Gpdh, αGpdh, α-Gpdh, Glycerol 3 phosphate dehydrogenase, glycerol-3-phosphate dehydrogenase
Please see the JBrowse view of Dmel\Gpdh1 for information on other features
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AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.53
Gene model reviewed during 5.46
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.39
Tissue-specific extension of 3' UTRs observed during later stages (FBrf0218523, FBrf0219848); all variants may not be annotated
Gene model reviewed during 5.56
1.6 (northern blot)
1.7 (northern blot)
One of several products generated by alternative splicing.
Homodimer.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Gpdh1 using the Feature Mapper tool.
The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).
Transcript levels increase 3-fold when dietary sucrose is raised from 0.1% to 10%. Transcript levels also increase with dietary glucose and starch but not fructose. Ethanol has no effect on transcript abundance.
Transcript levels increase 10-fold when dietary sucrose is raised from 0.1% to 10%. Transcript levels also increase with dietary glucose, starch or ethanol but no effect on transcript levels is observed in response to increase fructose. Sucrose and ethanol combined have no additive effect on transcript levels.
Gpdh1 transcripts containing terminal exon 6 are detected in larval and adult RNA.
Gpdh1 transcripts containing terminal exon 7 are detected in larval and adult RNA.
Gpdh1 transcripts containing terminal exon 8 are detected in adult RNA.
Different Gpdh1 transcripts and isoforms are generated by alternate splicing at the 3' end of the gene. Transcripts containing terminal exon 7 are abundant in larvae and are present at lower levels in adults.
Different Gpdh1 transcripts and isoforms are generated by alternate splicing at the 3' end of the gene. Transcripts containing terminal exon 8 are detected weakly in larvae and adults.
Different Gpdh1 transcripts and isoforms are generated by alternate splicing at the 3' end of the gene. Transcripts containing terminal exon 9 are abundant in adults and are not detected in larvae.
Glycolytic enzymes, including Gpdh1 protein are localized to M bands and Z discs, as visualized in the isolated myofibrils of flight muscles, where immunoreactivity appears as alternating bright and less-intense bands.
Gpdh1 activityincreases nearly fourfold when dietary sucrose is increase from 0.1% to10%. Glucose, fructose, or starch at a 5% concentration also lead to a2-3-fold increase in Gpdh1 activity. Gpdh1 activity increases withincreasing ethanol. Sucrose and ethanol together have an additive effecton Gpdh1 activity.
JBrowse - Visual display of RNA-Seq signals
View Dmel\Gpdh1 in JBrowse2-18
2-19.2
2-17.8
Mapping based on 422 recombinants.
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
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 JBrowse for alignment of the cDNAs and ESTs to the gene model.
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.
Alleles whose expressed products have 50-100% GPDH activity show an average relative viability of 51.6%. There is no significant effect between flies with different combinations of Gpdh alleles on the response of triglyceride and glycogen pools to starvation and refeeding treatments, when the activity of the expressed Gpdh products is as low as 10%.
Mutation rate at microsatellite loci in 119 lines maintained for approximately 250 generations is estimated to be 6.3x10-6, at least one order of magnitude lower than the mutation rate in mammals.
At least a substantial fraction of three glycolytic enzymes of flight muscle cells are found colocalised at the Z-discs and M-lines, glycolytic enzyme colocalisation is interdependent. Localisation of Gapdh1, Gapdh2 and Ald at the Z-discs and M-lines requires the presence of at least Gpdh at the Z-discs and M-lines.
DNA sequence analysis demonstrates the change in electrophoretic mobility in each of the six naturally occurring but rare ultra fast alleles of Gpdh are caused by a single amino acid residue substitution in the encoded protein.
Gpdh enzyme activity has been measured in D.melanogaster lines in which spontaneous mutations have accumulated over approximately 300 mutations.
The effects of a high sucrose diet on live weight, total protein, stored lipid and glycogen and crude activities of 12 enzymes involved in energy metabolism are quantified. The activities of many enzymes are reduced by the sucrose treatment.
Distribution of allele frequencies at seven polymorphic loci in 12 natural Indian populations studied: frequencies of particular alleles at Zind\Acph-1, Zind\Acph-2, Zind\Mdh1, Zind\Ao, Zind\Adh and Gpdh are positively correlated with latitude.
Polymorphism of electrophoretic forms of Adh and α-Gpdh has been studied in 11 natural populations of drosophilids. Polymorphism was higher for Adh than for α-Gpdh.
Widespread category of low-activity variant with reduced transcription of Gpdh were shown to have P elements inserted between the TATA box and the transcription start site: the target site for all the insertions is GTGCAAAC.
Gramoxone has no mutagenic effect on the genetic background of Gpdh.
The synergistic effects of the Adh locus, or a tightly linked locus, on the quantities of the Mdh1, Gpdh, Pgm, Idh, Men and Gapdh1 gene products in D.melanogaster derived from an African population has been determined.
