ID   ATG15_ASPFU             Reviewed;         650 AA.
AC   Q4X180;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Putative lipase atg15;
DE            EC=3.1.1.3;
DE   AltName: Full=Autophagy-related protein 15;
GN   Name=atg15; ORFNames=AFUA_2G10900;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000001; EAL93385.1; -; Genomic_DNA.
DR   RefSeq; XP_755423.1; XM_750330.1.
DR   AlphaFoldDB; Q4X180; -.
DR   STRING; 746128.CADAFUBP00002609; -.
DR   ESTHER; aspfu-atg15; Lipase_3.
DR   EnsemblFungi; EAL93385; EAL93385; AFUA_2G10900.
DR   GeneID; 3513512; -.
DR   KEGG; afm:AFUA_2G10900; -.
DR   VEuPathDB; FungiDB:Afu2g10900; -.
DR   eggNOG; KOG4540; Eukaryota.
DR   HOGENOM; CLU_028295_0_1_1; -.
DR   InParanoid; Q4X180; -.
DR   OMA; WFGCKDE; -.
DR   OrthoDB; 937562at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR   GO; GO:0034496; P:multivesicular body membrane disassembly; IBA:GO_Central.
DR   GO; GO:0046461; P:neutral lipid catabolic process; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
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..650
FT                   /note="Putative lipase atg15"
FT                   /id="PRO_0000090364"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..650
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        320
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        466
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   650 AA;  70250 MW;  6B0C115DBF6141AA CRC64;
     MKSSRKRTKR RVLQDMSISG LLLSVALLPS VVSAQDHVYL DPSSSGSPYL GPQIPLTGLP
     ALTGTHEFTL RHIYQRGTHD QPDLHRRLDI KPHTRLWAVS DDGLEKELVT FDTPLVASSS
     PLTIQRLADR RLSVIEGYLA AARSRGEAVA LSPSEWVMDT LAGPNVTDKE SVLTFAKMTA
     NDYIEEPGSG DWHYIHGRFN YSSSFGWQSD GLRGHIYADK TNSTIVISLK GTSPALFDGA
     GTTTNDKIND NLFFSCCCGQ GGSYLWRQVC DCQQSAFTAN LTCIVEAMND ENRYYRAAID
     LYSNVTDMYP DANVWLTGHS LGGAMSSLLG LTFGLPVVTF EAVPEALPAA RLGLPSPPGH
     DPRLPQSRQY TGAYHFGHTA DPVYMGTCNG VGSICTWGGY AMESACHTGQ MCVYDTVEDK
     GWRVALSTHR IEAVISDVLE VYEDIPPCAP EEECYDCELW KFFKSNGSES TTTSTTTTTT
     APTTTRTSTC KTPGWWGCLD ESTTTTTTTS TTTTTTTTTT STCKTPGWFG CKDPTTTTEA
     TAAPSVTTSI PTPTTYPTSS TSTCKDPGWF GCRDPPSTTA SITSSPSTTS TCDDPGFFWG
     CYDESTTATH PITSGPSAPY STPSPTHEHT CTSSIFFGLI CVGSTGTELR