ID A0A167Y174_9HYPO Unreviewed; 640 AA.
AC A0A167Y174;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AAL_06960 {ECO:0000313|EMBL:KZZ90734.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ90734.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ90734.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ90734.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ90734.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGY01000020; KZZ90734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167Y174; -.
DR STRING; 1081109.A0A167Y174; -.
DR OrthoDB; 1027561at2759; -.
DR Proteomes; UP000078544; 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:UP000078544};
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..640
FT /note="triacylglycerol lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007894579"
FT DOMAIN 294..328
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 563..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 68860 MW; 4CB3CF5B2ECB425F CRC64;
MPVSINSPLA GRTLTTFILS LLATFSPISA SRQHAGYQDS VGQEVLLPPT IGAPHLEAPQ
PADHTFTLRH LYHHGTRRHP QLHRRLDVAQ GTSARVFLAA EDGHEEYDVP RLRAKSVANS
IQRLVDRRPS VVDPMIAHAR ALGFAAVLDA SAWTLDELPS PDVTDKGTVV SLAYMAADAY
VETDTRPDWE EIGEPFNKSA DFGWQSDGLR GHIWADESNS TVVIGLKGTS PAVFDGDGTT
TNDKINDNLF FSCCCAQQGQ WTWHQVCDCA TGTYACNGTC VTKALREEDR YYGAARELYS
NVTELYPEST IWIVGHSLGG AVSSLLGLTY GLPVVTFEAV PEALAATRLG LPIPPGTDPA
APQTRQNTGA FHFGHTADPI YIGTCNGATA SCSFAGYAME STCHTGSECV YDVVSDKGWR
VGIGTHKIRA VISDVILKYD DVPQCTSTPD CRDCAQWKFY ESNGTETTTT SISSTTTRTR
TRTSTCKTPG WWGCLDTTTT TSETSTSTSV STSTCKTPGW FGCKDKTTTT SIVTTPGPTT
TAHSTPAPTT TCETPGRFWG CWDGEQTSTT SDIPTRPSLT GAPIATSTGG RPALSTSAPS
SPVDDAVPSE RKCLRRNFLG MCTEWQTDGG NAAEPYWEEI
//
