| IED ID |
IndEnz0002001739 |
| Enzyme Type ID |
protease001739 |
| Protein Name |
Sorting nexin-1
|
| Gene Name |
SNX1 |
| Organism |
Homo sapiens (Human) |
| 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
Primates
Haplorrhini
Simiiformes
Catarrhini
Hominoidea (apes)
Hominidae (great apes)
Homininae
Homo
Homo sapiens (Human)
|
| Enzyme Sequence |
MASGGGGCSASERLPPPFPGLEPESEGAAGGSEPEAGDSDTEGEDIFTGAAVVSKHQSPKITTSLLPINNGSKENGIHEEQDQEPQDLFADATVELSLDSTQNNQKKVLAKTLISLPPQEATNSSKPQPTYEELEEEEQEDQFDLTVGITDPEKIGDGMNAYVAYKVTTQTSLPLFRSKQFAVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKVGKEDSSSAEFLEKRRAALERYLQRIVNHPTMLQDPDVREFLEKEELPRAVGTQTLSGAGLLKMFNKATDAVSKMTIKMNESDIWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTAQFAKSLAMLGSSEDNTALSRALSQLAEVEEKIEQLHQEQANNDFFLLAELLSDYIRLLAIVRAAFDQRMKTWQRWQDAQATLQKKREAEARLLWANKPDKLQQAKDEILEWESRVTQYERDFERISTVVRKEVIRFEKEKSKDFKNHVIKYLETLLYSQQQLAKYWEAFLPEAKAIS |
| Enzyme Length |
522 |
| Uniprot Accession Number |
Q13596 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
BINDING 186; /note=Phosphatidylinositol 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q96L94; BINDING 188; /note=Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q96L94; BINDING 214; /note=Phosphatidylinositol 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q96L94; BINDING 238; /note=Phosphatidylinositol 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q96L94 |
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:12198132). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:19816406, PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1) and Shiginella dysenteria toxin stxB. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi (PubMed:12198132, PubMed:15498486, PubMed:17550970, PubMed:17101778, PubMed:18088323, PubMed:21040701). Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R (PubMed:16407403, PubMed:20070609). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (PubMed:23152498). {ECO:0000269|PubMed:12198132, ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:17550970, ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:19816406, ECO:0000269|PubMed:20070609, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:23152498, ECO:0000303|PubMed:15498486}. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Alternative sequence (2); Beta strand (4); Binding site (4); Chain (1); Compositional bias (2); Domain (2); Helix (9); Modified residue (9); Mutagenesis (5); Natural variant (2); Region (3); Sequence conflict (4); Turn (2) |
| Keywords |
3D-structure;Acetylation;Alternative splicing;Cell projection;Endosome;Golgi apparatus;Lipid-binding;Membrane;Phosphoprotein;Protein transport;Reference proteome;Transport |
| Interact With |
Q6RW13; Q15041; Q5T9G4-2; P07510-2; Q8IZR5-2; Q96DZ9; Q96DZ9-2; Q9NZJ6; B3EWG5; Q9Y680; Q8IVP5; P53701; Q9H400; O95563; O60664; Q9UI14; Q00765; Q96HR9; Q96HR9-2; Q6ZWK4; O95197; Q9NQC3; O00560; Q8N3Y7; Q8WV19; Q9Y371; Itself; O60749; Q86XE0; Q9Y5X3; Q9UNH7; O43759-2; P08247; Q8WW34-2; Q96QK1; Q12768 |
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:22431521}; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium {ECO:0000269|PubMed:20604901}. Note=Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:15498486). Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles (PubMed:18088323). Colocalizes with DNAJC13 and Shiginella dysenteria toxin stxB on early endosomes (PubMed:19874558). Colocalized with F-actin at the leading edge of lamellipodia in a KALRN-dependent manner (PubMed:20604901). {ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:20604901}. |
| Modified Residue |
MOD_RES 32; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"; MOD_RES 39; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"; MOD_RES 41; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q9WV80"; MOD_RES 48; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9WV80"; MOD_RES 72; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 188; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 237; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 280; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" |
| Post Translational Modification |
|
| Signal Peptide |
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| Structure 3D |
NMR spectroscopy (1); X-ray crystallography (1) |
| Cross Reference PDB |
2I4K;
4FZS;
|
| Mapped Pubmed ID |
19367725;
20711500;
21516116;
21900206;
21988832;
23416715;
25416956;
25609649;
|
| Motif |
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| Gene Encoded By |
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| Mass |
59,070 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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