Vacuole morphology and inheritance protein 14 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q06708 (VAC14_YEAST)

Last modified December 15, 2009. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Vacuole morphology and inheritance protein 14
Alternative name(s):
Swollen vacuole phenotype 2 protein

Gene names

Name:	VAC14
Synonyms:	SVP2
Ordered Locus Names:	YLR386W
ORF Names:	L3502.1

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	880 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2). Regulates the synthesis of PtdIns(3,5)P2 by positive activation of FAB1 and by controlling FIG4 localization. Required for FIG4-mediated turnover of PtdIns(3,5)P2 after hyperosmotic shock. Essential for the control of trafficking of some proteins to the vacuole lumen via the multivesicular body (MVB), and for maintenance of vacuole size and acidity. Ref.2 Ref.3 Ref.6 Ref.7 Ref.9
Subunit structure	Component of the PI(3,5)P2 regulatory complex, composed of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the complex and serves as a scaffold.
Subcellular location	Vacuole membrane; Peripheral membrane protein. Note: Limiting membrane of the vacuole. Localization requires FAB1 and FIG4. Ref.2 Ref.6 Ref.9 Ref.4 Ref.10
Domain	The N-terminal domain mediates interaction with FAB1 and VAC7 while the C-terminal domain mediates interaction with FIG4. Ref.9
Miscellaneous	Present with 12388 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the VAC14 family. Contains 5 HEAT repeats.

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Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Membrane Vacuole
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid metabolic process Inferred from genetic interaction. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW vacuole inheritance Inferred from mutant phenotype. Source: SGD
Cellular component	PAS complex Ref.9 Inferred from direct assay. Source: SGD extrinsic to vacuolar membrane Ref.2 Inferred from direct assay. Source: SGD fungal-type vacuole membrane Ref.2 Ref.6 Inferred from direct assay. Source: SGD
Molecular function	enzyme activator activity Ref.2 Ref.7 Inferred from mutant phenotype. Source: SGD protein binding, bridging Ref.9 Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	P38800	1	EBI-27189,EBI-24597
ADE6	P38972	2	EBI-27189,EBI-14246
ATG18	P43601	1	EBI-27189,EBI-22968
COG6	P53959	1	EBI-27189,EBI-4829
FIG4	P42837	1	EBI-27189,EBI-28407
NAM1	P10849	1	EBI-27189,EBI-11823
PRE8	P23639	1	EBI-27189,EBI-13959
TAF2	P23255	1	EBI-27189,EBI-18862

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 880

880

Vacuole morphology and inheritance protein 14

PRO_0000065756

Regions

Repeat

82 – 119

HEAT 1

Repeat

243 – 280

HEAT 2

Repeat

388 – 425

HEAT 3

Repeat

429 – 466

HEAT 4

Repeat

517 – 554

HEAT 5

Amino acid modifications

Modified residue

308

Phosphothreonine Ref.11

Modified residue

767

Phosphoserine Ref.8

Modified residue

805

Phosphoserine Ref.11

Modified residue

806

Phosphoserine Ref.11

Modified residue

853

Phosphoserine Ref.11

Modified residue

859

Phosphoserine Ref.11

Modified residue

867

Phosphoserine Ref.11

Experimental info

Mutagenesis

H → Y: Loss of interaction with ATG18 and VAC7. Ref.9

Mutagenesis

R → K: Loss of interaction with ATG18 and VAC7. Ref.9

Mutagenesis

101

Q → R: Loss of interaction with ATG18 and VAC7. Ref.9

Mutagenesis

149

L → R: Loss of interaction with ATG18, FAB1 and VAC7. No loss of interaction with FIG4. Ref.9

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Sequences

Sequence

Length

Mass (Da)

Tools

Q06708-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E625AB6F032D2E1B
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FASTA

880

99,773

        10         20         30         40         50         60 
MEKSIAKGLS DKLYEKRKAA ALELEKLVKQ CVLEGDYDRI DKIIDELCRD YAYALHQPMA 

        70         80         90        100        110        120 
RNAGLMGLAA TAIALGINDV GRYLRNILPP VLACFGDQND QVRFYACESL YNIAKIAKGE 

       130        140        150        160        170        180 
ILVYFNEIFD VLCKISADTE NSVRGAAELL DRLIKDIVAE RASNYISIVN NGSHGLLPAI 

       190        200        210        220        230        240 
KTDPISGDVY QEEYEQDNQL AFSLPKFIPL LTERIYAINP DTRVFLVDWL KVLLNTPGLE 

       250        260        270        280        290        300 
LISYLPSFLG GLFTFLGDSH KDVRTVTHTL MDSLLHEVDR ISKLQTEIKM KRLERLKMLE 

       310        320        330        340        350        360 
DKYNNSSTPT KKADGALIAE KKKTLMTALG GLSKPLSMET DDTKLSNTNE TDDERHLTSQ 

       370        380        390        400        410        420 
EQLLDSEATS QEPLRDGEEY IPGQDINLNF PEVITVLVNN LASSEAEIQL IALHWIQVIL 

       430        440        450        460        470        480 
SISPNVFIPF LSKILSVLLK LLSDSDPHIT EIAQLVNGQL LSLCSSYVGK ETDGKIAYGP 

       490        500        510        520        530        540 
IVNSLTLQFF DSRIDAKIAC LDWLILIYHK APNQILKHND SMFLTLLKSL SNRDSVLIEK 

       550        560        570        580        590        600 
ALSLLQSLCS DSNDNYLRQF LQDLLTLFKR DTKLVKTRAN FIMRQISSRL SPERVYKVIS 

       610        620        630        640        650        660 
SILDNYNDTT FVKMMIQILS TNLITSPEMS SLRNKLRTCE DGMFFNSLFK SWCPNPVSVI 

       670        680        690        700        710        720 
SLCFVAENYE LAYTVLQTYA NYELKLNDLV QLDILIQLFE SPVFTRMRLQ LLEQQKHPFL 

       730        740        750        760        770        780 
HKCLFGILMI IPQSKAFETL NRRLNSLNIW TSQSYVMNNY IRQRENSNFC DSNSDISQRS 

       790        800        810        820        830        840 
VSQSKLHFQE LINHFKAVSE EDEYSSDMIR LDHGANNKSL LLGSFLDGID EDKQEIVTPI 

       850        860        870        880 
SPMNEAINEE MESPNDNSSV ILKDSGSLPF NRNVSDKLKK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p." Bonangelino C.J., Nau J.J., Duex J.E., Brinkman M., Wurmser A.E., Gary J.D., Emr S.D., Weisman L.S. J. Cell Biol. 156:1015-1028(2002) [PubMed: 11889142] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[3]	"Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body." Dove S.K., McEwen R.K., Mayes A., Hughes D.C., Beggs J.D., Michell R.H. Curr. Biol. 12:885-893(2002) [PubMed: 12062051] [Abstract] Cited for: FUNCTION, INTERACTION WITH YDR466W; YGR241C; YLR093C; VAC14; FIG4 AND YPR029C.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Vacuole size control: regulation of PtdIns(3,5)P2 levels by the vacuole-associated Vac14-Fig4 complex, a PtdIns(3,5)P2-specific phosphatase." Rudge S.A., Anderson D.M., Emr S.D. Mol. Biol. Cell 15:24-36(2004) [PubMed: 14528018] [Abstract] Cited for: FUNCTION, INTERACTION WITH FIG4, SUBCELLULAR LOCATION.
[7]	"The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2 synthesis and turnover." Duex J.E., Tang F., Weisman L.S. J. Cell Biol. 172:693-704(2006) [PubMed: 16492811] [Abstract] Cited for: FUNCTION.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-767, MASS SPECTROMETRY.
[9]	"VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse." Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M., Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D., Meisler M.H., Weisman L.S. EMBO J. 27:3221-3234(2008) [PubMed: 19037259] [Abstract] Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF HIS-56; ARG-61; GLN-101 AND LEU-149.
[10]	"Assembly of a Fab1 phosphoinositide kinase signaling complex requires the Fig4 phosphoinositide phosphatase." Botelho R.J., Efe J.A., Teis D., Emr S.D. Mol. Biol. Cell 19:4273-4286(2008) [PubMed: 18653468] [Abstract] Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, SUBCELLULAR LOCATION.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308; SER-805; SER-806; SER-853; SER-859 AND SER-867, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U19104 Genomic DNA. Translation: AAB67272.1.
PIR	S51473.
RefSeq	NP_013490.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1176N.
IntAct	Q06708. 37 interactions.
STRING	Q06708.
Proteomic databases
PeptideAtlas	Q06708.
Genome annotation databases
Ensembl	YLR386W; YLR386W; YLR386W; Saccharomyces cerevisiae. [Genome view]
GeneID	851102.
KEGG	sce:YLR386W.
NMPDR	fig\|4932.3.peg.4515.
Organism-specific databases
CYGD	YLR386w.
SGD	S000004378. VAC14.
Phylogenomic databases
HOGENOM	HBG512104.
OMA	LQTEDSL.
OrthoDB	EOG91VMK8.
Gene expression databases
ArrayExpress	Q06708.
Genevestigator	Q06708.
GermOnline	YLR386W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000357. HEAT. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit.
Pfam	PF02985. HEAT. 1 hit. [Graphical view]
PROSITE	PS50077. HEAT_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967794.

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Entry information

Entry name

VAC14_YEAST

Accession

Primary (citable) accession number: Q06708

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	December 15, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents