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P25641 (ATG15_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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

Names and origin

Protein namesRecommended name:
Putative lipase ATG15

EC=3.1.1.3
Alternative name(s):
Autophagy-related protein 15
Cytoplasm to vacuole targeting protein 17
Gene names
Name:ATG15
Synonyms:AUT5, CVT17
Ordered Locus Names:YCR068W
ORF Names:YCR68W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipase which is essential for lysis of subvacuolar cytoplasm to vacuole targeted bodies and intravacuolar autophagic bodies. Involved in the lysis of intravacuolar multivesicular body (MVB) vesicles. The intravacuolar membrane disintegration by ATG15 is critical to life span extension. Ref.1 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

Binds to both phosphatidylinositol (PI) and phosphatidylinositol 3,5-bisphosphate (PIP2).

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Endosomemultivesicular body membrane; Single-pass type II membrane protein. Prevacuolar compartment membrane; Single-pass type II membrane protein. Note: From ER, targeted to vacuolar lumen at the MVB vesicles via the Golgi and the prevacuolar compartment (PVC). Ref.5 Ref.7

Post-translational modification

Glycosylated. Ref.1 Ref.5 Ref.7

Miscellaneous

Present with 3060 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Putative lipase ATG15
PRO_0000090372

Regions

Topological domain1 – 1414Cytoplasmic Ref.7
Transmembrane15 – 3521Helical; Signal-anchor for type II membrane protein
Topological domain36 – 520485Lumenal Ref.7

Sites

Active site3321Charge relay system By similarity

Amino acid modifications

Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis3321S → A: Loss of function. Ref.1 Ref.5

Sequences

Sequence LengthMass (Da)Tools
P25641 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: B56ABAB72B999019

FASTA52058,435
        10         20         30         40         50         60 
MLHKSPSRKR FASPLHLGCI LTLTVLCLIA YYFALPDYLS VGKSSSRGAM DQKSDGTFRL 

        70         80         90        100        110        120 
KSIYRHGVGA NHRLHQRLEV TPEVISAAGM LYQETTTQGQ DFEDQEPLWT TNAEYATTNP 

       130        140        150        160        170        180 
FDFEFELRRM PLLMKRMKER DPEFIESYIY GETYMTEEEE HAMWIDDDIV APNITDRGTV 

       190        200        210        220        230        240 
VSLALMSSNA YVRIPQTGDW RNVTEPWNET EPEDFGWDGD GIRGHVFYNE VENIVVLSIK 

       250        260        270        280        290        300 
GTSAQGLPGS GEDETTGNDK INDNLLFSCC CARVSYLWTT VCDCYVKSYI CDESCLEKEL 

       310        320        330        340        350        360 
RRKDRFYSAV VDIYKGVLKE YPDAAIWVTG HSLGGALASL LGRTFGLPAV AFESPGELLP 

       370        380        390        400        410        420 
SKRLHLPFPP GLPSYMEGIW HFGHNADPIF MGTCNGASSS CSLVGYAMET ACHTGRVCVY 

       430        440        450        460        470        480 
DVVNDKGWSV NMFNHRIHKV IDEVLLGYEQ AAKCVEPEPC VDCYNWKFIP SRDWESSSRL 

       490        500        510        520 
ITKTKSHAAP TTTTRTTATT TSSSTCVGRN WLGFCTKYEL 

« Hide

References

« Hide 'large scale' references
[1]"Degradation of lipid vesicles in the yeast vacuole requires function of Cvt17, a putative lipase."
Teter S.A., Eggerton K.P., Scott S.V., Kim J., Fischer A.M., Klionsky D.J.
J. Biol. Chem. 276:2083-2087(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, GLYCOSYLATION, MUTAGENESIS OF SER-332.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Aut5/Cvt17p, a putative lipase essential for disintegration of autophagic bodies inside the vacuole."
Epple U.D., Suriapranata I., Eskelinen E.-L., Thumm M.
J. Bacteriol. 183:5942-5955(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF SER-332.
[6]"Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae."
Hutchins M.U., Klionsky D.J.
J. Biol. Chem. 276:20491-20498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Intravacuolar membrane lysis in Saccharomyces cerevisiae. Does vacuolar targeting of Cvt17/Aut5p affect its function?"
Epple U.D., Eskelinen E.-L., Thumm M.
J. Biol. Chem. 278:7810-7821(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION.
[8]"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].
[9]"A life-span extending form of autophagy employs the vacuole-vacuole fusion machinery."
Tang F., Watkins J.W., Bermudez M., Gray R., Gaban A., Portie K., Grace S., Kleve M., Craciun G.
Autophagy 4:874-886(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Starvation induced cell death in autophagy-defective yeast mutants is caused by mitochondria dysfunction."
Suzuki S.W., Onodera J., Ohsumi Y.
PLoS ONE 6:E17412-E17412(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"An overexpression screen in Saccharomyces cerevisiae identifies novel genes that affect endocytic protein trafficking."
Arlt H., Perz A., Ungermann C.
Traffic 12:1592-1603(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Profiling lipid-protein interactions using nonquenched fluorescent liposomal nanovesicles and proteome microarrays."
Lu K.Y., Tao S.C., Yang T.C., Ho Y.H., Lee C.H., Lin C.C., Juan H.F., Huang H.C., Yang C.Y., Chen M.S., Lin Y.Y., Lu J.Y., Zhu H., Chen C.S.
Mol. Cell. Proteomics 11:1177-1190(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHOINOSITIDES-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAC42987.1.
BK006937 Genomic DNA. Translation: DAA07540.1.
PIRS19483.
S74292.
RefSeqNP_009994.2. NM_001178779.1.

3D structure databases

ProteinModelPortalP25641.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31044. 50 interactions.
DIPDIP-5001N.
IntActP25641. 5 interactions.
MINTMINT-535113.
STRING4932.YCR068W.

Proteomic databases

PaxDbP25641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR068W; YCR068W; YCR068W.
GeneID850432.
KEGGsce:YCR068W.

Organism-specific databases

CYGDYCR068w.
SGDS000000664. ATG15.

Phylogenomic databases

eggNOGCOG5153.
HOGENOMHOG000034133.
KOK17900.
OMATVVIGIK.
OrthoDBEOG71P2N8.

Enzyme and pathway databases

BioCycYEAST:YCR068W-MONOMER.

Gene expression databases

GenevestigatorP25641.

Family and domain databases

InterProIPR002921. Lipase_3.
[Graphical view]
PfamPF01764. Lipase_3. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966018.

Entry information

Entry nameATG15_YEAST
AccessionPrimary (citable) accession number: P25641
Secondary accession number(s): D6VR71, Q8NIL6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 24, 2003
Last modified: April 16, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

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

Yeast

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

SIMILARITY comments

Index of protein domains and families