Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS)
The protein contains 408 amino acids for an estimated molecular weight of 44501 Da.
May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity). (updated: April 1, 2015)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs2285514 |
No binding partner found
The reference OMIM entry for this protein is 609169
Glyceraldehyde-3-phosphate dehydrogenase, spermatogenic; gapdhs
Gapds
Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
Gapd2
DESCRIPTION
Glyceraldehyde 3-phosphate dehydrogenases (EC 1.2.1.12), such as GAPDS, are NAD-dependent enzymes that remove hydrogen and add phosphate to glyceraldehyde 3-phosphate to form 1,3-diphosphoglycerate (summary by Welch et al., 2000).CLONING
Using mouse Gapds to probe a testis cDNA library, Welch et al. (2000) cloned human GAPDS, which they designated GAPD2. The deduced 408-amino acid protein contains a 72-amino acid proline-rich N-terminal segment not found in somatic cell GAPD (138400), and the remainder of the molecule contains conserved residues that fold into the substrate-binding site and NAD+ cofactor-binding pocket. GAPDS shares 83% amino acid identity with mouse Gapds and 68% identity with GAPD. Northern blot analysis of several tissues detected a 1.5-kb GAPDS transcript only in testis. Immunolocalization of GAPDS in fixed permeabilized spermatozoa showed staining restricted to the principal piece of the flagellum. By SDS-PAGE, GAPDS had an apparent molecular mass of about 56 kD. GAPDS activity, purified from spermatozoa, resisted detergent extraction with CHAPS and remained associated with relatively insoluble components.GENE STRUCTURE
Welch et al. (2000) determined that the GAPDS gene contains 11 exons.MAPPING
By FISH, Welch et al. (2000) mapped the GAPDS gene to chromosome 19q13.1.MOLECULAR GENETICS
Several groups, including Myers et al. (2002), have reported linkage on chromosome 12 in late-onset Alzheimer disease (LOAD; 104300) families. To follow up on these results, Li et al. (2004) genotyped 282 single-nucleotide polymorphisms (SNPs) under the linkage peak which their group had previously identified, studying a multiple case-control series totaling 1,089 AD subjects and 1,196 non-demented controls. A strong association was observed in a small region chromosome 12 that includes the GAPD gene (138400), which led them to examine this gene and its paralogs on other chromosomes. These studies showed association with 2 other paralogs: GAPD2 on chromosome 19, and a GAPD pseudogene on chromosome 12. A significant association between LOAD and a compound genotype of 3 GAPD genes was observed in all 3 sample sets. Individually these SNPs made differential contributions to disease risk in each of the case-control series, suggesting that variants in functionally similar genes may account for series-to-series heterogeneity of disease risk. In general, the observations raised the possibility that the GAPD genes are AD risk factors, a hypothesis that is consistent with the role of GAPD in neuronal apoptosis.ANIMAL MODEL
Miki et al. (2004) disrupted expression of the Gapds gene to selectively block sperm glycolysis in mice. Gapds -/- males were infertile and had profound defects in sperm motility, exhibiting sluggish movement without forward progression. Although mitochondrial oxygen consumption was unchanged, sperm from Gapds -/- mice had ATP levels that were only 10.4% of those in sperm from wildtype mice. Miki et al. (2004) concluded that most of the energy required for sperm motility is generated by glycolysis rather than oxidative phosphorylation. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609169 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed