FlyBase Allele Report: Dmel\Adh[S]

General Information

Symbol

Dmel\Adh^S

Species

D. melanogaster

Name

Slow

FlyBase ID

FBal0000321

Feature type

allele

Associated gene

Dmel\Adh

Associated Insertion(s)

Carried in Construct

Also Known As

S, Adh-S

Key Links

Genomic Maps

JBrowse

Allele class

Mutagen

Nature of the Allele

Allele class

Mutagen

spontaneous

natural population

(Parkash et al., 1993)

Progenitor genotype

Cytology

Description

Amino acid replacement: T192K.

(Thatcher, 1980)

Standard nucleotide and protein sequence.

Mutations Mapped to the Genome

Curation Data

Type

Location

Additional Notes

References

sequence_variant

2L:14,617,051..14,617,051 [+]

Nucleotide change:

C8826A

Amino acid change:

Reported amino acid change:

T192K

Comment:

Amino acid substitution in Adh^S electrophorectic variant relative to Adh^F; site of nucleotide substitution in mutant inferred by FlyBase based on reported amino acid change.

(Thatcher, 1980)

Variant Molecular Consequences

Associated Sequence Data

DDBJ / EMBL / GenBank

DNA sequence

Protein sequence

UniProtKB/Swiss-Prot

P00334

UniProtKB/TrEMBL

Expression Data

Reporter Expression

Additional Information

Statement

Reference

Marker for

Reflects expression of

Reporter construct used in assay

Human Disease Associations

Disease Ontology (DO) Annotations

Models Based on Experimental Evidence ( 0 )

Disease

Evidence

References

Modifiers Based on Experimental Evidence ( 0 )

Disease

Interaction

References

Comments on Models/Modifiers Based on Experimental Evidence ( 0 )

Disease-implicated variant(s)

Phenotypic Data

Phenotypic Class

chemical resistant

(Garrido and Barbancho, 1990)

chemical sensitive

(Garrido and Barbancho, 1990)

electrophoretic variant

(Bubli et al., 1996, Parkash and Shamina, 1994, Parkash et al., 1993, Parkash and Vashisht, 1991)

Phenotype Manifest In

Detailed Description

Statement

Reference

Oviposition sites on standard medium and acetic acid supplement medium are studied.

(Eisses, 1997)

If reared at 25^oC homozygotes died at 35^oC. Flies reared at 29^oC showed less significant differences in survival between genotypes than flies reared at 20^oC and 25^oC.

(Oudman et al., 1992)

Egg to adult developmental time of Adh genotypes depends on the Gpdh genotype and temperature. Homozygotes demonstrate fast development with all Gpdh genotypes, the Adh^F/Adh^S heterozygote shows an intermediate rate between the homozygotes. Adult weight of Adh genotypes is not affected by temperature or Gpdh genotype: Adh heterozygote is significantly heavier than the homozygotes, which have a similar weight.

(Oudman et al., 1991)

Resistant to ethanol, sensitive to pentenol.

(Garrido and Barbancho, 1990)

Adh^F/Adh^S flies are more resistant to the effect of high temperature.

(Totskii et al., 1990)

External Data

Linkouts

Interactions

Show genetic interaction network for Enhancers & Suppressors

Phenotypic Class

Phenotype Manifest In

Additional Comments

Genetic Interactions

Statement

Reference

Xenogenetic Interactions

Statement

Reference

Complementation and Rescue Data

Comments

Images (0)

Mutant

Wild-type

Stocks (5)

Bloomington

4062

w¹¹¹⁸; Adh^S

6042

Adc^b-1 Adh^S pr¹ cn¹

2369

SM1, Got2¹ Gpdh1^A Mdh1⁴ Adh^F Cndp2⁴ Hex-C⁴ Amy-d¹/Got2² Gpdh1^B Mdh1⁶ Adh^S Cndp2² Hex-C⁶ Amy-p² Amy-d³

Kyoto

101984

Gpdh1^B Mdh1^S Adh^S ; Fdh^S Aldox89A^S

107289

SM1, Got2¹ Gpdh1^A Mdh1⁴ Adh^F Cndp2⁴ Hex-C⁴ Amy-d¹; Got2² Gpdh1^B Mdh1⁶ Adh^S Cndp2² Hex-C⁶ Amy-p² Amy-d³

Notes on Origin

Discoverer

Johnson and Denniston.

