ATG15_YEAST
ID ATG15_YEAST Reviewed; 520 AA.
AC P25641; D6VR71; Q8NIL6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
DE AltName: Full=Cytoplasm to vacuole targeting protein 17;
GN Name=ATG15; Synonyms=AUT5, CVT17; OrderedLocusNames=YCR068W;
GN ORFNames=YCR68W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, GLYCOSYLATION, AND MUTAGENESIS
RP OF SER-332.
RX PubMed=11085977; DOI=10.1074/jbc.c000739200;
RA Teter S.A., Eggerton K.P., Scott S.V., Kim J., Fischer A.M., Klionsky D.J.;
RT "Degradation of lipid vesicles in the yeast vacuole requires function of
RT Cvt17, a putative lipase.";
RL J. Biol. Chem. 276:2083-2087(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF SER-332.
RX PubMed=11566994; DOI=10.1128/jb.183.20.5942-5955.2001;
RA Epple U.D., Suriapranata I., Eskelinen E.-L., Thumm M.;
RT "Aut5/Cvt17p, a putative lipase essential for disintegration of autophagic
RT bodies inside the vacuole.";
RL J. Bacteriol. 183:5942-5955(2001).
RN [6]
RP FUNCTION.
RX PubMed=11264288; DOI=10.1074/jbc.m101150200;
RA Hutchins M.U., Klionsky D.J.;
RT "Vacuolar localization of oligomeric alpha-mannosidase requires the
RT cytoplasm to vacuole targeting and autophagy pathway components in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:20491-20498(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=12499386; DOI=10.1074/jbc.m209309200;
RA Epple U.D., Eskelinen E.-L., Thumm M.;
RT "Intravacuolar membrane lysis in Saccharomyces cerevisiae. Does vacuolar
RT targeting of Cvt17/Aut5p affect its function?";
RL J. Biol. Chem. 278:7810-7821(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION.
RX PubMed=18690010; DOI=10.4161/auto.6556;
RA Tang F., Watkins J.W., Bermudez M., Gray R., Gaban A., Portie K., Grace S.,
RA Kleve M., Craciun G.;
RT "A life-span extending form of autophagy employs the vacuole-vacuole fusion
RT machinery.";
RL Autophagy 4:874-886(2008).
RN [10]
RP FUNCTION.
RX PubMed=21364763; DOI=10.1371/journal.pone.0017412;
RA Suzuki S.W., Onodera J., Ohsumi Y.;
RT "Starvation induced cell death in autophagy-defective yeast mutants is
RT caused by mitochondria dysfunction.";
RL PLoS ONE 6:E17412-E17412(2011).
RN [11]
RP FUNCTION.
RX PubMed=21777356; DOI=10.1111/j.1600-0854.2011.01252.x;
RA Arlt H., Perz A., Ungermann C.;
RT "An overexpression screen in Saccharomyces cerevisiae identifies novel
RT genes that affect endocytic protein trafficking.";
RL Traffic 12:1592-1603(2011).
RN [12]
RP PHOSPHOINOSITIDES-BINDING.
RX PubMed=22843995; DOI=10.1074/mcp.m112.017426;
RA Lu K.Y., Tao S.C., Yang T.C., Ho Y.H., Lee C.H., Lin C.C., Juan H.F.,
RA Huang H.C., Yang C.Y., Chen M.S., Lin Y.Y., Lu J.Y., Zhu H., Chen C.S.;
RT "Profiling lipid-protein interactions using nonquenched fluorescent
RT liposomal nanovesicles and proteome microarrays.";
RL Mol. Cell. Proteomics 11:1177-1190(2012).
CC -!- FUNCTION: Lipase which is essential for lysis of subvacuolar cytoplasm
CC to vacuole targeted bodies and intravacuolar autophagic bodies.
