Glycerophosphodiester phosphodiesterase 1 (GDE1)
The protein contains 331 amino acids for an estimated molecular weight of 37718 Da.
Hydrolyzes the phosphodiester bond of glycerophosphodiesters such as glycerophosphoinositol (GroPIns) and glycerophosphoethanolamine (GroPEth), to yield a glycerol phosphate and an alcohol (By similarity). Hydrolyzes glycerophospho-N-acylethanolamines to N-acylethanolamines in the brain and partipates to bioactive N-acylethanolamines biosynthesis such as anandamide (an endocannabinoid), N-palmitoylethanolamine (an anti-inflammatory), and N-oleoylethanolamine (an anorexic). In addition, has a lysophospholipase D activity by hydrolyzing N-acyl-lysoplasmenylethanolamine (N-acyl-lysoPlsEt) to N-acylethanolamine. However lysophospholipase D activity is lower than glycerophosphodiester phosphodiesterase activity (By similarity). Has little or no activity towards glycerophosphocholine (By similarity). (updated: Aug. 12, 2020)
Protein identification was indicated in the following studies:
- 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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs2072086 | |
| dbSNP:rs34137361 |
The reference OMIM entry for this protein is 605943
Glycerophosphodiester phosphodiesterase 1; gde1
Membrane interacting protein of rgs16; mir16
Rgs16-interacting membrane protein
CLONING
Using a yeast 2-hybrid screen to identify proteins that interact with RGS16 (602514), Zheng et al. (2000) isolated a cDNA encoding rat Mir16. By searching sequence databases with rat Mir16 as the probe, they identified a cDNA encoding human MIR16 that had been reported by Loftus et al. (1999) as part of a large-scale chromosome 16 sequencing effort. The human MIR16 protein shares 94% amino acid similarity with rat MIR16 and also shares strong homology with bacterial glycerophosphodiester phosphodiesterases. Northern blot analysis detected widespread expression of a 1.8-kb Mir16 transcript in rat tissues, with highest levels in heart, brain, liver, kidney, and testis. Similar expression was observed for human and mouse MIR16. Using yeast 2-hybrid and GST pull-down assays, Zheng et al. (2000) demonstrated that MIR16 interacts with the RGS domain of RGS16 and weakly with other RGS proteins, including RGS2 (600861). Membrane association assays and endoglycosidase H digestion showed that MIR16 is an integral membrane glycoprotein. Immunofluorescence and immunoelectron microscopy localized Mir16 in the intracellular membranes in rat pituitary and on the plasma membrane in rat liver and kidney.MAPPING
By genomic sequence analysis, Loftus et al. (1999) mapped the GDE1 gene to chromosome 16p. ... More on the omim web site
Aug. 24, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 605943 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).