GPLD1

Phosphatidylinositol-glycan-specific phospholipase D is an enzyme that in humans is encoded by the GPLD1 gene.^[5][6]

AliasesGPLD1, GPIPLD, GPIPLDM, PIGPLD, PIPLD, glycosylphosphatidylinositol specific phospholipase D1

External IDsOMIM: 602515; MGI: 106604; HomoloGene: 1152; GeneCards: GPLD1; OMA:GPLD1 - orthologs

Chr.Chromosome 6 (human)^[1]

End24,495,205 bp^[1]

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GPLD1
Identifiers
Aliases	GPLD1, GPIPLD, GPIPLDM, PIGPLD, PIPLD, glycosylphosphatidylinositol specific phospholipase D1
External IDs	OMIM: 602515; MGI: 106604; HomoloGene: 1152; GeneCards: GPLD1; OMA:GPLD1 - orthologs
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p22.3 Start 24,424,565 bp[1] End 24,495,205 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13 A3.1|13 10.79 cM Start 25,127,135 bp[2] End 25,176,484 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte human penis liver buccal mucosa cell right lobe of liver right hemisphere of cerebellum skin of thigh testicle gonad Descending thoracic aorta Top expressed in left lobe of liver utricle dorsal tegmental nucleus dorsomedial hypothalamic nucleus transitional epithelium of urinary bladder mammillary body arcuate nucleus paraventricular nucleus of hypothalamus esophagus lumbar subsegment of spinal cord More reference expression data BioGPS More reference expression data
Gene ontology Molecular function sodium channel regulator activity phospholipase D activity glycosylphosphatidylinositol phospholipase D activity hydrolase activity Cellular component cytoplasm intracellular membrane-bounded organelle intracellular anatomical structure lysosomal membrane extracellular exosome extracellular region extracellular space extracellular matrix Biological process cellular response to calcium ion insulin receptor signaling pathway positive regulation of triglyceride biosynthetic process positive regulation of high-density lipoprotein particle clearance chondrocyte differentiation ossification cellular response to triglyceride hematopoietic stem cell migration to bone marrow positive regulation of membrane protein ectodomain proteolysis positive regulation of glucose metabolic process hematopoietic stem cell migration response to glucose cellular response to cholesterol cell migration involved in sprouting angiogenesis transepithelial transport positive regulation of endothelial cell migration GPI anchor release positive regulation of cytolysis cellular response to pH positive regulation of secretion regulation of cellular response to insulin stimulus positive regulation of alkaline phosphatase activity cellular response to insulin stimulus complement receptor mediated signaling pathway positive regulation of apoptotic process positive regulation of insulin secretion involved in cellular response to glucose stimulus negative regulation of triglyceride catabolic process phosphatidylcholine metabolic process negative regulation of cell population proliferation C-terminal protein lipidation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2822 14756 Ensembl ENSG00000112293 ENSMUSG00000021340 UniProt P80108 O70362 RefSeq (mRNA) NM_001503 NM_177483 NM_008156 RefSeq (protein) NP_001494 n/a Location (UCSC) Chr 6: 24.42 – 24.5 Mb Chr 13: 25.13 – 25.18 Mb PubMed search [3] [4]
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Many proteins are tethered to the extracellular face of eukaryotic plasma membranes by a glycosylphosphatidylinositol (GPI) anchor. The GPI-anchor is a glycolipid found on many blood cells. The protein encoded by the GPLD1 gene is a GPI degrading enzyme that hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, thereby releasing the attached protein from the plasma membrane.^[6]

Plasma concentrations of Gpld1 in mice were found to increase after exercise and to correlate with improved cognitive function, and concentrations of GPLD1 in blood were increased in active elderly humans.^[7][8]