ID   ATG15_YEAS7             Reviewed;         520 AA.
AC   A6ZTP2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 55.
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; ORFNames=SCY_0635;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity). {ECO:0000250}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC       {ECO:0000250|UniProtKB:P25641}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P25641}. Prevacuolar compartment membrane
CC       {ECO:0000250|UniProtKB:P25641}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P25641}. Note=From ER, targeted to vacuolar
CC       lumen at the MVB vesicles via the Golgi and the prevacuolar compartment
CC       (PVC). {ECO:0000250|UniProtKB:P25641}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFW02000089; EDN62181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZTP2; -.
DR   ESTHER; yeast-ATG15; Lipase_3.
DR   EnsemblFungi; EDN62181; EDN62181; SCY_0635.
DR   HOGENOM; CLU_028295_0_2_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Autophagy; Endosome; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..520
FT                   /note="Putative lipase ATG15"
FT                   /id="PRO_0000317974"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
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:0000250"
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"
SQ   SEQUENCE   520 AA;  58423 MW;  FAAA49BB1B5A9845 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 VCDCYVKSYT CDESCLEKEL
     RRKDRFYSAV VDIYKGVLKE YPDAAIWVTG HSLGGALASL LGRTFGLPAV AFESPGELLP
     SKRLHLPFPP GLPSYMEGIW HFGHNADPIF MGTCNGASSS CSLVGYAMET ACHTGRVCVY
     DVVNDKGWSV NMFNHRIHKV IDEVLLGYEQ AAKCVEPEPC VDCYNWKFIP SRDWESSSRL
     ITKTKSHAAP TTTTRTTATT TSSSTCVGRN WLGFCTKYEL