| Tissue Specificity | Widely expressed. In the brain, high levels of expression are detected in the frontal, temporal and occipital cortices and hippocampus. Expressed at low level in corpus callosum. |
| Post Translational Modifications | N-glycosylated. Proteolytically processed to a soluble form that is stable within endosomes and lysosomes. During transport through the secretory pathway becomes proteolysed by cysteine proteases, thereby releasing a stable soluble lysosomal lumenal polypeptide, whereas the transmembrane-bound fragment is rapidly degraded. Its transport route to lysosomes involves ubiquitination and the ESCRT complex. Ubiquitinated at N-terminus. Ubiquitination mediates sorting into lysosomes. |
| Function | 5'->3' DNA exonuclease which digests single-stranded DNA (ssDNA). Regulates inflammatory cytokine responses via the degradation of nucleic acids, by reducing the concentration of ssDNA able to stimulate TLR9, a nucleotide-sensing receptor in collaboration with PLD4. May be important in myotube formation. Plays a role in lysosomal homeostasis. Involved in the regulation of endosomal protein sorting. |
| Protein Name | 5'-3' Exonuclease Pld3Choline Phosphatase 3Hindiii K4l HomologHu-K4Phosphatidylcholine-Hydrolyzing Phospholipase D3Phospholipase D3Pld 3 |
| Database Links | Reactome: R-HSA-1483148Reactome: R-HSA-2029485 |
| Cellular Localisation | Endoplasmic Reticulum MembraneSingle-Pass Type Ii Membrane ProteinLysosome LumenEarly Endosome MembraneLate Endosome MembraneGolgi Apparatus MembraneEndosome MembraneLocalizes To Er-Associated Vesicles In Differentiating MyotubesThe Soluble Form In Lysosome Arises By Proteolytic Processing Of The Membrane-Bound FormColocalizes With App In Endosomes |
| Alternative Antibody Names | Anti-5'-3' Exonuclease Pld3 antibodyAnti-Choline Phosphatase 3 antibodyAnti-Hindiii K4l Homolog antibodyAnti-Hu-K4 antibodyAnti-Phosphatidylcholine-Hydrolyzing Phospholipase D3 antibodyAnti-Phospholipase D3 antibodyAnti-Pld 3 antibodyAnti-PLD3 antibody |
Information sourced from Uniprot.org
