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P25641

- ATG15_YEAST

UniProt

P25641 - ATG15_YEAST

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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

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
Complete GO annotation...

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 Source: UniProtKB-KW
  2. endosome Source: UniProtKB-KW
  3. Golgi apparatus Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB
  5. vacuolar lumen Source: UniProtKB
Complete GO annotation...

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.
InParanoidiP25641.
KOiK17900.
OMAiYMGVCNG.
OrthoDBiEOG71P2N8.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
[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

        10         20         30         40         50
MLHKSPSRKR FASPLHLGCI LTLTVLCLIA YYFALPDYLS VGKSSSRGAM
60 70 80 90 100
DQKSDGTFRL KSIYRHGVGA NHRLHQRLEV TPEVISAAGM LYQETTTQGQ
110 120 130 140 150
DFEDQEPLWT TNAEYATTNP FDFEFELRRM PLLMKRMKER DPEFIESYIY
160 170 180 190 200
GETYMTEEEE HAMWIDDDIV APNITDRGTV VSLALMSSNA YVRIPQTGDW
210 220 230 240 250
RNVTEPWNET EPEDFGWDGD GIRGHVFYNE VENIVVLSIK GTSAQGLPGS
260 270 280 290 300
GEDETTGNDK INDNLLFSCC CARVSYLWTT VCDCYVKSYI CDESCLEKEL
310 320 330 340 350
RRKDRFYSAV VDIYKGVLKE YPDAAIWVTG HSLGGALASL LGRTFGLPAV
360 370 380 390 400
AFESPGELLP SKRLHLPFPP GLPSYMEGIW HFGHNADPIF MGTCNGASSS
410 420 430 440 450
CSLVGYAMET ACHTGRVCVY DVVNDKGWSV NMFNHRIHKV IDEVLLGYEQ
460 470 480 490 500
AAKCVEPEPC VDCYNWKFIP SRDWESSSRL ITKTKSHAAP TTTTRTTATT
510 520
TSSSTCVGRN WLGFCTKYEL
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.
InParanoidi P25641.
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. Fungal_lipase-like.
[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

« Hide 'large scale' publications
  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 29, 2014
This is version 110 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