CC Involved in the lysis of intravacuolar multivesicular body (MVB)
CC vesicles. The intravacuolar membrane disintegration by ATG15 is
CC critical to life span extension. {ECO:0000269|PubMed:11085977,
CC ECO:0000269|PubMed:11264288, ECO:0000269|PubMed:11566994,
CC ECO:0000269|PubMed:12499386, ECO:0000269|PubMed:18690010,
CC ECO:0000269|PubMed:21364763, ECO:0000269|PubMed:21777356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC -!- SUBUNIT: Binds to both phosphatidylinositol (PI) and
CC phosphatidylinositol 3,5-bisphosphate (PIP2).
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000269|PubMed:12499386}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12499386}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:12499386}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12499386}. Note=From ER, targeted to vacuolar lumen
CC at the MVB vesicles via the Golgi and the prevacuolar compartment
CC (PVC). {ECO:0000269|PubMed:12499386}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11085977,
CC ECO:0000269|PubMed:11566994, ECO:0000269|PubMed:12499386}.
CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59720; CAC42987.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07540.1; -; Genomic_DNA.
DR PIR; S19483; S19483.
DR PIR; S74292; S74292.
DR RefSeq; NP_009994.2; NM_001178779.1.
DR AlphaFoldDB; P25641; -.
DR BioGRID; 31044; 318.
DR DIP; DIP-5001N; -.
DR IntAct; P25641; 7.
DR MINT; P25641; -.
DR STRING; 4932.YCR068W; -.
DR ESTHER; yeast-ATG15; Lipase_3.
DR TCDB; 8.A.178.1.1; the lipase atg15 (atg15) family.
DR MaxQB; P25641; -.
DR PaxDb; P25641; -.
DR PRIDE; P25641; -.
DR EnsemblFungi; YCR068W_mRNA; YCR068W; YCR068W.
DR GeneID; 850432; -.
DR KEGG; sce:YCR068W; -.
DR SGD; S000000664; ATG15.
DR VEuPathDB; FungiDB:YCR068W; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_2_1; -.
DR InParanoid; P25641; -.
DR OMA; WFGCKDE; -.
DR BioCyc; YEAST:YCR068W-MON; -.
DR PRO; PR:P25641; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25641; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005775; C:vacuolar lumen; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0030397; P:membrane disassembly; IDA:UniProtKB.
DR GO; GO:0034496; P:multivesicular body membrane disassembly; IMP:SGD.
DR GO; GO:0046461; P:neutral lipid catabolic process; IMP:SGD.
DR GO; GO:0000425; P:pexophagy; IMP:SGD.
DR GO; GO:0006660; P:phosphatidylserine catabolic process; IDA:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0006624; P:vacuolar protein processing; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Autophagy; Endosome; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Putative lipase ATG15"
FT /id="PRO_0000090372"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12499386"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 36..520
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:12499386"
FT ACT_SITE 332
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 332
FT /note="S->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:11085977,
FT ECO:0000269|PubMed:11566994"
SQ SEQUENCE 520 AA; 58435 MW; B56ABAB72B999019 CRC64;
MLHKSPSRKR FASPLHLGCI LTLTVLCLIA YYFALPDYLS VGKSSSRGAM DQKSDGTFRL
KSIYRHGVGA NHRLHQRLEV TPEVISAAGM LYQETTTQGQ DFEDQEPLWT TNAEYATTNP
FDFEFELRRM PLLMKRMKER DPEFIESYIY GETYMTEEEE HAMWIDDDIV APNITDRGTV
VSLALMSSNA YVRIPQTGDW RNVTEPWNET EPEDFGWDGD GIRGHVFYNE VENIVVLSIK
GTSAQGLPGS GEDETTGNDK INDNLLFSCC CARVSYLWTT VCDCYVKSYI CDESCLEKEL
RRKDRFYSAV VDIYKGVLKE YPDAAIWVTG HSLGGALASL LGRTFGLPAV AFESPGELLP
SKRLHLPFPP GLPSYMEGIW HFGHNADPIF MGTCNGASSS CSLVGYAMET ACHTGRVCVY
DVVNDKGWSV NMFNHRIHKV IDEVLLGYEQ AAKCVEPEPC VDCYNWKFIP SRDWESSSRL
ITKTKSHAAP TTTTRTTATT TSSSTCVGRN WLGFCTKYEL
