Lysophospholipase D GDPD1 (GDPD1)
The protein contains 314 amino acids for an estimated molecular weight of 36167 Da.
Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:27637550, PubMed:25596343). Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC) (PubMed:27637550, PubMed:25596343). May be involved in bioactive N-acylethanolamine biosynthesis from both N-acyl-lysoplasmenylethanolamin (N-acyl-lysoPlsEt) and N-acyl-lysophosphatidylethanolamin (N-acyl-lysoPE) (PubMed:27637550, PubMed:25596343). In addition, hydrolyzes glycerophospho-N-acylethanolamine to N-acylethanolamine (PubMed:27637550). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (By similarity). (updated: Aug. 12, 2020)
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.
This protein is predicted to be membranous by TOPCONS.
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Biological Process
Glycerophospholipid catabolic process
N-acylethanolamine metabolic process
Phospholipid metabolic process
The reference OMIM entry for this protein is 616317
Glycerophosphodiester phosphodiesterase domain-containing protein 1; gdpd1
Glycerophosphodiester phosphodiesterase 4; gde4
DESCRIPTION
GDPD1 appears to have lysophospholipase activity (EC 3.1.1.5), but not phosphodiesterase activity (Ohshima et al., 2015).CLONING
By sequencing clones obtained from a human fetal brain cDNA library, Wu et al. (2003) isolated a splice variant of GDPD1, which they called GDPD1v1. The deduced 289-amino acid protein has a short N-terminal tail, followed by a transmembrane domain, a large GDPD domain, and a C-terminal tail. Database analysis revealed 2 additional splice variants encoding proteins of 290 and 314 amino acids. RT-PCR analysis of 16 human tissues detected GDPD1v1 expression predominantly in ovary and small intestine. Database analysis suggested tissue-specific expression of the other splice variants. Ohshima et al. (2015) cloned mouse Gdpd1, which they called Gde4. The deduced 314-amino acid protein has a central GDE domain flanked by N- and C-terminal transmembrane regions. Mouse and human GDE4 share 92% amino acid homology. RT-PCR detected variable Gde4 expression in most of 20 mouse tissues examined, with highest expression in testis, followed by colon, intestine, and several brain regions. Little to no expression was detected in pancreas, olfactory bulb, and bone. Fluorescence-tagged Gde4 was expressed in the perinuclear region of transfected COS-7 cells.GENE FUNCTION
Following its expression and purification from insect cells, Ohshima et al. (2015) found that mouse Gde4 showed lysophospholipase activity toward several lysophospholipids, with highest activity against lyso-platelet-activating factor (lysoPAF; 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a proinflammatory phospholipid synthesized by macrophages. Gde4 also showed activity against lysophosphatidylcholine, and much lower activity against lysophosphatidylinositol, lysophosphatidylethanolamine, and lysophosphatidylserine. Gde4 did not show phosphodiesterase activity against any substrate examined. Expression of Gde4 mRNA was upregulated in RAW264-7 mouse macrophages following treatment with lipopolysaccharide. Gde4 protein was elevated in macrophages in white adipose tissue of db/db obese mice and in the stromal-vascular fraction from white adipose tissue in high-fat diet-induced obese mice, suggesting that Gde4 is upregulated with macrophage infiltration into adipose tissue.GENE STRUCTURE
Wu et al. (2003) determined that the GDPD1 gene contains 11 exons and spans more than 55 kb.MAPPING
By genomic sequence analysis, Wu et al. (2003) mapped the GDPD1 gene to chromosome 17q23.2. ... 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 616317 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).