Q9D8U8 · SNX5_MOUSE
- ProteinSorting nexin-5
- GeneSnx5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids404 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. 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). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin. Plays a role in the internalization of EGFR after EGF stimulation. Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C and is retromer-independent. Together with PIP5K1C facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation (By similarity).
Plays a role in macropinocytosis (PubMed:18854019).
Plays a role in macropinocytosis (PubMed:18854019).
Features
Showing features for binding site.
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSorting nexin-5
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D8U8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Early endosome membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2) (By similarity).
Detected on macropinosomes (PubMed:18854019).
Targeted to membrane ruffles in response to EGFR stimulation (By similarity).
Detected on macropinosomes (PubMed:18854019).
Targeted to membrane ruffles in response to EGFR stimulation (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000213845 | 2-404 | Sorting nexin-5 | |||
Sequence: AAVPELLEQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLSTFQSPEFSVTRQHEDFVWLHDTLTETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSTHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAETHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN | ||||||
Modified residue | 193 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 275 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Forms heterodimers with BAR domain-containing sorting nexins SNX1 and SNX2; does not homodimerize. The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS), and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. Interacts with SNX1, SNX2, VPS26A, VPS29, VPS35, DCTN1, DOCK1, MIB1, PIP5K1C. Interacts with HGS; increased by PIP5K1C kinase activity and by PtdIns(3P) and/or PtdIns(3,4)P2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9D8U8 | incE P0DJI4 | 4 | EBI-643385, EBI-22303778 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-172 | PX | ||||
Sequence: LNVDPSLQIDIPDALSERDKVKFTVHTKTTLSTFQSPEFSVTRQHEDFVWLHDTLTETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSTHEVFLQRLSSHPVLSKDRNFHVFLEYDQDL | ||||||
Region | 169-261 | Interaction with DOCK1 | ||||
Sequence: DQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTV | ||||||
Region | 183-200 | Membrane-binding amphipathic helix | ||||
Sequence: FGGFFKSVVKSADEVLFS | ||||||
Domain | 202-404 | BAR | ||||
Sequence: VKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAETHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN |
Domain
The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate.
The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of an amphipathic helix (AH) in the membrane (By similarity).
Sequence similarities
Belongs to the sorting nexin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length404
- Mass (Da)46,797
- Last updated2001-06-01 v1
- ChecksumC24D8C78F753FAFC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK007676 EMBL· GenBank· DDBJ | BAB25180.1 EMBL· GenBank· DDBJ | mRNA | ||
AK029463 EMBL· GenBank· DDBJ | BAC26460.1 EMBL· GenBank· DDBJ | mRNA | ||
AK031873 EMBL· GenBank· DDBJ | BAC27587.1 EMBL· GenBank· DDBJ | mRNA | ||
AK049129 EMBL· GenBank· DDBJ | BAC33558.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159904 EMBL· GenBank· DDBJ | BAE35468.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169786 EMBL· GenBank· DDBJ | BAE41365.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002242 EMBL· GenBank· DDBJ | AAH02242.1 EMBL· GenBank· DDBJ | mRNA |