Alleles Carried on Transgenic Constructs ( 396 )
For All Alleles Carried on Transgenic Constructs Show

Allele of AdhClassMutagenStocksKnown lesion
Adh+t3.264 Yes
AdhJF030421 Yes
Adh+t*0 --
Adh+t11.80 Yes
Adh+t3.2.Δ-492:-4810 Yes
Adh+t4.60 Yes
Adh+t4.80 Yes
Adh+tOa0 --
Adh+tS0 Yes
Adh-662.Adh0 Yes
Adh11Δ0 Yes
Adh3.20 Yes
Adh3.2dsw0 Yes
Adh386.NP60 Yes
Adh5'3'AAE0 Yes
Adh5'P3'DP0 Yes
AdhAct5C.T:SV40\nls20 Yes
AdhAF00 Yes
AdhALE:P-1100 Yes
AdhALE:P-1870 Yes
AdhALE:P-2420 Yes
AdhALE:P-3860 Yes
AdhALE:P-800 Yes
AdhALEhs0 Yes
AdhAmy-p.4300 Yes
AdhARP-90 Yes
AdhCA-194.70 Yes
AdhCA-194.880 Yes
AdhCA-194.80 Yes
AdhCOA-194.80 Yes
AdhcRa0 Yes
AdhD+53:+3280 Yes
AdhD-127:-630 Yes
AdhD-21900 Yes
AdhD-28300 Yes
AdhD-33500 Yes
AdhD-35500 Yes
AdhD-50000 Yes
AdhD-660:-1280 Yes
AdhD-660:-600 Yes
AdhD-6600 Yes
AdhD-66:+530 Yes
AdhD13200 Yes
AdhD690 Yes
AdhD69P3860 Yes
Adhd0 Yes
AdhDdc.S.+40 Yes
AdhDdc.S.+0 Yes
AdhDebA.DA4170 Yes
AdhDebA.DA4420 Yes
AdhDebA.DAJ0 Yes
AdhDebA.DAP0 Yes
AdhDebA.DAR0 Yes
AdhDebA.DAS0 Yes
AdhDsim\Adh-Ral1-2.P0 Yes
AdhdsRNA.cRa0 Yes
AdhE2mut0 Yes
AdhEip71CD.1880 Yes
AdhF.hs.P10 Yes
AdhF.hs.P20 Yes
AdhF.hs.P30 Yes
AdhF.hs.P40 Yes
AdhF.hs.P50 Yes
AdhF.hs.P60 Yes
AdhFA0 Yes
AdhFB0 Yes
AdhFbp1.-1300:+800 Yes
AdhFbp1.A110 Yes
AdhFbp1.A120 Yes
AdhFbp1.A10 Yes
AdhFbp1.A80 Yes
AdhFbp1.AHp0 Yes
AdhFbp1.ASt0 Yes
AdhFbp1.B160 Yes
AdhFbp1.C100 Yes
AdhFbp1.C210 Yes
AdhFbp1.H120 Yes
AdhFbp1.HHp0 Yes
AdhFbp1.HΔHp0 Yes
AdhFbp1.J160 Yes
AdhFbp1.J180 Yes
AdhFbp1.J90 Yes
AdhFbp1.M160 Yes
AdhFbp1.MHp0 Yes
AdhFbp1.N10 Yes
AdhFbp1.N30 Yes
AdhFbp1.O180 Yes
AdhFbp1.P0 Yes
AdhFbp1.R50 Yes
AdhFbp1.S110 Yes
AdhFbp1.SHp0 Yes
AdhFbp1.T70 Yes
AdhFbp1.X20 Yes
AdhFFS0 Yes
AdhFSF0 Yes
AdhFSS0 Yes
AdhfT176T0 Yes
AdhGC-1.B0 Yes
AdhGC-1.C0 Yes
AdhGC-1.D0 Yes
AdhGC-1.E0 Yes
AdhGC-1.F0 Yes
AdhGC-1.G0 Yes
AdhGC-1.H0 Yes
AdhGC-1.I0 Yes
AdhGC-1.J0 Yes
AdhGC-1.K0 Yes
AdhGGAX-70 Yes
AdhGGAX-880 Yes
AdhGGAX-80 Yes
AdhGOS0 Yes
AdhHAP-PEE0 Yes
AdhHAP0 Yes
AdhHindIII0 Yes
Adhhs.70CA700 Yes
Adhhs.70CAA0 Yes
Adhhs.A.700 Yes
Adhhs.A.A0 Yes
Adhhs.PC0 Yes
Adhhs.PG0 Yes
Adhhs.PS0 Yes
AdhK193T0 Yes
AdhKA27.MM0 Yes
AdhLsBbbf20 --
AdhLTR0 Yes
AdhMtnA.Pn0 Yes
Adhn4.Act5C.T:SV40\nls20 Yes
Adhn4.hs0 Yes
Adhn4.ΔIN3.Act5C.T:SV40\nls20 Yes
AdhnB.hs0 Yes
AdhnBR114.Act5C.T:SV40\nls20 Yes
AdhnBR114.ΔIN3.Act5C.T:SV40\nls20 Yes
AdhnL58A.hs0 Yes
AdhNS11860 Yes
AdhNS11910 Yes
AdhNS190 Yes
AdhNS10 Yes
AdhNS20 Yes
AdhNS30 Yes
AdhNS40 Yes
AdhNS50 Yes
AdhNS60 Yes
AdhNS70 Yes
AdhNS80 Yes
AdhNSΔ10 Yes
AdhNSΔ20 Yes
AdhNSΔ30 Yes
AdhNSΔ40 Yes
AdhNSΔ50 Yes
AdhNSΔ60 Yes
AdhNSΔ70 Yes
AdhNSΔ80 Yes
AdhP-3860 Yes
AdhPTC.ΔIN3.Act5C.T:SV40\nls20 Yes
AdhPTC2.ΔIN3.Act5C.T:SV40\nls20 Yes
AdhRI-42.tDa0 Yes
Adhrv10 --
Adhrv2-10 --
Adhrv20 --
Adhrv3-10 --
Adhrv3-20 --
Adhrv3-30 --
Adhrv50 --
Adhry.J150 Yes
Adhry.M120 Yes
Adhry.U40 Yes
Adhry.X10 Yes
Adhry.X30 Yes
AdhSA-400.80 Yes
AdhSalI0 Yes
AdhSFF0 Yes
AdhSFS0 Yes
AdhSgs3.GA930 Yes
AdhSgs3.glAd1300 Yes
AdhSgs3.glAd0 Yes
AdhSgs3.glAdE-G<down>1G2H3</up>0 Yes
AdhSgs3.glAdE-G<down>1H2H3</up>0 Yes
AdhSgs3.glAdE-H<down>1H2H3</up>0 Yes
AdhSgs3.glAdE0 Yes
AdhSgs3.glAdEΔU<down>1,2</up>0 Yes
AdhSgs3.glAdEΔU<down>1-3</up>0 Yes
AdhSgs3.glAdEΔU<down>1</up>0 Yes
AdhSgs3.glAdEΔU<down>1H1-3</up>0 Yes
AdhSgs3.glAdEΔU<down>1ΔU3RH1-3</up>0 Yes
AdhSgs3.glAdEΔU<down>3</up>0 Yes
AdhSgs3.glAdEΔU<down>3R</up>0 Yes
AdhSgs3.GOA.130 Yes
AdhSgs3.GOA.220 Yes
AdhSgs3.GOA.98.-100.-320 Yes
AdhSgs3.GOA.98.-101-930 Yes
AdhSgs3.GOA.98.-101.-750 Yes
AdhSgs3.GOA.98.-1020 Yes
AdhSgs3.GOA.98.-103.-530 Yes
AdhSgs3.GOA.98.-106-980 Yes
AdhSgs3.GOA.98.-340 Yes
AdhSgs3.GOA.98.-35.+2.-930 Yes
AdhSgs3.GOA.98.-370 Yes
AdhSgs3.GOA.98.-400 Yes
AdhSgs3.GOA.98.-430 Yes
AdhSgs3.GOA.98.-44.-43.-360 Yes
AdhSgs3.GOA.98.-45.-670 Yes
AdhSgs3.GOA.98.-470 Yes
AdhSgs3.GOA.98.-520 Yes
AdhSgs3.GOA.98.-540 Yes
AdhSgs3.GOA.98.-58.-810 Yes
AdhSgs3.GOA.98.-590 Yes
AdhSgs3.GOA.98.-60-520 Yes
AdhSgs3.GOA.98.-600 Yes
AdhSgs3.GOA.98.-61.-550 Yes
AdhSgs3.GOA.98.-62-540 Yes
AdhSgs3.GOA.98.-620 Yes
AdhSgs3.GOA.98.-630 Yes
AdhSgs3.GOA.98.-640 Yes
AdhSgs3.GOA.98.-65-570 Yes
AdhSgs3.GOA.98.-650 Yes
AdhSgs3.GOA.98.-66.+10 Yes
AdhSgs3.GOA.98.-670 Yes
AdhSgs3.GOA.98.-680 Yes
AdhSgs3.GOA.98.-690 Yes
AdhSgs3.GOA.98.-700 Yes
AdhSgs3.GOA.98.-710 Yes
AdhSgs3.GOA.98.-720 Yes
AdhSgs3.GOA.98.-730 Yes
AdhSgs3.GOA.98.-74-660 Yes
AdhSgs3.GOA.98.-74.-860 Yes
AdhSgs3.GOA.98.-750 Yes
AdhSgs3.GOA.98.-760 Yes
AdhSgs3.GOA.98.-770 Yes
AdhSgs3.GOA.98.-780 Yes
AdhSgs3.GOA.98.-790 Yes
AdhSgs3.GOA.98.-800 Yes
AdhSgs3.GOA.98.-810 Yes
AdhSgs3.GOA.98.-820 Yes
AdhSgs3.GOA.98.-83-750 Yes
AdhSgs3.GOA.98.-830 Yes
AdhSgs3.GOA.98.-84.-430 Yes
AdhSgs3.GOA.98.-850 Yes
AdhSgs3.GOA.98.-860 Yes
AdhSgs3.GOA.98.-870 Yes
AdhSgs3.GOA.98.-880 Yes
AdhSgs3.GOA.98.-89.-730 Yes
AdhSgs3.GOA.98.-890 Yes
AdhSgs3.GOA.98.-900 Yes
AdhSgs3.GOA.98.-91.-1030 Yes
AdhSgs3.GOA.98.-92-840 Yes
AdhSgs3.GOA.98.-92.+20 Yes
AdhSgs3.GOA.98.-930 Yes
AdhSgs3.GOA.98.-940 Yes
AdhSgs3.GOA.98.-950 Yes
AdhSgs3.GOA.98.-960 Yes
AdhSgs3.GOA.98.-970 Yes
AdhSgs3.GOA.98.-980 Yes
AdhSgs3.GOA.98.-99.-510 Yes
AdhSgs3.GOA.980 Yes
AdhSgs3.GOA.98DΔ3000 Yes
AdhSgs3.GOA.98DΔ300 Yes
AdhSgs3.GOA.98DΔ3540 Yes
AdhSgs3.GOA.98DΔ4100 Yes
AdhSgs3.GOA.98DΔ4400 Yes
AdhSgs3.GOA.98PΔ160 Yes
AdhSgs3.GOA.98PΔ200 Yes
AdhSgs3.GOA.98PΔ240 Yes
AdhSgs3.GOA.98PΔ880 Yes
AdhSgs3.GOA.98R0 Yes
AdhSgs3.GOA2.760 Yes
AdhSgs4.-4450 Yes
AdhSgs4.-4980 Yes
AdhSgs4.-5670 Yes
AdhSgs4.-8380 Yes
AdhSgs4.-838B0 Yes
AdhSgs4.-838C0 Yes
AdhSgs4.-838E0 Yes
AdhSgs4.3.I.II.III.IV0 Yes
AdhSgs4.5.I.II.III.IV0 Yes
AdhSgs4.AF-437-149:-568-4980 Yes
AdhSgs4.AF-464-1490 Yes
AdhSgs4.AF-498-1490 Yes
AdhSgs4.AF-498-2740 Yes
AdhSgs4.AF-498-3920 Yes
AdhSgs4.AF-498-4400 Yes
AdhSgs4.AF-515-1490 Yes
AdhSgs4.AF-515-4400 Yes
AdhSgs4.AF-568-1490 Yes
AdhSgs4.AF-568-149ΔII0 Yes
AdhSgs4.AF-568-2740 Yes
AdhSgs4.AF-568-274ΔII0 Yes
AdhSgs4.AF-568-3160 Yes
AdhSgs4.AF-568-3710 Yes
AdhSgs4.AF-568-3970 Yes
AdhSgs4.AF-568-4400 Yes
AdhSgs4.AF-568-4730 Yes
AdhSgs4.GARP-10 Yes
AdhSgs4.GARP-2120 Yes
AdhSgs4.GARP-3010 Yes
AdhSgs4.I.II0 Yes
AdhSgs4.I.III.IV0 Yes
AdhSgs4.I.III0 Yes
AdhSgs4.I0 Yes
AdhSgs4.II.III0 Yes
AdhSgs4.II0 Yes
AdhSgs4.III0 Yes
AdhSgs4.PASL0 Yes
AdhSgs4.SA-4000 Yes
AdhSgs4.SAX0 Yes
AdhSgs4.SMUL0 Yes
AdhSgs7.GAX0.120 Yes
AdhSgs7.GAX0.240 Yes
AdhSgs7.GAX0.260 Yes
AdhSgs7.GLAX1.00 Yes
AdhSSF0 Yes
AdhsT176T0 Yes
AdhT193K0 Yes
AdhTA20 Yes
AdhtAF00 Yes
Adhtra.rss0 Yes
Adhw.E10 Yes
Adhw.E20 Yes
Adhw.E40 Yes
Adhw.E50 Yes
Adhw.E60 Yes
Adhw.E70 Yes
Adhw.E80 Yes
Adhw.F10 Yes
Adhw.F20 Yes
Adhw.F30 Yes
Adhw.F4-10 Yes
Adhw.F4-20 Yes
Adhw.F4-30 Yes
Adhw.PR0 Yes
AdhWa-F.1-S0 Yes
AdhWa-F.10Leu0 Yes
AdhWa-F.1Leu0 Yes
AdhWa-F.6Leu0 Yes
AdhWa-F.C819T.G1756A0 Yes
AdhWa-F.C819T0 Yes
AdhWa-F.G1756A0 Yes
AdhWa-F.S0 Yes
AdhWa-F.tCa0 Yes
AdhWa-F.Δ1762-17690 Yes
AdhWa-S.1-F0 Yes
AdhWa-S.F0 Yes
AdhWa-S.tCa0 Yes
AdhWa-S.Δ1762-17690 Yes
AdhWX40090 Yes
AdhWX40140 Yes
AdhWX40150 Yes
AdhWX40160 Yes
AdhWX40170 Yes
AdhWX40500 Yes
AdhWX40630 Yes
AdhWX40640 Yes
AdhY152H0 Yes
AdhYp1.-8870 Yes
AdhYp1.37-1050 Yes
AdhYp1.65-360 Yes
AdhYp1.IRsub30 Yes
AdhYp1.PS0 Yes
AdhYp1.ZAPH0 Yes
AdhYp1.ZAPU0 Yes
AdhYp1.ZARG0 Yes
AdhYp1.ZARH0 Yes
AdhYp1.ZARS0 Yes
AdhYp1.ZARU0 Yes
AdhYp1.ZAΔUE0 Yes
AdhYp1Δb0 Yes
AdhYp1Δc0 Yes
AdhYp1Δd0 Yes
AdhYp1Δe0 Yes
AdhYp1Δf0 Yes
AdhYp1Δg0 Yes
AdhYp1Δh0 Yes
AdhYp1Δi0 Yes
AdhYp1Δj0 Yes
AdhΔ-1845:-6600 Yes
AdhΔ-2395:-6600 Yes
AdhΔ-2830:-6600 Yes
AdhΔ-447:-427.Adh0 Yes
AdhΔ-454:-440.Adh0 Yes
AdhΔ-470:-453.Adh0 Yes
AdhΔ-492:-481.Adh0 Yes
AdhΔ-497:-481.Adh0 Yes
AdhΔ-497:-489.Adh0 Yes
AdhΔ-531:-524.Adh0 Yes
AdhΔ-538:-532.Adh0 Yes
AdhΔ-543:-535.Adh0 Yes
AdhΔ1762-17650 Yes
AdhΔ1762-17690 Yes
AdhΔ1766-17690 Yes
AdhΔ3mut10 Yes
AdhΔ3mut20 Yes
AdhΔ3mut30 Yes
AdhΔcopia0 Yes
AdhΔIN3.Act5C.T:SV40\nls20 Yes
AdhΔIVS1,20 Yes
AdhΔIVS10 Yes
AdhΔIVS20 Yes
hide Aneuploid Aberrations
Disrupted in
Duplicated in
Not disrupted in
Not duplicated in
hide Transgenic Constructs & Insertions
Transgenic Constructs
UAS construct
NameExpression Data
P{GD10979}NA
P{GD10981}NA
P{GD17561}NA
P{GD17693}NA
P{TRiP.JF03042}NA
reporter construct
NameExpression Data
P{Adh-lacZ.Dsw}No
P{Adh-lacZ.mut.Adh-lacZ.wt.loxP.FRT}No
P{Adh-lacZ.P(m)}No
P{lacZAdh.AAE}No
P{lacZAdh.AEF1}No
P{lacZAdh.LsAEF1}No
P{lacZAdh.LsBbbf2}No
P{lacZAdh.LsC/EBP-S}No
P{lacZAdh.LsC/EBP-W}No
heat-shock construct
NameExpression Data
P{AdhALEhs}NA
P{hs/ADH1}NA
P{hs/ADH2a}NA
P{hs/ADH2b}NA
P{hs/ADH3}NA
P{hs/ADH4}NA
P{hs/ADH5}NA
P{hs/ADH6}NA
P{hs-Adh.C}NA
characterization construct
NameExpression Data
P{1009}NA
P{1010}NA
P{AFBFCS}NA
P{AFBSCF}NA
P{AFBSCS}NA
P{ASBFCF}NA
P{ASBFCS}NA
P{ASBSCF}NA
P{Adh3.2XbaI}NA
P{Adh3.2A}NA
P{Adh3.2-ry}NA
P{Adh4.8}NA
P{Adh4.8EcoRI}NA
P{Adh4.8-ry}NA
P{Adh8.6}NA
P{Adh11.8SacI}NA
P{Adh.E2mut}NA
P{Adh.Wa-F.1Leu}NA
P{Adh.Wa-F.6Leu}NA
P{Adh.Wa-F.10Leu}NA
P{Adh.Wa-F.S}NA
P{Adh.Wa-F.tri1-S}NA
P{Adh.Wa-F.Δ1762-1769}NA
P{Adh.Wa-F}NA
P{Adh.Wa-S.F}NA
P{Adh.Wa-S.tri1-F}NA
P{Adh.Wa-S.Δ1762-1769}NA
P{Adh.Wa-S}NA
P{Adh.Δ3mut1}NA
P{Adh.Δ3mut2}NA
P{Adh.Δ3mut3}NA
P{Adh5'3'AAE}NA
P{Adh5'P3'DP}NA
P{Adh+t3.2.Δ-492/-481}NA
P{AdhALE/P-80}NA
P{AdhALE/P-110}NA
P{AdhALE/P-187}NA
P{AdhALE/P-242}NA
P{AdhALE/P-386}NA
P{AdhD-66/+53}NA
P{AdhD-69/-386}NA
P{AdhD-69}NA
P{AdhD-127/-63}NA
P{AdhD-660/-60}NA
P{AdhD-660/-128}NA
P{AdhD-660}NA
P{AdhD-1320}NA
P{AdhD-2190}NA
P{AdhD-2830}NA
P{AdhD-3350}NA
P{AdhD-3550}NA
P{AdhD-5000}NA
P{AdhD+53/+328}NA
P{AdhFA}NA
P{AdhFB}NA
P{AdhfT176T}NA
P{AdhHindIII}NA
P{AdhKA27.MM}NA
P{AdhL193T}NA
P{AdhLsBbbf2}NA
P{AdhLTR}NA
P{AdhP-386}NA
P{Adhrv1}NA
P{Adhrv2-1}NA
P{Adhrv2}NA
P{Adhrv3-1}NA
P{Adhrv3-2}NA
P{Adhrv3-3}NA
P{Adhrv5}NA
P{AdhSalI}NA
P{AdhsT176T}NA
P{AdhT193L}NA
P{AdhΔ1762-1765}NA
P{AdhΔ1762-1769}NA
P{AdhΔ1766-1769}NA
P{AdhΔ-1845/-660}NA
P{AdhΔ-2395/-660}NA
P{AdhΔ-2830/-660}NA
P{Adh-Ddc}NA
P{Adh-lac1}NA
P{Adh-lac2}NA
P{Adh-lac3}NA
P{Adh-lac4}NA
P{Adh-lac5}NA
P{Adh-lac6}NA
P{Adh-lacZ.mut.loxP.(-FRT)}NA
P{Adh-lacZ.wt.(-loxP).FRT}NA
P{Adh-w.B}NA
P{AP-2}NA
P{AP-5}NA
P{Daff\Adh}NA
P{Ddc+,Adh+}NA
P{Dhaw\Adh-JJ1}NA
P{Dhaw\Adh-JJ3}NA
P{Dmul\Adh-1+}NA
P{Dmul\Adh-1LS1}NA
P{Dmul\Adh-1LS2}NA
P{Dmul\Adh-1LS3}NA
P{Dmul\Adh-1LS4}NA
P{Dmul\Adh-1LS5}NA
P{Dmul\Adh-1LS6}NA
P{Dmul\Adh-1LS7}NA
P{Dmul\Adh-1LS8}NA
P{Dmul\Adh-1LS9}NA
P{Dmul\Adh-1LS10}NA
P{Dmul\Adh-1LS11}NA
P{Dmul\Adh-1LS12}NA
P{Dmul\Adh-1LS13}NA
P{Dmul\Adh-1LS14}NA
P{Dmul\Adh-1LS15}NA
P{Dmul\Adh-1LS16}NA
P{Dmul\Adh-1LS17}NA
P{Dmul\Adh-1LS18}NA
P{Dmul\Adh-1LS19}NA
P{Dmul\Adh-1LS20}NA
P{Dmul\Adh-1LS21}NA
P{Dmul\Adh-1LS22}NA
P{Dmul\Adh-1LS23}NA
P{Dmul\Adh-1LS24}NA
P{Dmul\Adh-1ΔA}NA
P{Dmul\Adh-1ΔAB}NA
P{Dmul\Adh-1ΔAS}NA
P{Dmul\Adh-1ΔB}NA
P{Dmul\Adh-1ΔS1}NA
P{Dmul\Adh-1ΔS2}NA
P{GAL4-Adh.Dmul}NA
P{GOS}NA
P{hs/ADH2}NA
P{hs-Adh.HAP}NA
P{mutC819T}NA
P{mutC819T-G1756A}NA
P{mutG1756A}NA
P{NS1}NA
P{NS2}NA
P{NS3}NA
P{NS4}NA
P{NS5}NA
P{NS6}NA
P{NS7}NA
P{NS8}NA
P{RI42.Δcopia}NA
P{RI42}NA
P{SAC}NA
P{Sgs4-Adh.SAX}NA
P{tARP-9}NA
Insertions
Type of insertions
Name
Expression data
insertion of enhancer trap
hide Gene Ontology: Function, Process & Cellular Component ( 14 unique terms )
hide Terms Based on Experimental Evidence ( 13 terms )
Molecular Function
CV term
References
inferred from direct assay
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProtKB)
inferred from physical interaction with Adh
Biological Process
CV term
References
inferred from direct assay
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProtKB)
inferred from mutant phenotype
inferred from direct assay
Cellular Component
CV term
References
inferred from direct assay
inferred from physical interaction with Adh
hide Terms Based on Predictions or Assertions ( 1 term )
Molecular Function
CV term
References
Biological Process ( 0 terms)
Cellular Component ( 0 terms)
hide Sequence Ontology: Class of Gene
hide Interactions & Pathways
hide Summary of Physical Interactions
Protein-protein
Interacting group
Assay
References
hide Summary of Genetic Interactions
Interacts with
Please look at the allele data for full details of the genetic interactions
Adh allele
Gene
References
hide External Data
Linkouts
DroID - A comprehensive database of gene and protein interactions.
