| Function | Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G. Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes. Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor TFRC presumably by delivering the transferrin:transferrin receptor complex to recycling endosomes.the function may involve the CSC retromer subcomplex. In the case of Salmonella enterica infection plays arole in maturation of the Salmonella-containing vacuole (SCV) and promotes recruitment of LAMP1 to SCVs. |
| Protein Name | Sorting Nexin-3Protein Sdp3 |
| Database Links | Reactome: R-HSA-3238698Reactome: R-HSA-5689880 |
| Cellular Localisation | Early EndosomeCytoplasmic VesiclePhagosomeColocalizes To Clathrin-Coated Endosomal Vesicles Morphologically Distinct From Retromer-Decorated Non-Branched Endosomal Tubule Structures Colocalizes With Eea1 On Nascent Phagosomes In Dendritic Cells But Competes With Eea1 For Binding To Phagosomal MembraneIn The Case Of Salmonella Enterica Infection Localizes To Salmonella-Containing Vacuoles (Scvs) From Which Snx3-Containing Tubules Form 30-60 Minutes After Infection |
| Alternative Protein Names | Sorting Nexin-3 proteinProtein Sdp3 proteinSNX3 protein |
Information sourced from Uniprot.org
