Skip Header

Contribute Send feedback
Read comments (?) or add your own

P25591 (VAC17_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
vacuole-related protein 17
Alternative name(s):
Vacuole-specific MYO2 receptor VAC17
Gene names
Name:VAC17
Ordered Locus Names:YCL063W
ORF Names:YCL63W/YCL62W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vacuole-specific MYO2 receptor required for vacuole inheritance. Binds simultaneously to MYO2 and to VAC8, a vacuolar membrane protein, forming a transport complex which moves the attached vacuole membrane along actin cables into the bud. Once the vacuole arrives in the bud, VAC17 is degraded, depositing the vacuole in its correct location. Ref.4 Ref.5 Ref.10

Subunit structure

Interacts with MYO2 and VAC8. Interacts with ATG18. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Vacuole membrane; Peripheral membrane protein; Cytoplasmic side Ref.5.

Sequence similarities

Belongs to the VAC17 family.

Ontologies

Keywords
   Cellular componentMembrane
Vacuole
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processvacuole inheritance

Inferred from genetic interaction Ref.5. Source: SGD

   Cellular componentfungal-type vacuole membrane

Inferred from direct assay Ref.5. Source: SGD

   Molecular functionprotein anchor

Inferred from physical interaction Ref.4. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423vacuole-related protein 17
PRO_0000202554

Regions

Region110 – 17061MYO2-binding
Region290 – 38091VAC8-binding

Amino acid modifications

Modified residue1191Phosphoserine Ref.10
Modified residue1491Phosphothreonine Ref.10
Modified residue1781Phosphoserine Ref.10
Modified residue2481Phosphothreonine Ref.10

Experimental info

Mutagenesis1191S → A: Impairs phosphorylation; when associated with A-149; A-178 and A-248. Ref.10
Mutagenesis1491T → A: Impairs phosphorylation; when associated with A-119; A-178 and A-248. Ref.10
Mutagenesis1781S → A: Impairs phosphorylation; when associated with A-119; A-149 and A-248. Ref.10
Mutagenesis2251F → S: Stabilizes VAC17 whose protein levels are about 10-fold higher than wild-type. Ref.10
Mutagenesis2481T → A: Impairs phosphorylation; when associated with A-119; A-149 and A-178. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P25591 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 7F14A3A0BFE9571B

FASTA42347,843
        10         20         30         40         50         60 
MATQALEDIT ERLLIRSQEA ILQLDLWIQR QQRSSICQTT DQESLDKLSQ QYNQYMSQLN 

        70         80         90        100        110        120 
SLYVRSESVR DKLSKEQQRR LITEDNEHQR IEDLVREFQD ITLRLNELAT VPNEAPNDSP 

       130        140        150        160        170        180 
QSQSTRSSLG SFQPRPLKII ERQRLCMVTP SKPPKKSVGF NPINEVDCPS KTNSLPCSPK 

       190        200        210        220        230        240 
KQPARNRTLR AAKSHDTGLN KSKKPSSSDT YESFFKNRQR LSLTFFDEMD DEDFDSDQDT 

       250        260        270        280        290        300 
IILPNISTPP HVGVTAKGAE FEPLRRYNSH ESILSNKPAP SKSLNLGSFS ASFFRPSNPT 

       310        320        330        340        350        360 
FGTSISNVQV NCHPTVAATM APSRNGPRIS SSKALLSSFI ARSDTHTVKE NNTNLKHASF 

       370        380        390        400        410        420 
MDKFNSSLST ISESFQSKRG RKNKGMNEER ISNHNVAQEQ KNNMDISVSI EELQDALNTE 


LLF

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed: 1574125] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Gromadka R.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Identification of an organelle-specific myosin V receptor."
Ishikawa K., Catlett N.L., Novak J.L., Tang F., Nau J.J., Weisman L.S.
J. Cell Biol. 160:887-897(2003) [PubMed: 12642614] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYO2 AND VAC8.
[5]"Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole."
Tang F., Kauffman E.J., Novak J.L., Nau J.J., Catlett N.L., Weisman L.S.
Nature 422:87-92(2003) [PubMed: 12594460] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAINS, INTERACTION WITH MYO2 AND VAC8.
[6]"A point mutation in the cargo-binding domain of myosin V affects its interaction with multiple cargoes."
Pashkova N., Catlett N.L., Novak J.L., Weisman L.S.
Eukaryot. Cell 4:787-798(2005) [PubMed: 15821138] [Abstract]
Cited for: INTERACTION WITH MYO2.
[7]"Myosin V attachment to cargo requires the tight association of two functional subdomains."
Pashkova N., Catlett N.L., Novak J.L., Wu G., Lu R., Cohen R.E., Weisman L.S.
J. Cell Biol. 168:359-364(2005) [PubMed: 15684027] [Abstract]
Cited for: INTERACTION WITH MYO2.
[8]"Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes."
Tang F., Peng Y., Nau J.J., Kauffman E.J., Weisman L.S.
Traffic 7:1368-1377(2006) [PubMed: 16824055] [Abstract]
Cited for: INTERACTION WITH VAC8.
[9]"Atg18 regulates organelle morphology and Fab1 kinase activity independent of its membrane recruitment by phosphatidylinositol 3,5-bisphosphate."
Efe J.A., Botelho R.J., Emr S.D.
Mol. Biol. Cell 18:4232-4244(2007) [PubMed: 17699591] [Abstract]
Cited for: INTERACTION WITH ATG18.
[10]"The cyclin-dependent kinase Cdk1 directly regulates vacuole inheritance."
Peng Y., Weisman L.S.
Dev. Cell 15:478-485(2008) [PubMed: 18804442] [Abstract]
Cited for: PHOSPHORYLATION AT SER-119; THR-149; SER-178 AND THR-248, INTERACTION WITH MYO2, FUNCTION, MUTAGENESIS OF SER-119; THR-149; SER-178; PHE-225 AND THR-248.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X59720 Genomic DNA. Translation: CAA42404.1.
BK006937 Genomic DNA. Translation: DAA07424.1.
PIRS74278.
RefSeqNP_009870.1. NM_001178705.1.

3D structure databases

ProteinModelPortalP25591.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2065N.
IntActP25591. 4 interactions.
MINTMINT-476227.
STRINGP25591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL063W; YCL063W; YCL063W.
GeneID850296.
KEGGsce:YCL063W.
NMPDRfig|4932.3.peg.588.

Organism-specific databases

CYGDYCL063w.
SGDS000000568. VAC17.

Phylogenomic databases

eggNOGfuNOG12705.
HOGENOMHBG204102.
OMARCNSHES.
OrthoDBEOG437VQJ.

Gene expression databases

ArrayExpressP25591.
GenevestigatorP25591.
GermOnlineYCL063W. Saccharomyces cerevisiae.

Family and domain databases

ProtoNetSearch...

Other

NextBio965667.

Entry information

Entry nameVAC17_YEAST
AccessionPrimary (citable) accession number: P25591
Secondary accession number(s): D6VQV5, P25590
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 1998
Last modified: January 25, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents