Glucosamine-6-phosphate isomerase 1 (GNPDA1)
The protein contains 289 amino acids for an estimated molecular weight of 32669 Da.
Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity). (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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Biological Process
Carbohydrate metabolic process
Generation of precursor metabolites and energy
Glucosamine catabolic process
N-acetylglucosamine catabolic process
N-acetylglucosamine metabolic process
N-acetylneuraminate catabolic process
Single fertilization
UDP-N-acetylglucosamine biosynthetic process
The reference OMIM entry for this protein is 601798
Glucosamine-6-phosphate deaminase 1; gnpda1
Gnp1
Gnpi
Oscillin, hamster, homolog of
Kiaa0060
DESCRIPTION
Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium (Arreola et al., 2003).CLONING
By sequencing clones obtained from the KG-1 immature myeloid cell line, Nomura et al. (1994) cloned GNPDA1, which they designated KIAA0060. The deduced protein contains 289 amino acids. Northern blot analysis detected GNPDA1 expression in all human tissues and cell lines examined, with highest expression in ovary and colon and in KG-1 and HeLa cell lines. The hamster sperm oscillin protein is responsible for oocyte calcium oscillations. By screening a testis cDNA library for a homolog of hamster oscillin, Shevchenko et al. (1998) obtained a cDNA encoding GNPI. The deduced 289-amino acid protein is 96% identical to the hamster sequence. SDS-PAGE and Western blot analysis showed that GNPI was expressed as a 33-kD cytosolic protein in various cell lines. By screening a mouse EST database for sequences similar to hamster oscillin, followed by screening human BAC genomic libraries by PCR, Nakamura et al. (2000) identified the GNPI gene. Northern and dot blot analyses revealed ubiquitous expression that was highest in spleen, ovary, kidney, uterus, and testis. Promoter analysis indicated that GNPI is most likely a housekeeping gene.GENE FUNCTION
In the course of investigating hexosamine catabolism in the human malaria parasite, Plasmodium falciparum, Weidanz et al. (1995) became aware of deficiencies in understanding the relevant enzymatic reactions in the host erythrocyte. For that reason, they undertook studies of human glucosamine-6-phosphate deaminase using a newly developed sensitive radiometric assay. They characterized biochemically the erythrocyte enzyme and reported data on its kinetics, temperature stability, and chromatographic purification. Weidanz et al. (1995) noted that the nucleotide sequence of the nagB gene, encoding the deaminase in E. coli K12, had been determined (Rogers et al., 1988). Functional analysis by Shevchenko et al. (1998) showed that GNPI had glucosamine-6-phosphate deaminase activity. However, it did not induce calcium oscillations in mammalian eggs.BIOCHEMICAL FEATURES
Arreola et al. (2003) solved the crystal structure of human GNP1 in the presence of an allosteric activator, a competitive inhibitor, ammonia, inorganic sulfate, and a cryoprotectant to 1.75-angstrom resolution. They found that, like E. coli Gnp1, human GNP1 formed a 6-monomer unit. However, each of the 6 GNP1 monomers showed a different conformation for the active-site lid, and all conformations differed from that observed in the E. coli enzyme. Moreover, all human GNP1 monomers differed from E. coli Gnp1 in the phosphate-binding loop.GENE STRUCTURE
Shevchenko et al. (1998) determined that the single-copy GNPI gene contains 8 exons. Nakamura et al. (2000) found that the GNPI gene spans approximately 12.4 kb and contains 8 exons. Arreola et al. (2003) determined that the GNPDA1 gene contains 6 exons.MAPPING
Using FISH, Shevchenko et al. (1998) mapped the GNPI gene to chromosome 5q31. ... 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 601798 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed