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P25641

- ATG15_YEAST

UniProt

P25641 - ATG15_YEAST

Protein

Putative lipase ATG15

Gene

ATG15

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (24 Oct 2003)
      Previous versions | rss
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    Functioni

    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.7 Publications

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei332 – 3321Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. triglyceride lipase activity Source: UniProtKB-EC

    GO - Biological processi

    1. autophagy Source: UniProtKB
    2. lipid catabolic process Source: UniProtKB-KW
    3. membrane disassembly Source: UniProtKB
    4. multivesicular body membrane disassembly Source: SGD
    5. piecemeal microautophagy of nucleus Source: SGD
    6. vacuolar protein processing Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Autophagy, Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    BioCyciYEAST:YCR068W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative lipase ATG15 (EC:3.1.1.3)
    Alternative name(s):
    Autophagy-related protein 15
    Cytoplasm to vacuole targeting protein 17
    Gene namesi
    Name:ATG15
    Synonyms:AUT5, CVT17
    Ordered Locus Names:YCR068W
    ORF Names:YCR68W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCR068w.
    SGDiS000000664. ATG15.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB
    4. multivesicular body membrane Source: UniProtKB-SubCell
    5. vacuolar lumen Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi332 – 3321S → A: Loss of function. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 520520Putative lipase ATG15PRO_0000090372Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylated.3 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP25641.
    PaxDbiP25641.

    Expressioni

    Gene expression databases

    GenevestigatoriP25641.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi31044. 58 interactions.
    DIPiDIP-5001N.
    IntActiP25641. 5 interactions.
    MINTiMINT-535113.
    STRINGi4932.YCR068W.

    Structurei

    3D structure databases

    ProteinModelPortaliP25641.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1414Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini36 – 520485Lumenal1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei15 – 3521Helical; Signal-anchor for type II membrane proteinAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5153.
    HOGENOMiHOG000034133.
    KOiK17900.
    OMAiYMGVCNG.
    OrthoDBiEOG71P2N8.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002921. Lipase_3.
    [Graphical view]
    PfamiPF01764. Lipase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25641-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLHKSPSRKR FASPLHLGCI LTLTVLCLIA YYFALPDYLS VGKSSSRGAM    50
    DQKSDGTFRL KSIYRHGVGA NHRLHQRLEV TPEVISAAGM LYQETTTQGQ 100
    DFEDQEPLWT TNAEYATTNP FDFEFELRRM PLLMKRMKER DPEFIESYIY 150
    GETYMTEEEE HAMWIDDDIV APNITDRGTV VSLALMSSNA YVRIPQTGDW 200
    RNVTEPWNET EPEDFGWDGD GIRGHVFYNE VENIVVLSIK GTSAQGLPGS 250
    GEDETTGNDK INDNLLFSCC CARVSYLWTT VCDCYVKSYI CDESCLEKEL 300
    RRKDRFYSAV VDIYKGVLKE YPDAAIWVTG HSLGGALASL LGRTFGLPAV 350
    AFESPGELLP SKRLHLPFPP GLPSYMEGIW HFGHNADPIF MGTCNGASSS 400
    CSLVGYAMET ACHTGRVCVY DVVNDKGWSV NMFNHRIHKV IDEVLLGYEQ 450
    AAKCVEPEPC VDCYNWKFIP SRDWESSSRL ITKTKSHAAP TTTTRTTATT 500
    TSSSTCVGRN WLGFCTKYEL 520
    Length:520
    Mass (Da):58,435
    Last modified:October 24, 2003 - v2
    Checksum:iB56ABAB72B999019
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAC42987.1.
    BK006937 Genomic DNA. Translation: DAA07540.1.
    PIRiS19483.
    S74292.
    RefSeqiNP_009994.2. NM_001178779.1.

    Genome annotation databases

    EnsemblFungiiYCR068W; YCR068W; YCR068W.
    GeneIDi850432.
    KEGGisce:YCR068W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAC42987.1 .
    BK006937 Genomic DNA. Translation: DAA07540.1 .
    PIRi S19483.
    S74292.
    RefSeqi NP_009994.2. NM_001178779.1.

    3D structure databases

    ProteinModelPortali P25641.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31044. 58 interactions.
    DIPi DIP-5001N.
    IntActi P25641. 5 interactions.
    MINTi MINT-535113.
    STRINGi 4932.YCR068W.

    Proteomic databases

    MaxQBi P25641.
    PaxDbi P25641.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR068W ; YCR068W ; YCR068W .
    GeneIDi 850432.
    KEGGi sce:YCR068W.

    Organism-specific databases

    CYGDi YCR068w.
    SGDi S000000664. ATG15.

    Phylogenomic databases

    eggNOGi COG5153.
    HOGENOMi HOG000034133.
    KOi K17900.
    OMAi YMGVCNG.
    OrthoDBi EOG71P2N8.

    Enzyme and pathway databases

    BioCyci YEAST:YCR068W-MONOMER.

    Miscellaneous databases

    NextBioi 966018.

    Gene expression databases

    Genevestigatori P25641.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002921. Lipase_3.
    [Graphical view ]
    Pfami PF01764. Lipase_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiATG15_YEAST
    AccessioniPrimary (citable) accession number: P25641
    Secondary accession number(s): D6VR71, Q8NIL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: October 24, 2003
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 3060 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 III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3