An investigation of the role of temperature resistance in the world-wide cline of Adh and Gpdh allele frequencies demonstrated that allele frquencies cannot simply be explained by genotypic differences in resistance to high temperatures.
No difference in allele fixed in lines selected over 700 generations for high (negative) and low (positive) geotaxis.
The Gpdh locus in the Cardwell population has been assessed and found to carry a duplication in one third of the lines, these lines have a higher level of Gpdh gene activity. The duplication is incomplete and lacks exons 1 and 2, and can also be found in populations from Chinese and Africa. Three insertions are present in the gene region, only one affected Gpdh activity.
Characterization of the 26A region has identified the Gpdh transcription unit at the 26A5-26A7 region.
The interactions of Adh and Gpdh genotypes with different temperature (20--29oC) was studied for changes in developmental time, adult weight, protein content of adult males and triglyceride content of adult males.
Modulation of Gpdh, Ald, Pgk and RpL32 proteins and their transcript levels was investigated in larvae.
Gpdh has been cloned and sequenced.
A shift in third-codon-nucleotide frequency is seen when comparing species of the two subgenera Drosophila and Sophophora. This data is comparable to codon usage of Gpdh in D.melanogaster. The reason for the shift in codon usage is unknown.
A strong linkage disequilibrium due to the presence of the inversion In(2L)t was found between the Adh and Gpdh loci in a seminatural population kept in a tropical greenhouse for a prolonged period. The inversion frequency increased at high temperatures accompanied by an increase in AdhS and GpdhA frequency. Selection is a likely cause of any changes that occurred, mediated by average temperature and selection acting on the chromosomal rearrangement and hitchhiking of the allozymes.
The relative viability of Gpdh/Gpo double mutants has been studied to determine certain interactions between Gpdh and Gpo.
Adh and Gpdh null alleles have been detected in Australian populations at frequencies up to 3.9%.
Gpdh protein expression during different stages of development has been studied.
The effect of dietary sucrose and ethanol on Gpdh activity in the third larval instar has been studied.
Allelic frequencies have been determined between European and African populations. African populations show a greater genetic diversity, as measured by the number of alleles found. Within each geographic group there is a homogeneity of allele frequencies.
A series of Gpdh-Gpo double mutants were constructed by Davis and MacIntyre (1988); four of these mutants were found to be viable and flightless; two others were allele-dependent synthetic lethals. A trans-acting regulatory element tightly linked to the Gpdh locus has been isolated in a natural population of D.melanogaster in Tasmania (Gibson, Wilks, Cao and Freeth, 1986). Flies homozygous for second chromosomes carrying the element (designated H31) have half the GPDH activity of normal homozygotes.
The structural gene for α glycerol-3-phosphate dehydrogenase (NAD+) (α GPDH), a homodimer with subunit molecular weight 31700 (Collier, Sullivan and MacIntyre, 1976). Natural populations are polymorphic for electrophoretic variants as well as for regulatory elements that determine enzyme level; induced electromorphs have also been recovered. There are a number of spontaneous and induced amorphic and hypomorphic alleles. Purification and structural analysis of enzyme by Niesel, Bewley, Miller, Armstrong and Lee (1980). Three isozymes designated GPDH-1, GPDH-2, and GPDH-3 in order of decreasing rate of migration toward the anode (Wright and Shaw, 1968). The three forms respond alike to electrophoretic alleles, null alleles and dosage of Gpdh+ (Bewley, Rawls and Lucchesi, 1974); all three are products of the same structural gene for developmental profile (see Bewley, 1981). GPDH-1 first appears in late pupae and is present in high concentration in the adult thorax where it functions to provide energy for flight muscles; GPDH-2 also appears in late pupae and is present in low concentration throughout the fly; GPDH-3 is present throughout the life cycle; it is concentrated in the larval fat body (Rechsteiner, 1970) and the adult abdomen (Wright and Shaw, 1968); GPDH-1 and GPDH-3 present in equal amounts in adult head. Product of paternally inherited allele first appears at 22 hr, just before hatching of larva (Wright and Shaw, 1968). GPDH-1 is stable at 50oC but decays at 57oC; GPDH-3 is labile at 50oC (Bewley et al.). Studies by Bewley and Lucchesi indicate the presence of a heat-labile RNase-resistant factor in crude larval extracts able to convert GPDH-1 into GPDH-2 and GPDH-3 but not vice versa; GPDH-3 lacks three C-terminal amino acids present on GPDH-1 (Niesel, Bewley, Miller, Armstrong and Lee, 1980). Homozygotes for null alleles are fertile, show reduced viability and are unable to sustain flight (O'Brien and MacIntyre, 1972); ultrastructural integrity of flight muscle sarcosomes degenerates prematurely (O'Brien and Shimada, 1974). Homozygous stocks maintained for 25 generations regain the ability to fly despite continued absence of GPDH activity (O'Brien and Shimada, 1974).
Source for identity of: Gpdh1 Gpdh
