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P22543 (VPS34_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 3-kinase VPS34

Short name=PI3-kinase VPS34
Short name=PI3K VPS34
Short name=PtdIns-3-kinase VPS34
EC=2.7.1.137
Alternative name(s):
Carboxypeptidase Y-deficient protein 15
Vacuolar protein sorting-associated protein 34
Vacuolar protein-targeting protein 29
Gene names
Name:VPS34
Synonyms:END12, PEP15, VPL7, VPT29
Ordered Locus Names:YLR240W
ORF Names:L9672.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length875 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphatidylinositol 3-kinase required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Its activation by VPS15 may lead to the phosphorylation of phosphatidylinositol in the sorting compartment membrane. Finally, it might also be involved in ethanol tolerance and cell wall integrity. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate.

Enzyme regulation

Phosphatidylinositol 3-kinase activity is directly dependent on VPS15 protein kinase activity.

Subunit structure

Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34 and ATG14; and of the VPS34 PI3-kinase complex II composed of VPS15, VPS30, VPS34 and VPS38.

Subcellular location

Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein Ref.10 Ref.13.

Post-translational modification

Autophosphorylated. Might also be phosphorylated by VPS15. Ref.8

Miscellaneous

Present with 1080 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentEndosome
Golgi apparatus
Membrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processperoxisome degradation

Inferred from mutant phenotype PubMed 21121900. Source: SGD

phosphatidylinositol phosphorylation

Inferred from direct assay Ref.8Ref.7. Source: SGD

phosphatidylinositol-3-phosphate biosynthetic process

Inferred from direct assay Ref.8Ref.7. Source: GOC

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23335340. Source: SGD

protein phosphorylation

Inferred from direct assay Ref.8. Source: SGD

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from direct assay PubMed 16421251. Source: SGD

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

fungal-type vacuole membrane

Inferred from direct assay PubMed 16421251. Source: SGD

nucleus-vacuole junction

Inferred from direct assay PubMed 23335340. Source: SGD

peroxisome

Inferred from direct assay PubMed 21121900. Source: SGD

phosphatidylinositol 3-kinase complex I

Inferred from direct assay Ref.10. Source: SGD

phosphatidylinositol 3-kinase complex II

Inferred from direct assay Ref.10. Source: SGD

pre-autophagosomal structure

Inferred from direct assay PubMed 16421251. Source: SGD

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from direct assay Ref.8Ref.7. Source: SGD

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16839886. Source: IntAct

protein kinase activity

Inferred from direct assay Ref.8. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GPA1P085393EBI-20405,EBI-7376

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 875875Phosphatidylinositol 3-kinase VPS34
PRO_0000088818

Regions

Domain14 – 188175C2 PI3K-type
Domain293 – 526234PIK helical
Domain619 – 873255PI3K/PI4K

Experimental info

Mutagenesis7311D → A: Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. Ref.7
Mutagenesis7361N → K: Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. Ref.7
Mutagenesis7491D → E: Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P22543 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 806E3404EF260287

FASTA875100,921
        10         20         30         40         50         60 
MSLNNITFCV SQDLDVPLKV KIKSLEGHKP LLKPSQKILN PELMLIGSNV FPSSDLIVSL 

        70         80         90        100        110        120 
QVFDKERNRN LTLPIYTPYI PFRNSRTWDY WLTLPIRIKQ LTFSSHLRII LWEYNGSKQI 

       130        140        150        160        170        180 
PFFNLETSIF NLKDCTLKRG FESLKFRYDV IDHCEVVTDN KDQENLNKYF QGEFTRLPWL 

       190        200        210        220        230        240 
DEITISKLRK QRENRTWPQG TFVLNLEFPM LELPVVFIER EIMNTQMNIP TLKNNPGLST 

       250        260        270        280        290        300 
DLREPNRNDP QIKISLGDKY HSTLKFYDPD QPNNDPIEEK YRRLERASKN ANLDKQVKPD 

       310        320        330        340        350        360 
IKKRDYLNKI INYPPGTKLT AHEKGSIWKY RYYLMNNKKA LTKLLQSTNL REESERVEVL 

       370        380        390        400        410        420 
ELMDSWAEID IDDALELLGS TFKNLSVRSY AVNRLKKASD KELELYLLQL VEAVCFENLS 

       430        440        450        460        470        480 
TFSDKSNSEF TIVDAVSSQK LSGDSMLLST SHANQKLLKS ISSESETSGT ESLPIVISPL 

       490        500        510        520        530        540 
AEFLIRRALV NPRLGSFFYW YLKSESEDKP YLDQILSSFW SRLDKKSRNI LNDQVRLINV 

       550        560        570        580        590        600 
LRECCETIKR LKDTTAKKME LLVHLLETKV RPLVKVRPIA LPLDPDVLIC DVCPETSKVF 

       610        620        630        640        650        660 
KSSLSPLKIT FKTTLNQPYH LMFKVGDDLR QDQLVVQIIS LMNELLKNEN VDLKLTPYKI 

       670        680        690        700        710        720 
LATGPQEGAI EFIPNDTLAS ILSKYHGILG YLKLHYPDEN ATLGVQGWVL DNFVKSCAGY 

       730        740        750        760        770        780 
CVITYILGVG DRHLDNLLVT PDGHFFHADF GYILGQDPKP FPPLMKLPPQ IIEAFGGAES 

       790        800        810        820        830        840 
SNYDKFRSYC FVAYSILRRN AGLILNLFEL MKTSNIPDIR IDPNGAILRV RERFNLNMSE 

       850        860        870 
EDATVHFQNL INDSVNALLP IVIDHLHNLA QYWRT 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of VPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccharomyces cerevisiae."
Herman P.K., Emr S.D.
Mol. Cell. Biol. 10:6742-6754(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"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. expand/collapse author list , 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.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases."
Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.
Mol. Cell. Biol. 8:4936-4948(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Phosphatidylinositol 3-kinase and its novel product, phosphatidylinositol 3-phosphate, are present in Saccharomyces cerevisiae."
Auger K.R., Carpenter C.L., Cantley L.C., Varticovski L.
J. Biol. Chem. 264:20181-20184(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole."
Stack J.H., Herman P.K., Schu P.V., Emr S.D.
EMBO J. 12:2195-2204(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VPS15.
[7]"Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting."
Schu P.V., Takegawa K., Fry M.J., Stack J.H., Waterfield M.D., Emr S.D.
Science 260:88-91(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-731; ASN-736 AND ASP-749.
[8]"Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities."
Stack J.H., Emr S.D.
J. Biol. Chem. 269:31552-31562(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION.
[9]"Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: identification of six new END genes."
Munn A.L., Riezman H.
J. Cell Biol. 127:373-386(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae."
Kihara A., Noda T., Ishihara N., Ohsumi Y.
J. Cell Biol. 152:519-530(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS15; VPS30; VPS38 AND ATG14.
[11]"Identification of genes required for growth under ethanol stress using transposon mutagenesis in Saccharomyces cerevisiae."
Takahashi T., Shimoi H., Ito K.
Mol. Genet. Genomics 265:1112-1119(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase."
Burda P., Padilla S.M., Sarkar S., Emr S.D.
J. Cell Sci. 115:3889-3900(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53531 Genomic DNA. Translation: CAA37610.1.
U20865 Genomic DNA. Translation: AAB67396.1.
U19027 Genomic DNA. Translation: AAB67422.2.
BK006945 Genomic DNA. Translation: DAA09554.1.
PIRA36369.
RefSeqNP_013341.1. NM_001182127.1.

3D structure databases

ProteinModelPortalP22543.
SMRP22543. Positions 268-874.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31507. 46 interactions.
DIPDIP-97N.
IntActP22543. 5 interactions.
MINTMINT-2780608.
STRING4932.YLR240W.

Proteomic databases

MaxQBP22543.
PaxDbP22543.
PeptideAtlasP22543.
PRIDEP22543.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR240W; YLR240W; YLR240W.
GeneID850941.
KEGGsce:YLR240W.

Organism-specific databases

CYGDYLR240w.
SGDS000004230. VPS34.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00620000087805.
HOGENOMHOG000174003.
KOK00914.
OMASAMTRRI.
OrthoDBEOG7WHHK2.

Enzyme and pathway databases

BioCycYEAST:YLR240W-MONOMER.
BRENDA2.7.1.137. 984.

Gene expression databases

GenevestigatorP22543.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 2 hits.
2.60.40.150. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR008290. PI3K_Vps34.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
PIRSFPIRSF000587. PI3K_Vps34. 1 hit.
SMARTSM00142. PI3K_C2. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967390.
PROP22543.

Entry information

Entry nameVPS34_YEAST
AccessionPrimary (citable) accession number: P22543
Secondary accession number(s): D6VYN8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 11, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families