ID B8NAY9_ASPFN Unreviewed; 591 AA.
AC B8NAY9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=AFLA_043640 {ECO:0000313|EMBL:EED52662.1}, G4B84_010741
GN {ECO:0000313|EMBL:QMW35250.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED52662.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED52662.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED52662.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW35250.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW35250.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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; EQ963476; EED52662.1; -; Genomic_DNA.
DR EMBL; CP059872; QMW35250.1; -; Genomic_DNA.
DR RefSeq; XP_002377826.1; XM_002377785.1.
DR AlphaFoldDB; B8NAY9; -.
DR STRING; 332952.B8NAY9; -.
DR EnsemblFungi; EED52662; EED52662; AFLA_043640.
DR VEuPathDB; FungiDB:AFLA_007935; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_1_1; -.
DR OMA; CHDCYNW; -.
DR OrthoDB; 1027561at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 7.
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: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 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}; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..591
FT /note="triacylglycerol lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035105559"
FT DOMAIN 286..315
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 591 AA; 63737 MW; 0FC10A83FC99C327 CRC64;
MIISNALLGV ALLPSTAFGL GSVYFGSRGS SPLIPPQVPL AEPPALSGTH EFTLRHIFRR
GAYEQPDLHQ RLDIKPYTRL RTVSEDGLEE GPAILDFPLV ALSRPISIER LADRRPSKIE
AHLMAARSSG SAAVLSPSDW VMDTLAGPDV THKESVLTFA QMTANDYIEE PGSEDWQDVH
GHFNYSSSFG WRGDGLRGHI YADKANSTII ISLKGTSPAL FDGAGTTTND KENDNLFFSC
CCGQGGSYLW RQVCDCQTSA YKANLTCITE AMNDENRYYR AALDLYSNVT ELYPEANVWL
TGHSLGGAMS SLLGLTYGLP VVTFEAVPEA LPAARLGLPS PPGYDPRHPQ SRRYTGAYHF
GHTADPVYMG TCNGVSSVCT WGGYAMESAC HTGQMCVYDT VEDKGWRVGI GTHRIKAVIS
DVIKVYDKVP DCAAEEECYD CVLWKYFRSN GSEITTTSST TSTTSSTPIS TSTCKTPGWW
GCLDESTTTT ATTTSTSTST STCKTPGWFG CNDPTTTADA TTVPSPTTTA PTMTSSTCKT
PGWFGCNDPT TTSKVPQTAP PTLTHTCLTP GYVWGCWDSV TTSSHPITTP P
//
