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Protein

Vacuolar protein 8

Gene

VAC8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.1 Publication

GO - Molecular functioni

  • protein anchor Source: SGD

GO - Biological processi

  • CVT vesicle assembly Source: SGD
  • macroautophagy Source: SGD
  • nucleus-vacuole junction assembly Source: SGD
  • piecemeal microautophagy of nucleus Source: SGD
  • vacuole fusion, non-autophagic Source: SGD
  • vacuole inheritance Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30139-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein 8
Gene namesi
Name:VAC8
Synonyms:YEB3
Ordered Locus Names:YEL013W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL013W.
SGDiS000000739. VAC8.

Subcellular locationi

  • Vacuole membrane 1 Publication; Lipid-anchor 1 Publication

GO - Cellular componenti

  • fungal-type vacuole membrane Source: SGD
  • Myo2p-Vac17p-Vac8p transport complex Source: SGD
  • nucleus-vacuole junction Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 74CCSC → GTSS in VAC8-3; not palmitoylated. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 578577Vacuolar protein 8PRO_0000064302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Lipidationi4 – 41S-palmitoyl cysteine1 Publication
Lipidationi5 – 51S-palmitoyl cysteine1 Publication
Lipidationi7 – 71S-palmitoyl cysteine1 Publication
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei16 – 161Phosphoserine3 Publications

Post-translational modificationi

Palmitoylated on one or more of its N-terminal cysteine residues by PFA3, which is required for vacuole fusion.3 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP39968.
PaxDbiP39968.
PeptideAtlasiP39968.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG13Q066285EBI-20212,EBI-36188
NVJ1P388814EBI-20212,EBI-24885
VAB2P400032EBI-20212,EBI-22275

Protein-protein interaction databases

BioGridi36717. 106 interactions.
DIPiDIP-5121N.
IntActiP39968. 20 interactions.
MINTiMINT-517641.
STRINGi4932.YEL013W.

Structurei

3D structure databases

ProteinModelPortaliP39968.
SMRiP39968. Positions 46-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati37 – 7539ARM 1Add
BLAST
Repeati76 – 11439ARM 2Add
BLAST
Repeati116 – 15540ARM 3Add
BLAST
Repeati157 – 19640ARM 4Add
BLAST
Repeati198 – 23740ARM 5Add
BLAST
Repeati239 – 28042ARM 6Add
BLAST
Repeati282 – 32140ARM 7Add
BLAST
Repeati323 – 36341ARM 8Add
BLAST
Repeati407 – 44640ARM 9Add
BLAST

Sequence similaritiesi

Belongs to the beta-catenin family.Curated
Contains 9 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5064.
GeneTreeiENSGT00770000120927.
HOGENOMiHOG000177331.
InParanoidiP39968.
KOiK08332.
OMAiVQCHAIS.
OrthoDBiEOG7Q8CX4.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
[Graphical view]
PfamiPF00514. Arm. 8 hits.
[Graphical view]
SMARTiSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39968-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSCCSCLKD SSDEASVSPI ADNEREAVTL LLGYLEDKDQ LDFYSGGPLK
60 70 80 90 100
ALTTLVYSDN LNLQRSAALA FAEITEKYVR QVSREVLEPI LILLQSQDPQ
110 120 130 140 150
IQVAACAALG NLAVNNENKL LIVEMGGLEP LINQMMGDNV EVQCNAVGCI
160 170 180 190 200
TNLATRDDNK HKIATSGALI PLTKLAKSKH IRVQRNATGA LLNMTHSEEN
210 220 230 240 250
RKELVNAGAV PVLVSLLSST DPDVQYYCTT ALSNIAVDEA NRKKLAQTEP
260 270 280 290 300
RLVSKLVSLM DSPSSRVKCQ ATLALRNLAS DTSYQLEIVR AGGLPHLVKL
310 320 330 340 350
IQSDSIPLVL ASVACIRNIS IHPLNEGLIV DAGFLKPLVR LLDYKDSEEI
360 370 380 390 400
QCHAVSTLRN LAASSEKNRK EFFESGAVEK CKELALDSPV SVQSEISACF
410 420 430 440 450
AILALADVSK LDLLEANILD ALIPMTFSQN QEVSGNAAAA LANLCSRVNN
460 470 480 490 500
YTKIIEAWDR PNEGIRGFLI RFLKSDYATF EHIALWTILQ LLESHNDKVE
510 520 530 540 550
DLVKNDDDII NGVRKMADVT FERLQRSGID VKNPGSNNNP SSNDNNSNNN
560 570
DTGSEHQPVE DASLELYNIT QQILQFLH
Length:578
Mass (Da):63,208
Last modified:January 23, 2007 - v3
Checksum:iB2E75774B47E5933
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005267 mRNA. Translation: AAQ13402.1.
U18530 Genomic DNA. Translation: AAB64490.1.
BK006939 Genomic DNA. Translation: DAA07640.1.
PIRiS50446.
RefSeqiNP_010903.3. NM_001178828.3.

Genome annotation databases

EnsemblFungiiYEL013W; YEL013W; YEL013W.
GeneIDi856702.
KEGGisce:YEL013W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005267 mRNA. Translation: AAQ13402.1.
U18530 Genomic DNA. Translation: AAB64490.1.
BK006939 Genomic DNA. Translation: DAA07640.1.
PIRiS50446.
RefSeqiNP_010903.3. NM_001178828.3.

3D structure databases

ProteinModelPortaliP39968.
SMRiP39968. Positions 46-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36717. 106 interactions.
DIPiDIP-5121N.
IntActiP39968. 20 interactions.
MINTiMINT-517641.
STRINGi4932.YEL013W.

Proteomic databases

MaxQBiP39968.
PaxDbiP39968.
PeptideAtlasiP39968.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL013W; YEL013W; YEL013W.
GeneIDi856702.
KEGGisce:YEL013W.

Organism-specific databases

EuPathDBiFungiDB:YEL013W.
SGDiS000000739. VAC8.

Phylogenomic databases

eggNOGiCOG5064.
GeneTreeiENSGT00770000120927.
HOGENOMiHOG000177331.
InParanoidiP39968.
KOiK08332.
OMAiVQCHAIS.
OrthoDBiEOG7Q8CX4.

Enzyme and pathway databases

BioCyciYEAST:G3O-30139-MONOMER.

Miscellaneous databases

NextBioi982766.
PROiP39968.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
[Graphical view]
PfamiPF00514. Arm. 8 hits.
[Graphical view]
SMARTiSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "New members of the plakoglobin/armadillo/beta-catenin family characterized by armadillo repeats."
    Fischer R.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole."
    Wang Y.-X., Catlett N.L., Weisman L.S.
    J. Cell Biol. 140:1063-1074(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4; CYS-5 AND CYS-7, MUTAGENESIS OF 4-CYS--CYS-7, SUBCELLULAR LOCATION.
  5. "Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting."
    Scott S.V., Nice D.C. III, Nau J.J., Weisman L.S., Kamada Y., Keizer-Gunnink I., Funakoshi T., Veenhuis M., Ohsumi Y., Klionsky D.J.
    J. Biol. Chem. 275:25840-25849(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH ATG13.
  6. "Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion."
    Veit M., Laage R., Dietrich L., Wang L., Ungermann C.
    EMBO J. 20:3145-3155(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p."
    Smotrys J.E., Schoenfish M.J., Stutz M.A., Linder M.E.
    J. Cell Biol. 170:1091-1099(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVAC8_YEAST
AccessioniPrimary (citable) accession number: P39968
Secondary accession number(s): D3DLN6, Q549T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5680 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.