VAC14/YLR386W Protein Information Help

Standard Name Vac14p 1
Systematic Name Ylr386wp
ORF Classification Verified
Description Enzyme regulator; involved in synthesis of phosphatidylinositol 3,5-bisphosphate, in control of trafficking of some proteins to the vacuole lumen via the MVB, and in maintenance of vacuole size and acidity; binds negative (Fig4p) and positive (Fab1p) regulators of PtdIns(3,5)P(2) to control endolysosome function (1, 2, 3, 4)
Name Description VACuole morphology and inheritance mutant 1
Experimental Data
Molecules/cell 12400 5
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 880
Molecular Weight (Da) 99,771
Isoelectric Point (pI) 5.24

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Vac14p (InterPro)
Physical Interactions There are 56 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052F7A | Q06708
MIPS: YLR386W
NCBI: 398366065 | 609424 | 8928506 | NP_013490.3 | NM_001182275.3
GenBank/EMBL/DDBJ: AAB67272.1 | DAA09687.1 | U19104
Amino Acid Sequence (or in FASTA format)
       1  MEKSIAKGLS DKLYEKRKAA ALELEKLVKQ CVLEGDYDRI DKIIDELCRD
      51  YAYALHQPMA RNAGLMGLAA TAIALGINDV GRYLRNILPP VLACFGDQND
     101  QVRFYACESL YNIAKIAKGE ILVYFNEIFD VLCKISADTE NSVRGAAELL
     151  DRLIKDIVAE RASNYISIVN NGSHGLLPAI KTDPISGDVY QEEYEQDNQL
     201  AFSLPKFIPL LTERIYAINP DTRVFLVDWL KVLLNTPGLE LISYLPSFLG
     251  GLFTFLGDSH KDVRTVTHTL MDSLLHEVDR ISKLQTEIKM KRLERLKMLE
     301  DKYNNSSTPT KKADGALIAE KKKTLMTALG GLSKPLSMET DDTKLSNTNE
     351  TDDERHLTSQ EQLLDSEATS QEPLRDGEEY IPGQDINLNF PEVITVLVNN
     401  LASSEAEIQL IALHWIQVIL SISPNVFIPF LSKILSVLLK LLSDSDPHIT
     451  EIAQLVNGQL LSLCSSYVGK ETDGKIAYGP IVNSLTLQFF DSRIDAKIAC
     501  LDWLILIYHK APNQILKHND SMFLTLLKSL SNRDSVLIEK ALSLLQSLCS
     551  DSNDNYLRQF LQDLLTLFKR DTKLVKTRAN FIMRQISSRL SPERVYKVIS
     601  SILDNYNDTT FVKMMIQILS TNLITSPEMS SLRNKLRTCE DGMFFNSLFK
     651  SWCPNPVSVI SLCFVAENYE LAYTVLQTYA NYELKLNDLV QLDILIQLFE
     701  SPVFTRMRLQ LLEQQKHPFL HKCLFGILMI IPQSKAFETL NRRLNSLNIW
     751  TSQSYVMNNY IRQRENSNFC DSNSDISQRS VSQSKLHFQE LINHFKAVSE
     801  EDEYSSDMIR LDHGANNKSL LLGSFLDGID EDKQEIVTPI SPMNEAINEE
     851  MESPNDNSSV ILKDSGSLPF NRNVSDKLKK *                    

external links for Vac14p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily LoQate
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) CYC2008 (complexes) MIPS YeastGFP
Candida (CGD) Complexome Pfam domains YeastRC Public Image Repository
YGOB DIP YeastRC Structure Prediction (Seattle)
YOGY GeneMANIA


IMP

References cited on this page View Complete Literature Guide for Vac14p
1) Bonangelino CJ, et al.  (2002) Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p. J Cell Biol 156(6):1015-28
2) Dove SK, et al.  (2002) Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body. Curr Biol 12(11):885-93
3) Rudge SA, et al.  (2004) Vacuole size control: regulation of PtdIns(3,5)P2 levels by the vacuole-associated Vac14-Fig4 complex, a PtdIns(3,5)P2-specific phosphatase. Mol Biol Cell 15(1):24-36
4) Alghamdi TA, et al.  (2013) Vac14 protein multimerization is a prerequisite step for Fab1 protein complex assembly and function. J Biol Chem 288(13):9363-72
5) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41