InterologFinder Protein-protein interactions (PPI) from both known and predicted PPI data sets.
hide Orthologs
Genome-wide drosophilid orthologs
Curated drosophilid orthologs
Linkouts
InParanoid A subset of ortholog calls from InParanoid.
OrthoDB (Arthropod subset) The hierarchical catalog of eukaryotic orthologs.
hide Stocks & Reagents
hide Stocks Listed in FlyBase ( 263 )
Bloomington
6040
3975
3976
Kyoto
101293
107539
101299
hide Genomic Clones ( 2 )
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
hide 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
cDNA Clones, End Sequenced (ESTs)
BDGP DGC clones
Other clones
hide RNAi & Array Information
Linkouts
DRSC - Results from RNAi screens.
GenomeRNAi - GenomeRNAi – A database for cell-based and in vivo RNAi phenotypes and reagents
hide Antibody Information
monoclonal
hide Other Information
hide Discoverer
hide Etymology
hide Identification
hide Relationship to Other Genes
Source for database identity 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.
hide 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.
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.
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.
AdhF homozygotes usually show a better ability to survive on ethanol as a sole energy source than AdhS homozygotes.
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.
The relative thermostabilities of the Adh products are to be AdhS > AdhF > Adhn5 > AdhD.
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.
Flies carrying AdhF tend to be more resistant than those carrying only AdhS to ethanol.
AdhF and AdhS homozygotes show behavioural differences in their response to ethanol.
flies lacking Adh protein rapidly become intoxicated and eventually die on exposure 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 protein is maternally inherited by embryos and resulting larvae.
Utilization of ethanol as an energy source depends on Adh activity.
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.
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.
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Sequence Crossreferences
RefSeq (Transcripts)
RefSeq (Proteins)
Entrez Gene - A searchable database of RefSeq genes.
Other Crossreferences
EPD - Eukarytoic Promoter Database, an annotated collection of POL II promoters
InterPro domains - A database of protein families, domains, and functional sites
Linkouts
DroID - A comprehensive database of gene and protein interactions.
DRSC - Results from RNAi screens.
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
FlyMine - Integrated genomics database for Drosophila, Anopheles, and C.elegans
GenomeRNAi - GenomeRNAi – A database for cell-based and in vivo RNAi phenotypes and reagents
InParanoid A subset of ortholog calls from InParanoid.
InterologFinder Protein-protein interactions (PPI) from both known and predicted PPI data sets.
modMine - Data generated by the modENCODE project.
OrthoDB (Arthropod subset) The hierarchical catalog of eukaryotic orthologs.
REDfly - A database of transcriptional regulatory elements.
hide Synonyms & Secondary IDs ( 17 )
Reported As
Symbol Synonym
Adh
(Heinstra et al., 1983, Leal and Barbancho, 1992, Winberg et al., 1982, Beller et al., 2006, Beller et al., 2006, Wang et al., 2004, Akashi et al., 2006, Kadener et al., 2006, Rehwinkel et al., 2005, Geiger-Thornsberry and Mackay, 2004, LANG et al., 2007, Pérez-Farrerons and Juan, 2007, Katoh et al., 2000, Holloway et al., 2008, Gim et al., 2001, Negre et al., 2006, Lott et al., 2011, Carlini, 2004, Malherbe et al., 2005, Glavan et al., 2006, Vasemagi, 2006, Pal Bhadra et al., 2006, Wei and Brennan, 2001, Stark et al., 2007, Jagadeeshan and Singh, 2005, Casillas et al., 2007, Wei and Brennan, 2000, Chen and Stephan, 2003, Gonzalez et al., 2000, Walser et al., 2006, Metzstein and Krasnow, 2006, Dorus, 2008.10.28, Schmidt et al., 2005, Dorus et al., 2006, McDermott and Kliman, 2008, Juven-Gershon et al., 2008, Eanes et al., 2009, Hollis et al., 2009, Li et al., 2009, O'Keefe et al., 2011, Laayouni et al., 2007, Passananti et al., 2004, Deckert-Cruz et al., 2004, Vaulin and Zakharov, 2006, Noor and Kliman, 2003, Veuille et al., 2004, Ludwig and Loreto, 2007, Montooth et al., 2006, Christophides et al., 2001, Schlenke and McKean, 2005, Jensen et al., 2006, Grönke et al., 2007, Umina et al., 2006, Roote, 2009.11.24, Zhang and Townsend, 2009, Morozova et al., 2007, Ranz et al., 2004, Adryan et al., 2007, Hense et al., 2010, Jung et al., 2010, Lang and Juan, 2010, Wu et al., 1998, Colon-Parrilla and Perez-Chiesa, 1999, Kovac and Marinkovic, 1999, Albalat et al., 2001, Reumer et al., 2009, Gao et al., 2011, Bokor and Pecsenye, 2000)
Reg-1
 
Name Synonym
alcoholdehydrogenase
alcohol dehyrdrogenase
Drosophila Rhythmically expressed gene 1
Secondary FlyBase IDs
  • FBgn0016704
  • FBgn0052954
hide References ( 1067 )
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hide Recent research papers ( 10 )
Gao et al., 2011, Molec. Phylog. Evol. 60(1): 98--107
Phylogenetic relationships between Sophophora and Lordiphosa, with proposition of a hypothesis on the vicariant divergences of tropical lineages between the Old and New Worlds in the family Drosophilidae. [FBrf0213767]
Graveley et al., 2011, Nature 471(7339): 473--479
The developmental transcriptome of Drosophila melanogaster. [FBrf0213330]
Lott et al., 2011, PLoS Biol. 9(2): e1000590
Noncanonical Compensation of Zygotic X Transcription in Early Drosophila melanogaster Development Revealed through Single-Embryo RNA-Seq. [FBrf0213135]
O'Keefe et al., 2011, Hum. Mol. Genet. 20(3): 497--509
Drosophila orthologue of WWOX, the chromosomal fragile site FRA16D tumour suppressor gene, functions in aerobic metabolism and regulates reactive oxygen species. [FBrf0212691]
Sun et al., 2011, PLoS ONE 6(4): e18215
Systems-scale analysis reveals pathways involved in cellular response to methamphetamine. [FBrf0213560]
Hense et al., 2010, Genetics 184(2): 547--555
Experimentally increased codon bias in the Drosophila adh gene leads to an increase in larval, but not adult, alcohol dehydrogenase activity. [FBrf0209817]
Jung et al., 2010, Genomics 96(3): 154--166
Identification of conserved Drosophila-specific euchromatin-restricted non-coding sequence motifs. [FBrf0211521]
Lang and Juan, 2010, Nucleic Acids Res. 38(19): 6404--6417
Binding site number variation and high-affinity binding consensus of Myb-SANT-like transcription factor Adf-1 in Drosophilidae. [FBrf0212173]
Mahapatra et al., 2010, Toxicol. Sci. 116(1): 225--238
Identification of methylmercury tolerance gene candidates in Drosophila. [FBrf0211073]
Robinson et al., 2010, Mech. Ageing Dev. 131(9): 584--590
Insights into aging through measurements of the Drosophila proteome as a function of temperature. [FBrf0211959]
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All reviews listed in FlyBase were published before 2010