ID M3D268_SPHMS Unreviewed; 659 AA.
AC M3D268;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=SEPMUDRAFT_126805 {ECO:0000313|EMBL:EMF11222.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF11222.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF11222.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF11222.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB456266; EMF11222.1; -; Genomic_DNA.
DR RefSeq; XP_016759343.1; XM_016902104.1.
DR AlphaFoldDB; M3D268; -.
DR STRING; 692275.M3D268; -.
DR GeneID; 27899241; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_1_1; -.
DR OMA; TYHFGHT; -.
DR OrthoDB; 1027561at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:EMF11222.1};
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:UP000016931};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..659
FT /note="triacylglycerol lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004032167"
FT DOMAIN 288..321
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 457..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 71471 MW; 085494A7AC4B70BD CRC64;
MCSRSLLVVG LLVFFAGLIH SADAARPAHL RAPSQVVLPP LLGGGVSSGK GSRDLGERVF
KLRHIYHHGT HKYPDLHRYT DIEPEAKLRV TYDDGRTIED APNELRAQAV TTNIQRLVAR
NKTDIDDLLA ESAWYGRAAD LPASAWTSDE IAGPNISDKS TVITFAKMAA NAYVQTRLDG
AWLPVKGGFN YTDDFGWQTD GLRGHIFADE SNSTVVIGLK GTSPAIFDGA DTTGNDKLND
NLFGSCCCGQ GGQYLWKQVC DCMTGTYQCN STCLVKSLQT KSHYYWAVRD LYHNVTERYP
NSDVWLSGHS LGGVVSSLLG LTYGLPTMTF EAFPDAMAAS RLGLPTPPGY QIGSHQSRSD
VQLHHFGHTA DPIYMGTCNA ASSFCTIAGY AFQGVCHTGK TCTYDTVGDL GWRVGIGTHK
IVNVIKDVLE KYDTVPTCEA DEECVDCYNW KFYESNGTES TTTSSSSSTS TTTRTRTETC
KTPGWFGCLD ESTTTTTTTS TSSTSSTSTS TCHTPGWFGC KDESTTTSAA TITTTSAAPG
STTTVITTTS KSTSTCTPGF FWGCDDEPST TTSATPKPSR TSSHASSTTS APDDKDDCTS
REFFGLICVD PSPPTTNLVT PSPTRLPTTK RKHCVGRHWY GSCKEWRWEH TLDPKWDLL
//
