P39968 · VAC8_YEAST
- ProteinVacuolar protein 8
- GeneVAC8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids578 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole (cvt) (PubMed:9490720).
Involved in the formation of nucleus-vacuole junctions (NVJs) during piecemeal microautophagy of the nucleus (PMN) (PubMed:10888680, PubMed:12529432, PubMed:16912077).
NVJs are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane (PubMed:10888680, PubMed:12529432, PubMed:16912077).
Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process (PubMed:10888680, PubMed:12529432, PubMed:16912077).
Involved in the formation of nucleus-vacuole junctions (NVJs) during piecemeal microautophagy of the nucleus (PMN) (PubMed:10888680, PubMed:12529432, PubMed:16912077).
NVJs are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane (PubMed:10888680, PubMed:12529432, PubMed:16912077).
Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process (PubMed:10888680, PubMed:12529432, PubMed:16912077).
Miscellaneous
Present with 5680 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameVacuolar protein 8
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP39968
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Lipid-anchor
Note: Localizes at sites of nucleus-vacuole junctions.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 4-7 | In VAC8-3; not palmitoylated. | ||||
Sequence: CCSC → GTSS | ||||||
Mutagenesis | 51 | Fails to undergo self-association in the presence of NVJ1 or ATG13. | ||||
Sequence: A → R | ||||||
Mutagenesis | 60 | Fails to support the Cvt pathway, but does not affect the PMN pathway; when associated with R-62. | ||||
Sequence: N → R | ||||||
Mutagenesis | 62 | Does not affect self-association in the presence of NVJ1 but fails to undergo self-association in the presence of ATG13. Fails to support the cvt pathway, but does not affect the PMN pathway; when associated with R-60. | ||||
Sequence: N → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000064302 | 2-578 | Vacuolar protein 8 | |||
Sequence: GSCCSCLKDSSDEASVSPIADNEREAVTLLLGYLEDKDQLDFYSGGPLKALTTLVYSDNLNLQRSAALAFAEITEKYVRQVSREVLEPILILLQSQDPQIQVAACAALGNLAVNNENKLLIVEMGGLEPLINQMMGDNVEVQCNAVGCITNLATRDDNKHKIATSGALIPLTKLAKSKHIRVQRNATGALLNMTHSEENRKELVNAGAVPVLVSLLSSTDPDVQYYCTTALSNIAVDEANRKKLAQTEPRLVSKLVSLMDSPSSRVKCQATLALRNLASDTSYQLEIVRAGGLPHLVKLIQSDSIPLVLASVACIRNISIHPLNEGLIVDAGFLKPLVRLLDYKDSEEIQCHAVSTLRNLAASSEKNRKEFFESGAVEKCKELALDSPVSVQSEISACFAILALADVSKLDLLEANILDALIPMTFSQNQEVSGNAAAALANLCSRVNNYTKIIEAWDRPNEGIRGFLIRFLKSDYATFEHIALWTILQLLESHNDKVEDLVKNDDDIINGVRKMADVTFERLQRSGIDVKNPGSNNNPSSNDNNSNNNDTGSEHQPVEDASLELYNITQQILQFLH | ||||||
Lipidation | 4 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 5 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 7 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 11 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 16 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 77 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 515 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Palmitoylated on one or more of its N-terminal cysteine residues by PFA3, which is required for vacuole fusion.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with NVJ1 (PubMed:10888680, PubMed:16912077, PubMed:28533415).
Forms heterotetramers of two VAC8 and two NVJ1 or two VAC8 and two ATG13 (PubMed:31512555).
Forms heterotetramers of two VAC8 and two NVJ1 or two VAC8 and two ATG13 (PubMed:31512555).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39968 | ATG13 Q06628 | 7 | EBI-20212, EBI-36188 | |
BINARY | P39968 | NVJ1 P38881 | 10 | EBI-20212, EBI-24885 | |
BINARY | P39968 | VAB2 P40003 | 3 | EBI-20212, EBI-22275 | |
BINARY | P39968 | VAC17 P25591 | 3 | EBI-20212, EBI-21800 | |
BINARY | P39968 | VAC8 P39968 | 2 | EBI-20212, EBI-20212 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 37-75 | ARM 1 | ||||
Sequence: DKDQLDFYSGGPLKALTTLVYSDNLNLQRSAALAFAEIT | ||||||
Repeat | 76-114 | ARM 2 | ||||
Sequence: EKYVRQVSREVLEPILILLQSQDPQIQVAACAALGNLAV | ||||||
Repeat | 116-155 | ARM 3 | ||||
Sequence: NENKLLIVEMGGLEPLINQMMGDNVEVQCNAVGCITNLAT | ||||||
Repeat | 157-196 | ARM 4 | ||||
Sequence: DDNKHKIATSGALIPLTKLAKSKHIRVQRNATGALLNMTH | ||||||
Repeat | 198-237 | ARM 5 | ||||
Sequence: EENRKELVNAGAVPVLVSLLSSTDPDVQYYCTTALSNIAV | ||||||
Repeat | 239-280 | ARM 6 | ||||
Sequence: EANRKKLAQTEPRLVSKLVSLMDSPSSRVKCQATLALRNLAS | ||||||
Repeat | 282-321 | ARM 7 | ||||
Sequence: TSYQLEIVRAGGLPHLVKLIQSDSIPLVLASVACIRNISI | ||||||
Repeat | 323-363 | ARM 8 | ||||
Sequence: PLNEGLIVDAGFLKPLVRLLDYKDSEEIQCHAVSTLRNLAA | ||||||
Repeat | 407-446 | ARM 9 | ||||
Sequence: DVSKLDLLEANILDALIPMTFSQNQEVSGNAAAALANLCS | ||||||
Region | 527-557 | Disordered | ||||
Sequence: SGIDVKNPGSNNNPSSNDNNSNNNDTGSEHQ | ||||||
Compositional bias | 530-557 | Polar residues | ||||
Sequence: DVKNPGSNNNPSSNDNNSNNNDTGSEHQ |
Domain
Comprises a flexibly connected N-terminal H1 helix followed by armadillo repeats (ARMs) that form a right-handed superhelical structure.
the H1 helix directly interacts with ARM1 and hinders the dimeric interface (PubMed:28533415, PubMed:31512555).
ARM1 serves as a binding interface for the formation of the 2-fold dimer of VAC8, which is crucial for heterotetramer formation with either NVJ1 or ATG13 and subsequent PMN and Cvt pathways (PubMed:28533415, PubMed:31512555).
ARM1 serves as a binding interface for the formation of the 2-fold dimer of VAC8, which is crucial for heterotetramer formation with either NVJ1 or ATG13 and subsequent PMN and Cvt pathways (PubMed:28533415, PubMed:31512555).
The highly conserved innergroove formed by the ARMs specifically binds the extended 80 Angstroms-longloop of NVJ1 (PubMed:28533415).
The ARMs domain also binds the he 70 Angstroms extended loop of ATG13 in an antiparallel manner (PubMed:31512555).
The ARMs domain also binds the he 70 Angstroms extended loop of ATG13 in an antiparallel manner (PubMed:31512555).
Sequence similarities
Belongs to the beta-catenin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length578
- Mass (Da)63,208
- Last updated2007-01-23 v3
- ChecksumB2E75774B47E5933
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 530-557 | Polar residues | ||||
Sequence: DVKNPGSNNNPSSNDNNSNNNDTGSEHQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF005267 EMBL· GenBank· DDBJ | AAQ13402.1 EMBL· GenBank· DDBJ | mRNA | ||
U18530 EMBL· GenBank· DDBJ | AAB64490.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006939 EMBL· GenBank· DDBJ | DAA07640.1 EMBL· GenBank· DDBJ | Genomic DNA |