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Database: UniProt
Entry: A0A067NZW0_PLEOS
LinkDB: A0A067NZW0_PLEOS
Original site: A0A067NZW0_PLEOS 
ID   A0A067NZW0_PLEOS        Unreviewed;       439 AA.
AC   A0A067NZW0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=PLEOSDRAFT_1032173 {ECO:0000313|EMBL:KDQ33424.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ33424.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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}.
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DR   EMBL; KL198004; KDQ33424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067NZW0; -.
DR   STRING; 1137138.A0A067NZW0; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_1032173; -.
DR   HOGENOM; CLU_028295_1_1_1; -.
DR   InParanoid; A0A067NZW0; -.
DR   OrthoDB; 1027561at2759; -.
DR   Proteomes; UP000027073; Unassembled WGS sequence.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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:UP000027073};
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..439
FT                   /note="triacylglycerol lipase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001647127"
FT   DOMAIN          224..251
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
FT   REGION          278..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  48742 MW;  CF48C2D707619DD1 CRC64;
     MLPALFLSLL ILTSAADARH VHFNIQHPLL LDQYPTPTPI SQSLLARPTT VYRPRDPAAL
     DRARIRSLRY GQSEPLEWYE KEVLAPDIED RHTIEQLARM AGNAYALPGQ KNWYDVDTAW
     NTSFPFGWED HANGFRGNVF LSSDNSTVVL SIKGTTIQGP TSKKDKFNDN LLFSCCCARV
     DFSWVFRTVC DCYANHWKCD DTCLSDALIQ DSLFYTTGVK LVMDLTFLYP SANIWLVGHS
     LGGSLASLLG ATFGLPAIAF EAPGERLAAQ RLHLPLPPPV SSPNSTTPPS PTASLLPNRP
     RIRIPSTAPL PVTHIYHTAD PIPQGTCTGP LSPCAQGGYA LETRCHLGKS IVYDTVGVLG
     WRVDIRKHVI REVVEKVLGW EDGWPDEDAE GEAASETEMS RNVPRAKEEV DCTDCFKWEF
     GHFKDVPPPE DFNPKTIDI
//
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