ATG15_ASPNC
ID ATG15_ASPNC Reviewed; 595 AA.
AC A2QGD9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Putative lipase atg15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=atg15; ORFNames=An03g02820;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Lipase which is essential for lysis of subvacuolar cytoplasm
CC to vacuole targeted bodies and intravacuolar autophagic bodies.
CC Involved in the lysis of intravacuolar multivesicular body (MVB)
CC vesicles. The intravacuolar membrane disintegration by atg15 is
CC critical to life span extension (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Binds to both phosphatidylinositol (PI) and
CC phosphatidylinositol 3,5-bisphosphate (PIP2). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:P25641}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P25641}. Prevacuolar compartment membrane
CC {ECO:0000250|UniProtKB:P25641}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P25641}. Note=From ER, targeted to vacuolar
CC lumen at the MVB vesicles via the Golgi and the prevacuolar compartment
CC (PVC). {ECO:0000250|UniProtKB:P25641}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AM270049; CAK44586.1; -; Genomic_DNA.
DR RefSeq; XP_001390178.1; XM_001390141.1.
DR AlphaFoldDB; A2QGD9; -.
DR ESTHER; aspnc-atg15; Lipase_3.
DR PaxDb; A2QGD9; -.
DR EnsemblFungi; CAK44586; CAK44586; An03g02820.
DR GeneID; 4980272; -.
DR KEGG; ang:ANI_1_1202034; -.
DR VEuPathDB; FungiDB:An03g02820; -.
DR HOGENOM; CLU_028295_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 6R.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..595
FT /note="Putative lipase atg15"
FT /id="PRO_5000219762"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 42..595
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT ACT_SITE 319
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 595 AA; 64654 MW; EC1983AFC1D703BA CRC64;
MKGLRGHNKK SFWGNTRLSD LLWPVTLLPG LISAYQPVYL GSRQSSPFLP PQIPLGDSPP
LSDTHEFTLR HIFHRGTYQD PDLHRRLDIT PDTRLRAVSD AGIESDVVTP NTPLVASSQP
LIIERLADRR LSVIEEHLVT ARSSGSAVAL SPSDWVMDTL PGPNVTEKKT VVALAMMTAN
DYIEVPGTGD WQDIHGRFNH SGSFGWQGDG LRGHVYADKT NSTVVISLKG TSPALFDGEG
TTTNDKINDN LFFSCCCGQG GSYLWRQVCD CQTTLYNANL TCIVEAMLDE NRYYRASLDL
YSNITEMYPN ANVWLTGHSL GGAVSSLLGL TFGVPVVTFE AVPEALPAAR LGLPSPPGHD
SRYPQSRRNT GSYHFGHTAD PVYMGTCNGV SSVCTWGGYA MESACHTGQM CVYDTVEDKG
WRVGLSKHRI NYVIANVLAG YDDVPPCAPE EECYDCELWK FFRSNGSEIT TTTSATSTST
STTTSRTSTC KTPGWWGCLD QTTTTETTST STSTSTCKTP GWFGCKDPTT TSDITSVPTI
TTTEPPMTST TTCKTPGWFG CKDETTTQVI APAATLTITE PPVTSTTTGK HLGRF
