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Protein

Vacuole morphology and inheritance protein 14

Gene

VAC14

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

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.5 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein binding, bridging Source: SGD

GO - Biological processi

  • phosphatidylinositol biosynthetic process Source: SGD
  • positive regulation of kinase activity Source: SGD
  • protein transport Source: UniProtKB-KW
  • regulation of lipid kinase activity Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15185.
YEAST:G3O-32452-MONOMER.
ReactomeiR-SCE-1660514. Synthesis of PIPs at the Golgi membrane.
R-SCE-1660516. Synthesis of PIPs at the early endosome membrane.
R-SCE-1660517. Synthesis of PIPs at the late endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuole morphology and inheritance protein 14
Alternative name(s):
Swollen vacuole phenotype 2 protein
Gene namesi
Name:VAC14
Synonyms:SVP2
Ordered Locus Names:YLR386W
ORF Names:L3502.1
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR386W.
SGDiS000004378. VAC14.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of vacuolar membrane Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • PAS complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561H → Y: Loss of interaction with ATG18 and VAC7. 1 Publication
Mutagenesisi61 – 611R → K: Loss of interaction with ATG18 and VAC7. 1 Publication
Mutagenesisi101 – 1011Q → R: Loss of interaction with ATG18 and VAC7. 1 Publication
Mutagenesisi149 – 1491L → R: Loss of interaction with ATG18, FAB1 and VAC7. No loss of interaction with FIG4. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 880880Vacuole morphology and inheritance protein 14PRO_0000065756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei767 – 7671PhosphoserineCombined sources
Modified residuei805 – 8051PhosphoserineCombined sources
Modified residuei867 – 8671PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06708.
PeptideAtlasiQ06708.

PTM databases

iPTMnetiQ06708.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-27189,EBI-27189
ATG18P436015EBI-27189,EBI-22968
FAB1P347569EBI-27189,EBI-6754
FIG4P428377EBI-27189,EBI-28407
VAC7P539504EBI-27189,EBI-28714

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi31645. 178 interactions.
DIPiDIP-1176N.
IntActiQ06708. 26 interactions.
MINTiMINT-401035.

Structurei

3D structure databases

ProteinModelPortaliQ06708.
SMRiQ06708. Positions 3-150, 246-274, 523-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati82 – 11938HEAT 1Add
BLAST
Repeati243 – 28038HEAT 2Add
BLAST
Repeati388 – 42538HEAT 3Add
BLAST
Repeati429 – 46638HEAT 4Add
BLAST
Repeati517 – 55438HEAT 5Add
BLAST

Domaini

The N-terminal domain mediates interaction with FAB1 and VAC7 while the C-terminal domain mediates interaction with FIG4.1 Publication

