ID A0A0A2LKP5_PENIT Unreviewed; 558 AA.
AC A0A0A2LKP5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=triacylglycerol lipase {ECO:0000256|ARBA:ARBA00013279};
DE EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279};
DE AltName: Full=Autophagy-related protein 15 {ECO:0000256|ARBA:ARBA00029828};
GN ORFNames=PITC_004210 {ECO:0000313|EMBL:KGO77000.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77000.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO77000.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77000.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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 Evidence={ECO:0000256|ARBA:ARBA00001024};
CC -!- SUBUNIT: Binds to both phosphatidylinositol (PI) and
CC phosphatidylinositol 3,5-bisphosphate (PIP2).
CC {ECO:0000256|ARBA:ARBA00011137}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004343}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004343}. Prevacuolar compartment membrane
CC {ECO:0000256|ARBA:ARBA00004270}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004270}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO77000.1}.
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DR EMBL; JQGA01000226; KGO77000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2LKP5; -.
DR STRING; 40296.A0A0A2LKP5; -.
DR HOGENOM; CLU_028295_0_1_1; -.
DR OMA; TYHFGHT; -.
DR OrthoDB; 1027561at2759; -.
DR PhylomeDB; A0A0A2LKP5; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
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.
PE 3: Inferred from homology;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..558
FT /note="triacylglycerol lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002002285"
FT DOMAIN 248..276
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 558 AA; 60072 MW; 250709299D896307 CRC64;
MPRKRSWIKF SVHSLLLSAA GLSSAASASG YYPPSQQLPI IQVPLNGAEV SPDTHEFSLR
HIFHRGTYEQ PELHARLDVK PDTRLRTVSE DGYGEQFIAS ESSLVASSSP LKIQRLVDRR
LSVIEGHLAA ARSSGFAAAL SPLEWAMDTL PGPNITDKQT VLTFAQMTAN DYIEEPGTGQ
WHTIHGKFNY SGSFGWQKDG LRGHIYSDKT NKTVVISLKG TSPALFDGTV ESMTDENRYY
RAAIDLYSNV TEIYPDANIW MTGHSLGGAM TSLVGLTFGL PVVTFEAVPE ALPAARLGLP
SPPGYDPRFP QSRQFTGSYH FGHTADPIYM GTCNGINSIC TWGGYAMESV CHTGQVCTYD
TVADKGWRVG LGTHKIENVI SDVISKYDSV PTCVAEEECF DCELWKFFRS NGSEVTTTTT
TTTTASPTRT STCKTPGWWG CLDDSTTATT TTTTTTSPTS TATTTTCLTP GWFGCNDPTT
TATPAPTVTT TLPSVTATTS CHDPGWFGCR DETSTVATTT ASSASTTSAT CNSPGRVWGC
WDDSTNTPAI TSVPTPTS
//
