ID   ATG15_PICGU             Reviewed;         566 AA.
AC   A5DC90;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   02-SEP-2026, entry version 89.
DE   RecName: Full=Putative lipase ATG15;
DE            EC=3.1.1.3;
DE   AltName: Full=Autophagy-related protein 15;
GN   Name=ATG15; ORFNames=PGUG_00895;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408155; EDK36797.2; -; Genomic_DNA.
DR   RefSeq; XP_001487518.2; XM_001487468.1.
DR   AlphaFoldDB; A5DC90; -.
DR   FunCoup; A5DC90; 65.
DR   STRING; 294746.A5DC90; -.
DR   ESTHER; picgu-atg15; ATG15-related-lipase.
DR   GlyCosmos; A5DC90; 3 sites, No reported glycans.
DR   GeneID; 5128702; -.
DR   KEGG; pgu:PGUG_00895; -.
DR   eggNOG; KOG4540; Eukaryota.
DR   HOGENOM; CLU_028295_0_2_1; -.
DR   InParanoid; A5DC90; -.
DR   OMA; TYHFGHT; -.
DR   OrthoDB; 58570at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005775; C:vacuolar lumen; IEA:TreeGrafter.
DR   GO; GO:0004620; F:glycerophospholipase activity; IEA:TreeGrafter.
DR   GO; GO:0004806; F:triacylglycerol lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034496; P:multivesicular body membrane disassembly; IEA:TreeGrafter.
DR   GO; GO:0046461; P:neutral lipid catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006660; P:phosphatidylserine catabolic process; IEA:TreeGrafter.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:TreeGrafter.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR050805; ATG15_Lipase.
DR   InterPro; IPR002921; Fungal_lipase-type.
DR   PANTHER; PTHR47175; LIPASE ATG15-RELATED; 1.
DR   PANTHER; PTHR47175:SF2; LIPASE ATG15-RELATED; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..566
FT                   /note="Putative lipase ATG15"
FT                   /id="PRO_0000317970"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        18..38
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        39..566
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   REGION          507..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..543
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        366
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   566 AA;  64076 MW;  4E888F2055B87459 CRC64;
     MGSKHKKNAS KSLRAFSFII LSASIALVYI FNPVKLIFPS SIIRFHHGLP PQSQEIVTEQ
     PKSHSKFQLK HIYHHGSGKN YKIHRRLDIT PEYLAKHDAY FQHFNQLQSG TEQVSLDNLD
     SVVAQYDWPK HHQGKNPWTI ELPMKIAKRP AVRLKQRHDH NYIDSYLQYA LSVKSNPQHI
     NNVQLEWISE DISVPDVKDR DTVVSLATIS SNAYVRFPKD DDEKKNSDWI DVGEPWVPDD
     RNNNIEFGWG DDGLRGHIFV SEDNKTVVIG VKGTSGAGLP GSGSEETQAN DKTNDNLLFS
     CCCARISYMW TTVCDCYEKT YTCNQDCLEK ELVRKDRYYQ AVLDLYRNVT EIYPSESHDI
     WVTGHSLGGA LASLLGRTYG LPVVAYEAPG EMLATQRLHL PQPPGLPKHA ENIWHFGNTA
     DPIFMGVCNG ASSSCNLAGY ALETACHTGR QCVYDVVTDK GWHVNLLNHR IHTVIDDIIM
     TYNDTAPCAD QPPCRDCFNW RFTSRDDSLD DEPPLPNPLR PGKPSTTSSS QHHTSTTTTT
     ETSRPQKCLK RTWYGWCVEW GDEEDA
//