P39929 · SNF7_YEAST
- ProteinVacuolar-sorting protein SNF7
- GeneSNF7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids240 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB) (PubMed:11559748, PubMed:12194857).
The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting (PubMed:12194857).
Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen (PubMed:24139821, PubMed:24711499).
ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery (PubMed:24139821, PubMed:24711499).
SNF7 is the most abundant ESCRT-III subunit which forms membrane-sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface (PubMed:26670543).
Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces (PubMed:26670543).
SNF7 filaments then form spirals that could function as spiral springs (PubMed:26522593).
The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission (PubMed:26522593).
SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles (PubMed:11029042, PubMed:15935782).
ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly (PubMed:25303532).
The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting (PubMed:12194857).
Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen (PubMed:24139821, PubMed:24711499).
ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery (PubMed:24139821, PubMed:24711499).
SNF7 is the most abundant ESCRT-III subunit which forms membrane-sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface (PubMed:26670543).
Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces (PubMed:26670543).
SNF7 filaments then form spirals that could function as spiral springs (PubMed:26522593).
The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission (PubMed:26522593).
SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles (PubMed:11029042, PubMed:15935782).
ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly (PubMed:25303532).
Miscellaneous
Present with 3270 molecules/cell in log phase SD medium.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | ESCRT III complex | |
Cellular Component | multivesicular body | |
Cellular Component | nuclear envelope | |
Cellular Component | plasma membrane | |
Molecular Function | identical protein binding | |
Biological Process | ATP export | |
Biological Process | ESCRT III complex assembly | |
Biological Process | intralumenal vesicle formation | |
Biological Process | late endosome to vacuole transport | |
Biological Process | late endosome to vacuole transport via multivesicular body sorting pathway | |
Biological Process | protein transport | |
Biological Process | reticulophagy | |
Biological Process | ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway | |
Biological Process | vesicle budding from membrane |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameVacuolar-sorting protein SNF7
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP39929
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endosome membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Exhibits defects in the sorting and processing of native vacuolar proteins (PubMed:3062374).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Impairs binding to membrane. | ||||
Sequence: W → E | ||||||
Mutagenesis | 6 | Impairs binding to membrane. | ||||
Sequence: F → E | ||||||
Mutagenesis | 8 | Impairs binding to membrane. | ||||
Sequence: W → E | ||||||
Mutagenesis | 25 | Leads to severe sorting defects; when associated with E-29 and E-36. | ||||
Sequence: R → E | ||||||
Mutagenesis | 29 | Leads to severe sorting defects; when associated with E-25 and E-36. | ||||
Sequence: H → E | ||||||
Mutagenesis | 36 | Leads to severe sorting defects; when associated with E-25 and E-29. | ||||
Sequence: K → E | ||||||
Mutagenesis | 52 | Impairs the formation of protofilaments; when associated with K-90. Also impairs the formation of protofilaments; when associated with E-94. Also impairs the formation of protofilaments; when associated with E-107. Also impairs the formation of protofilaments; when associated with E-114. | ||||
Sequence: R → E | ||||||
Mutagenesis | 83 | Leads to severe sorting defects. | ||||
Sequence: T → E | ||||||
Mutagenesis | 87 | Leads to severe sorting defects. | ||||
Sequence: M → E | ||||||
Mutagenesis | 90 | Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. | ||||
Sequence: Q → K | ||||||
Mutagenesis | 94 | Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. | ||||
Sequence: I → E | ||||||
Mutagenesis | 95 | Leads to severe sorting defects; when associated with K-102 and K-109. | ||||
Sequence: E → K | ||||||
Mutagenesis | 97 | Leads to severe sorting defects. | ||||
Sequence: A → K | ||||||
Mutagenesis | 99 | Leads to severe sorting defects. | ||||
Sequence: L → K | ||||||
Mutagenesis | 101 | Leads to severe sorting defects. | ||||
Sequence: L → E | ||||||
Mutagenesis | 102 | Leads to severe sorting defects; when associated with K-95 and K-109. | ||||
Sequence: E → K | ||||||
Mutagenesis | 103 | Leads to severe sorting defects. | ||||
Sequence: T → E | ||||||
Mutagenesis | 104 | Leads to severe sorting defects. | ||||
Sequence: M → E | ||||||
Mutagenesis | 107 | Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. | ||||
Sequence: M → E | ||||||
Mutagenesis | 109 | Leads to severe sorting defects; when associated with K-95 and K-102. | ||||
Sequence: E → K | ||||||
Mutagenesis | 114 | Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. | ||||
Sequence: M → E | ||||||
Mutagenesis | 117 | Leads to severe sorting defects. | ||||
Sequence: I → E | ||||||
Mutagenesis | 121 | Leads to severe sorting defects. | ||||
Sequence: L → D |
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000211446 | 1-240 | Vacuolar-sorting protein SNF7 | |||
Sequence: MWSSLFGWTSSNAKNKESPTKAIVRLREHINLLSKKQSHLRTQITNQENEARIFLTKGNKVMAKNALKKKKTIEQLLSKVEGTMESMEQQLFSIESANLNLETMRAMQEGAKAMKTIHSGLDIDKVDETMDEIREQVELGDEISDAISRPLITGANEVDEDELDEELDMLAQENANQETSKIVNNNVNAAPISENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL | ||||||
Modified residue | 72 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 119 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 193 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 229 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Core component of the ESCRT-III complex (endosomal sorting required for transport complex III) (PubMed:12194857, PubMed:18854142).
ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24 (PubMed:18854142).
SNF7 polymerizes into spirals at the surface of lipid bilayers (PubMed:26522593).
SNF7 polymerization is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament (PubMed:24058170, PubMed:24711499).
Interacts with VTA1; the interaction requires DID2 (PubMed:16601096, PubMed:24058170).
Interacts with BRO1 (PubMed:15086794, PubMed:15935782, PubMed:24058170).
Interacts with DOA4 (PubMed:26427873).
Interacts with HEH1 and HEH2 (PubMed:25303532).
Interacts with RIM20 and YGR122W (PubMed:24058170).
ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24 (PubMed:18854142).
SNF7 polymerizes into spirals at the surface of lipid bilayers (PubMed:26522593).
SNF7 polymerization is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament (PubMed:24058170, PubMed:24711499).
Interacts with VTA1; the interaction requires DID2 (PubMed:16601096, PubMed:24058170).
Interacts with BRO1 (PubMed:15086794, PubMed:15935782, PubMed:24058170).
Interacts with DOA4 (PubMed:26427873).
Interacts with HEH1 and HEH2 (PubMed:25303532).
Interacts with RIM20 and YGR122W (PubMed:24058170).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39929 | BRO1 P48582 | 4 | EBI-17554, EBI-3768 | |
BINARY | P39929 | DID2 P69771 | 3 | EBI-17554, EBI-2053489 | |
BINARY | P39929 | DID4 P36108 | 5 | EBI-17554, EBI-26574 | |
BINARY | P39929 | HEH2 Q03281 | 3 | EBI-17554, EBI-22131 | |
BINARY | P39929 | SNF7 P39929 | 9 | EBI-17554, EBI-17554 | |
BINARY | P39929 | VPS20 Q04272 | 5 | EBI-17554, EBI-28157 | |
BINARY | P39929 | VPS24 P36095 | 3 | EBI-17554, EBI-26653 | |
BINARY | P39929 | VPS4 P52917 | 3 | EBI-17554, EBI-20475 | |
BINARY | P39929 | VPS60 Q03390 | 3 | EBI-17554, EBI-2090142 | |
BINARY | P39929 | VTA1 Q06263 | 2 | EBI-17554, EBI-37098 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 193-210 | Polar residues | ||||
Sequence: SENKVSLPSVPSNKIKQS | ||||||
Region | 193-240 | Disordered | ||||
Sequence: SENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL | ||||||
Compositional bias | 216-230 | Acidic residues | ||||
Sequence: DGEEEEDEEDEDEKA |
Domain
The N-terminus (residues 1 to 11) forms an amphipathic helix which is required for the association to membrane.
Sequence similarities
Belongs to the SNF7 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length240
- Mass (Da)26,987
- Last updated1995-02-01 v1
- Checksum5241A18BB181F0C1
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 173 | in Ref. 4; AAS56528 | ||||
Sequence: E → G | ||||||
Compositional bias | 193-210 | Polar residues | ||||
Sequence: SENKVSLPSVPSNKIKQS | ||||||
Compositional bias | 216-230 | Acidic residues | ||||
Sequence: DGEEEEDEEDEDEKA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L09751 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z73197 EMBL· GenBank· DDBJ | CAA97548.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY558202 EMBL· GenBank· DDBJ | AAS56528.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09343.1 EMBL· GenBank· DDBJ | Genomic DNA |