| IED ID | IndEnz0002008623 |
| Enzyme Type ID | protease008623 |
| Protein Name |
Sorting nexin-3 SDP3 protein |
| Gene Name | Snx3 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRHVPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA |
| Enzyme Length | 162 |
| Uniprot Accession Number | O70492 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 70; /note=Phosphatidylinositol 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q96L94; BINDING 72; /note=Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q96L94; BINDING 95; /note=Phosphatidylinositol 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q96L94; BINDING 118; /note=Phosphatidylinositol 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q96L94 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Also can bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (PubMed:19576982). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC). May act in part as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (By similarity). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (PubMed:18632802). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (By similarity). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor Tfrc presuambly by delivering the transferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (PubMed:23416069). Involved in regulation of neurite outgrowth in primary neurons (PubMed:19576982). {ECO:0000250|UniProtKB:O60493, ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:23416069}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (4); Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (3); Mutagenesis (4); Region (1) |
| Keywords | Acetylation;Cytoplasmic vesicle;Endosome;Isopeptide bond;Lipid-binding;Methylation;Phosphoprotein;Protein transport;Reference proteome;Transport;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:23416069}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:O60493}. Note=Colocalizes 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 membrane (By similarity). {ECO:0000250|UniProtKB:O60493, ECO:0000269|PubMed:23416069}. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:O60493; MOD_RES 43; /note=Omega-N-methylarginine; /evidence=ECO:0007744|PubMed:24129315; MOD_RES 72; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O60493 |
| Post Translational Modification | PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10. {ECO:0000269|PubMed:18632802}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 11707774; 12079282; 12466851; 12520002; 12627228; 14610273; 15215310; 16141072; 16214895; 16615898; 17967808; 18799693; 20817026; 21267068; 23237080; 24194600; 26045162; 33214242; |
| Motif | |
| Gene Encoded By | |
| Mass | 18,757 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |