ATG15_ASPCL
ID ATG15_ASPCL Reviewed; 630 AA.
AC A1C6D6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Putative lipase atg15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=atg15; ORFNames=ACLA_069880;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027045; EAW13957.1; -; Genomic_DNA.
DR RefSeq; XP_001275383.1; XM_001275382.1.
DR AlphaFoldDB; A1C6D6; -.
DR STRING; 5057.CADACLAP00006966; -.
DR ESTHER; aspcl-atg15; Lipase_3.
DR PRIDE; A1C6D6; -.
DR EnsemblFungi; EAW13957; EAW13957; ACLA_069880.
DR GeneID; 4707621; -.
DR KEGG; act:ACLA_069880; -.
DR VEuPathDB; FungiDB:ACLA_069880; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_1_1; -.
DR OMA; WFGCKDE; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000006701; 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..630
FT /note="Putative lipase atg15"
FT /id="PRO_0000317958"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 41..630
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 577..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
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 630 AA; 68898 MW; D43F76BCDDE74A4D CRC64;
MKSSQRRIKR HAMRDMSIST LLLSVVLLPS VVSANDHVYF NPPSPGSPFL GPQIPLTGPP
SLTNEHEFTL RHIYERGTND QPDLHRRLDI KPHTRLWAVS DDGLEKELVT FDTPLVASSS
PLTIQRLADR RPSVIEGYLT AARYNGEAVA LSSSDWVMDT LAGPDVTKKE TVLTFAKMTA
NDYIEEPGTE DWNYIHGRFN YSSSFGWQSD GLRGHIYADT KNNTIVISLK GTSPALFDGA
GTTTNDKIND NLFFSCCCGQ GGSYLWRQVC DCQQSAFTAN LTCIAEAMND ENKYYRAAID
LYTNVTDMYP DANVWMTGHS LGGAMSSLLG LTFGLPVVTF EAVPEALPAA RLGLPSPPGH
DPRLPQTRKY TGTYHFGHTA DPVYMGTCNG VGSICTWGGY AMESACHTGQ MCVYDTVEDK
GWRVALSTHR IKAVISDVLE VYDNVPPCAA EEECYDCELW KFFRSNGSET TTTSRTSTTT
TPTTTRTLTC ETPGWWGCLD ESTTTTATTA TSTTTTTSTC KTPGWFGCKD STTTVDATAA
PTVTTTIATP TTFPISSTTC KDPGWFGCRD PSSTTASVTA PPFSTSTSSD HVRADHSIGD
GAAHPLTRMY LERLRQVEFA WGSDIEHYEI
