P32939 · YPT7_YEAST
- ProteinYpt/Rab-type GTPase YPT7
- GeneYPT7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids208 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (Probable). Involved in regulation of vesicular protein transport in exo- and endocytosis (PubMed:8308065).
Involved in regulation of late endosome to vacuole trafficking and homotypic vacuole fusion, by interacting in its GTP-bound state on the donor membrane with the large multiprotein HOPS/class C-Vps tethering complex on the acceptor membrane (PubMed:10725336, PubMed:10944212, PubMed:11062257, PubMed:11118206, PubMed:11210571, PubMed:11590240, PubMed:19386605, PubMed:21062894, PubMed:7489715, PubMed:8308065).
Involved in retromer assembly and cargo export, recognizing the cargo selection complex (CSC). GTP-bound YPT7 recruits CSC to vacuolar membranes via retromer subunit VPS35 (PubMed:22593205).
Interacts with the HOPS complex subunit VPS39 independent of the HOPS complex at mitochondria-vacuole contact sites (vCLAMPs), providing a physical and metabolic interconnection between the endocytic pathway and mitochondria (PubMed:25026035).
Involved in regulation of late endosome to vacuole trafficking and homotypic vacuole fusion, by interacting in its GTP-bound state on the donor membrane with the large multiprotein HOPS/class C-Vps tethering complex on the acceptor membrane (PubMed:10725336, PubMed:10944212, PubMed:11062257, PubMed:11118206, PubMed:11210571, PubMed:11590240, PubMed:19386605, PubMed:21062894, PubMed:7489715, PubMed:8308065).
Involved in retromer assembly and cargo export, recognizing the cargo selection complex (CSC). GTP-bound YPT7 recruits CSC to vacuolar membranes via retromer subunit VPS35 (PubMed:22593205).
Interacts with the HOPS complex subunit VPS39 independent of the HOPS complex at mitochondria-vacuole contact sites (vCLAMPs), providing a physical and metabolic interconnection between the endocytic pathway and mitochondria (PubMed:25026035).
Miscellaneous
Present with 5530 molecules/cell in log phase SD medium.
Activity regulation
Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). YPT7 is activated by GEFs MON1-CCZ1 complex (MC1) and VAM6/VPS39, and inactivated by GAPs GYP7 and GYP1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17-23 | GTP (UniProtKB | ChEBI) | ||||
Sequence: SGVGKTS | ||||||
Binding site | 33-40 | GTP (UniProtKB | ChEBI) | ||||
Sequence: YSQQYKAT | ||||||
Binding site | 67 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 126-129 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKID | ||||||
Binding site | 158-160 | GTP (UniProtKB | ChEBI) | ||||
Sequence: SAK |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | fungal-type vacuole | |
Cellular Component | fungal-type vacuole membrane | |
Cellular Component | late endosome | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Cellular Component | multivesicular body | |
Cellular Component | vacuole | |
Cellular Component | vacuole-mitochondrion membrane contact site | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | protein-containing complex binding | |
Biological Process | cytoplasm to vacuole targeting by the Cvt pathway | |
Biological Process | endocytosis | |
Biological Process | macroautophagy | |
Biological Process | piecemeal microautophagy of the nucleus | |
Biological Process | protein localization to vacuole | |
Biological Process | regulation of protein-containing complex assembly | |
Biological Process | regulation of vacuole fusion, non-autophagic | |
Biological Process | retrograde transport, endosome to Golgi | |
Biological Process | vacuole inheritance | |
Biological Process | vesicle-mediated transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameYpt/Rab-type GTPase YPT7
- Short namesYpt7p
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32939
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Lipid-anchor