Comments

pI of protein: 7.

The frequency of Adh^F in a wine cellar was higher than Adh^S. Statistical analysis demonstrates a significant increase of Adh^F inside the cellar with respect to outside, and the converse situation or Adh^S.

(Wallace, 1984)

The analysis of within and between species polymorphism has shown a balanced polymorphism near position 1490, the site of the amino acid replacement difference (lys to thr) between Adh^F and Adh^S. The pattern of silent polymorphisms in the coding region can be explained by the presence of the single balanced polymorphism.

(Kreitman and Hudson, 1991)

Adh^F homozygote and the Adh^F/Adh^S heterozygote have a high adult male protein content within the temperature range analysed. The Adh heterozygote has a significantly lower triglyceride content than the homozygotes which have a similar higher content, the values varied slightly in different Gpdh genotypes and temperatures. At all the temperatures ADH activity in Adh^F homozygotes is high in all Gpdh genotypes and the Adh heterozygote ADH activity is intermediate between the homozygotes.

(Oudman et al., 1991)

Adult homozygotes have approximately twice the level of ADH activity and CRM as do D.simulans flies.

(Thomson et al., 1991)

This allele fixed in lines selected for high geotaxis.

(Stoltenberg et al., 1992)

Protein content, triglyceride content and ADH enzyme activity decreased significantly at 35^oC, no correlation was observed between survival and these traits.

(Oudman et al., 1992)

Average Adh protein activity was higher in Chinese than Australian populations for Adh^F and Adh^S lines. There is a significant correlation between Adh protein activity and Adh protein levels. Adh^F lines had more CRM than Adh^S lines.

(Jiang and Gibson, 1992)

Homozygotes have decreased specific activities of Mdh1, Gpdh, Pgm, Idh, Me and Gapdh1 gene products. The differences between the enzyme quantities in Adh^F homozygotes and Adh^S homozygotes segregate as if caused by a single Mendelian gene with codominant alleles.

(Li, 1992)

Gramoxone increases the frequency of the Adh^S allele and decreases the frequency of the Adh^F allele in the offspring of treated flies.

(el Abidin Salam et al., 1993)

The frequency of the Adh^S allele in Eurasian natural populations is negatively correlated with latitude and the average rainfall of the driest calendar month, and positively correlated with the average temperature of the coldest calendar month and the average rainfall of the wettest calendar month.

(Bublii et al., 1994)

The influence of starvation on Adh^S enzyme activity has been studied in D.melanogaster larvae and adults.

(Pecsenye et al., 1994)

The influence of ethanol on Adh^S enzyme activity has been studied in D.melanogaster larvae.

(Pecsenye et al., 1994)

External Crossreferences and Linkouts ( 1 )

Crossreferences

UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information

P00334

Synonyms and Secondary IDs (6)

Reported As

Symbol Synonym

ADH-S

(Bublii et al., 1994)

Adh-S

(Andolfatto et al., 1999, Eisses et al., 1994)

Adh^II

(Pipkin et al., 1976)

Adh^S

(Wu et al., 1998)

(Ochando and Ayala, 1999, Bubli et al., 1996, Vasisht et al., 1996, McDonald, 1994, el Abidin Salam et al., 1993, el Amrani et al., 1992, Stoltenberg et al., 1992, Totskii et al., 1990)

Name Synonyms

Slow

(Andolfatto, 2001, Crossley and Hirsch, 1991)

Secondary FlyBase IDs

References (119)

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