ID   ATG15_NEOFI             Reviewed;         634 AA.
AC   A1DH10;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Putative lipase atg15;
DE            EC=3.1.1.3;
DE   AltName: Full=Autophagy-related protein 15;
GN   Name=atg15; ORFNames=NFIA_086220;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW18667.1; -; Genomic_DNA.
DR   RefSeq; XP_001260564.1; XM_001260563.1.
DR   AlphaFoldDB; A1DH10; -.
DR   STRING; 36630.CADNFIAP00007612; -.
DR   ESTHER; neofi-atg15; Lipase_3.
DR   EnsemblFungi; EAW18667; EAW18667; NFIA_086220.
DR   GeneID; 4587122; -.
DR   KEGG; nfi:NFIA_086220; -.
DR   VEuPathDB; FungiDB:NFIA_086220; -.
DR   eggNOG; KOG4540; Eukaryota.
DR   HOGENOM; CLU_028295_0_1_1; -.
DR   OMA; WFGCKDE; -.
DR   OrthoDB; 937562at2759; -.
DR   Proteomes; UP000006702; 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: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.
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..634
FT                   /note="Putative lipase atg15"
FT                   /id="PRO_0000317965"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        26..634
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   REGION          518..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   634 AA;  68394 MW;  349855D3C98461E2 CRC64;
     MSISGLLLSV ALLPSVVSAH DHVYFDPPSS GSPFLGPQIP LTGPPALTGT HEFTLRHIYQ
     RGTRDQPDLH RRLDIKPHTR LWAVSDDGLE KELVTFDTPL VASSSPLTIQ RLADRRLSVI
     EGYLAAARSS GEAVALSPSE WVMDTLAGPN VTDKESVLTF AKMTANDYIE EPGTEDWHYI
     HGRFNYSSSF GWQSDGLRGH IYADKTNSTI VISLKGTSPA LFDGAGTTTN DKINDNLFFS
     CCCGQGGSYL WRQVCDCQQS AFTANLTCIV EAMNDENRYY RAAIDLYSNV TDMYPDANVW
     MTGHSLGGAM SSLLGLTFGL PVVTFEAVPE ALPAARLGLP SPPGHDPRLP QSRQYTGAYH
     FGHTADPVYM GTCNGVGSIC TWGGYAMESA CHTGQMCVYD TVEDKGWRVA LSTHRIRAVI
     SDVLEVYEDL PPCAPEEECY DCELWKFFKS NGSESTTTST TTTTTAPTTT RTSTCKTPGW
     WGCLDESTTT TTITSTTTTT TTSTSTCKTP GWFGCKDPTT TTEATPAPSV TTTIPTPTTY
     PTSSTSTCKD PGWFGCRDPS STTASITSSP STTSTCDDPG FFWGCYDEST TATHPITPGP
     SAPYSTPSPT NKHTCTSSIF FGLICVGSTG TELR