Note: Localizes to sites of contact between the vacuole and mitochondria (vCLAMPs). Vacuolar membrane localization requires the action of small GTPase Rab5 homologs such as YPT52, YPT10 or VPS21 (PubMed:32391792).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Endocytosed alpha-factor accumulates in late endosomes.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 22 | Constitutively in the GDP-bound conformation. Causes loss of function during vacuolar morphogenesis. Does not suppress the zinc, caffeine and calcium sensitivity of CCZ1 mutants. | ||||
Sequence: T → N | ||||||
Mutagenesis | 68 | GTP-bound stabilized constitutively active mutant. Complements the fragmented vacuolar morphology of YPT7 null mutant cells. Does not suppress the zinc, caffeine and calcium sensitivity of CCZ1 mutants. | ||||
Sequence: Q → L | ||||||
Mutagenesis | 127 | Reduced nucleotide affinity leading to increased turnover between GDP- and GTP-bound states without the need of a guanine nucleotide-exchange factor. Suppresses the zinc, caffeine and calcium sensitivity of CCZ1 mutants. | ||||
Sequence: K → E | ||||||
Mutagenesis | 129 | Reduced nucleotide affinity leading to increased turnover between GDP- and GTP-bound states without the need of a guanine nucleotide-exchange factor. Suppresses the zinc, caffeine and calcium sensitivity of CCZ1 mutants. | ||||
Sequence: D → G, N, or A | ||||||
Mutagenesis | 157 | Reduced nucleotide affinity leading to increased turnover between GDP- and GTP-bound states without the need of a guanine nucleotide-exchange factor. Suppresses the zinc, caffeine and calcium sensitivity of CCZ1 mutants. | ||||
Sequence: T → P | ||||||
Mutagenesis | 159 | Reduced nucleotide affinity leading to increased turnover between GDP- and GTP-bound states without the need of a guanine nucleotide-exchange factor. Suppresses the zinc, caffeine and calcium sensitivity of CCZ1 mutants. | ||||
Sequence: A → P |
PTM/Processing
Features
Showing features for chain, cross-link, lipidation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000121320 | 1-208 | Ypt/Rab-type GTPase YPT7 | |||
Sequence: MSSRKKNILKVIILGDSGVGKTSLMHRYVNDKYSQQYKATIGADFLTKEVTVDGDKVATMQVWDTAGQERFQSLGVAFYRGADCCVLVYDVTNASSFENIKSWRDEFLVHANVNSPETFPFVILGNKIDAEESKKIVSEKSAQELAKSLGDIPLFLTSAKNAINVDTAFEEIARSALQQNQADTEAFEDDYNDAINIRLDGENNSCSC | ||||||
Cross-link | 147 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Lipidation | 206 | S-geranylgeranyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 208 | Cysteine methyl ester | ||||
Sequence: C | ||||||
Lipidation | 208 | S-geranylgeranyl cysteine | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with IVY1 (PubMed:12553664).
Interacts with YIF1, YIP4 and YIP5 (PubMed:11943201).
Interacts with the HOPS complex (PubMed:10944212, PubMed:19386605).
Interacts with the class C-Vps complex (PubMed:11062257).
Interacts with VPS35 (PubMed:22593205).
Interacts with VPS39 (PubMed:25026035).
Interacts with the GDP dissociation inhibitor GDI1 (PubMed:11118206, PubMed:11785952).
Interacts with CCZ1 (PubMed:11590240).
Interacts with YIF1, YIP4 and YIP5 (PubMed:11943201).
Interacts with the HOPS complex (PubMed:10944212, PubMed:19386605).
Interacts with the class C-Vps complex (PubMed:11062257).
Interacts with VPS35 (PubMed:22593205).
Interacts with VPS39 (PubMed:25026035).
Interacts with the GDP dissociation inhibitor GDI1 (PubMed:11118206, PubMed:11785952).
Interacts with CCZ1 (PubMed:11590240).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P32939 | GDI1 P39958 | 4 | EBI-29509, EBI-7517 | |
BINARY | P32939 | IVY1 Q04934 | 3 | EBI-29509, EBI-35255 | |
BINARY | P32939 | YIF1 P53845 | 2 | EBI-29509, EBI-28230 | |
BINARY | P32939 | YIP4 P53093 | 2 | EBI-29509, EBI-24124 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 37-45 | Effector region | ||||
Sequence: YKATIGADF |
Sequence similarities
Belongs to the small GTPase superfamily. Rab family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length208
- Mass (Da)23,043
- Last updated1993-10-01 v1
- Checksum0E2B72BDA7F7CEE5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X68144 EMBL· GenBank· DDBJ | CAA48244.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D64114 EMBL· GenBank· DDBJ | BAA10973.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z48613 EMBL· GenBank· DDBJ | CAA88515.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA09898.1 EMBL· GenBank· DDBJ | Genomic DNA |