ID   ATG15_KLULA             Reviewed;         531 AA.
AC   Q6CU02;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Putative lipase ATG15;
DE            EC=3.1.1.3;
DE   AltName: Full=Autophagy-related protein 15;
GN   Name=ATG15; OrderedLocusNames=KLLA0C08679g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382123; CAH01438.1; -; Genomic_DNA.
DR   RefSeq; XP_452587.1; XM_452587.1.
DR   AlphaFoldDB; Q6CU02; -.
DR   STRING; 28985.XP_452587.1; -.
DR   ESTHER; klula-q6cu02; Lipase_3.
DR   PRIDE; Q6CU02; -.
DR   EnsemblFungi; CAH01438; CAH01438; KLLA0_C08679g.
DR   GeneID; 2892241; -.
DR   KEGG; kla:KLLA0_C08679g; -.
DR   eggNOG; KOG4540; Eukaryota.
DR   HOGENOM; CLU_028295_0_2_1; -.
DR   InParanoid; Q6CU02; -.
DR   OMA; WFGCKDE; -.
DR   Proteomes; UP000000598; Chromosome C.
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:0005775; C:vacuolar lumen; IEA:EnsemblFungi.
DR   GO; GO:0004620; F:phospholipase activity; IEA:EnsemblFungi.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034496; P:multivesicular body membrane disassembly; IEA:EnsemblFungi.
DR   GO; GO:0046461; P:neutral lipid catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR   GO; GO:0006660; P:phosphatidylserine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006624; P:vacuolar protein processing; IEA:EnsemblFungi.
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; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..531
FT                   /note="Putative lipase ATG15"
FT                   /id="PRO_0000090369"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..531
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          482..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        340
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   531 AA;  58819 MW;  234A7D25A1E891E2 CRC64;
     MKPGIKISKR YSARNASVIT VLLLLIYLIY INKETIQTKY QGSRINHDSG GDSTKDKTHT
     FTIKEIHFRP LDEKTQSYGS LQVTPEFVNM AKSEFEQNVA VASGDNEDLY DKQLWSASIK
     SNPWTHQFTL KQGSIKMKRM VNRDPDYVES FLDYAHENPE MARKVHLDWV DESVLAPNVT
     DKETVISLAL MSSNAYVRLP YEGDWRNLSD WNNDLNPDLS VGIGWDSDGV RGHIFSNDDS
     SVIVIALKGT SAQGLPGSGE DETTDNDKLN DNVLFSCCCA RVSYLWKTAC DCYVKSYTCD
     EKCLEQELVR KDRYYQAVLD IYRSVVTAHP NSAIWITGHS LGGALASLLG RTFGAPAVAF
     EAPGELLATK RLHLPMPPGL PAYQEGVWHI GHTADPIFMG TCNGASSSCS IAGYAMETSC
     HSGKVCVYDV VTDKGWHVNM LNHRIHTVID GILTDYDTVA KCKTPDACHD CFNWNYVKGR
     DVPKKHKSSS STASSTSAET STLTVGPSPP EKTTTSCIGR NWIGICTEYG I