Sequence similaritiesi

Belongs to the VAC14 family.Curated
Contains 5 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000008385.
HOGENOMiHOG000216640.
InParanoidiQ06708.
KOiK15305.
OMAiCIEKEED.
OrthoDBiEOG70PC63.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021133. HEAT_type_2.
IPR026825. Vac14.
IPR032878. Vac14_Fab1-bd.
IPR021841. VAC14_Fig4p-bd.
[Graphical view]
PANTHERiPTHR16023. PTHR16023. 3 hits.
PfamiPF12755. Vac14_Fab1_bd. 1 hit.
PF11916. Vac14_Fig4_bd. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06708-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSIAKGLS DKLYEKRKAA ALELEKLVKQ CVLEGDYDRI DKIIDELCRD
60 70 80 90 100
YAYALHQPMA RNAGLMGLAA TAIALGINDV GRYLRNILPP VLACFGDQND
110 120 130 140 150
QVRFYACESL YNIAKIAKGE ILVYFNEIFD VLCKISADTE NSVRGAAELL
160 170 180 190 200
DRLIKDIVAE RASNYISIVN NGSHGLLPAI KTDPISGDVY QEEYEQDNQL
210 220 230 240 250
AFSLPKFIPL LTERIYAINP DTRVFLVDWL KVLLNTPGLE LISYLPSFLG
260 270 280 290 300
GLFTFLGDSH KDVRTVTHTL MDSLLHEVDR ISKLQTEIKM KRLERLKMLE
310 320 330 340 350
DKYNNSSTPT KKADGALIAE KKKTLMTALG GLSKPLSMET DDTKLSNTNE
360 370 380 390 400
TDDERHLTSQ EQLLDSEATS QEPLRDGEEY IPGQDINLNF PEVITVLVNN
410 420 430 440 450
LASSEAEIQL IALHWIQVIL SISPNVFIPF LSKILSVLLK LLSDSDPHIT
460 470 480 490 500
EIAQLVNGQL LSLCSSYVGK ETDGKIAYGP IVNSLTLQFF DSRIDAKIAC
510 520 530 540 550
LDWLILIYHK APNQILKHND SMFLTLLKSL SNRDSVLIEK ALSLLQSLCS
560 570 580 590 600
DSNDNYLRQF LQDLLTLFKR DTKLVKTRAN FIMRQISSRL SPERVYKVIS
610 620 630 640 650
SILDNYNDTT FVKMMIQILS TNLITSPEMS SLRNKLRTCE DGMFFNSLFK
660 670 680 690 700
SWCPNPVSVI SLCFVAENYE LAYTVLQTYA NYELKLNDLV QLDILIQLFE
710 720 730 740 750
SPVFTRMRLQ LLEQQKHPFL HKCLFGILMI IPQSKAFETL NRRLNSLNIW
760 770 780 790 800
TSQSYVMNNY IRQRENSNFC DSNSDISQRS VSQSKLHFQE LINHFKAVSE
810 820 830 840 850
EDEYSSDMIR LDHGANNKSL LLGSFLDGID EDKQEIVTPI SPMNEAINEE
860 870 880
MESPNDNSSV ILKDSGSLPF NRNVSDKLKK
Length:880
Mass (Da):99,773
Last modified:November 1, 1996 - v1
Checksum:iE625AB6F032D2E1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19104 Genomic DNA. Translation: AAB67272.1.
BK006945 Genomic DNA. Translation: DAA09687.1.
PIRiS51473.
RefSeqiNP_013490.3. NM_001182275.3.

Genome annotation databases

EnsemblFungiiYLR386W; YLR386W; YLR386W.
GeneIDi851102.
KEGGisce:YLR386W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19104 Genomic DNA. Translation: AAB67272.1.
BK006945 Genomic DNA. Translation: DAA09687.1.
PIRiS51473.
RefSeqiNP_013490.3. NM_001182275.3.

3D structure databases

ProteinModelPortaliQ06708.
SMRiQ06708. Positions 3-150, 246-274, 523-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31645. 178 interactions.
DIPiDIP-1176N.
IntActiQ06708. 26 interactions.
MINTiMINT-401035.

PTM databases

iPTMnetiQ06708.

Proteomic databases

MaxQBiQ06708.
PeptideAtlasiQ06708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR386W; YLR386W; YLR386W.
GeneIDi851102.
KEGGisce:YLR386W.

Organism-specific databases

EuPathDBiFungiDB:YLR386W.
SGDiS000004378. VAC14.

Phylogenomic databases

GeneTreeiENSGT00390000008385.
HOGENOMiHOG000216640.
InParanoidiQ06708.
KOiK15305.
OMAiCIEKEED.
OrthoDBiEOG70PC63.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15185.
YEAST:G3O-32452-MONOMER.
ReactomeiR-SCE-1660514. Synthesis of PIPs at the Golgi membrane.
R-SCE-1660516. Synthesis of PIPs at the early endosome membrane.
R-SCE-1660517. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

PROiQ06708.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021133. HEAT_type_2.
IPR026825. Vac14.
IPR032878. Vac14_Fab1-bd.
IPR021841. VAC14_Fig4p-bd.
[Graphical view]
PANTHERiPTHR16023. PTHR16023. 3 hits.
PfamiPF12755. Vac14_Fab1_bd. 1 hit.
PF11916. Vac14_Fig4_bd. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YDR466W; YGR241C; YLR093C; VAC14; FIG4 AND YPR029C.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FIG4, SUBCELLULAR LOCATION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-767 AND SER-805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVAC14_YEAST
AccessioniPrimary (citable) accession number: Q06708
Secondary accession number(s): D6VZ21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12388 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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 one 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.