ATG15_PICST
ID ATG15_PICST Reviewed; 628 AA.
AC A3LV34;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; ORFNames=PICST_89908;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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; CP000499; ABN67059.2; -; Genomic_DNA.
DR RefSeq; XP_001385088.2; XM_001385051.1.
DR AlphaFoldDB; A3LV34; -.
DR STRING; 4924.XP_001385088.2; -.
DR ESTHER; picst-atg15; Lipase_3.
DR PRIDE; A3LV34; -.
DR EnsemblFungi; ABN67059; ABN67059; PICST_89908.
DR GeneID; 4839141; -.
DR KEGG; pic:PICST_89908; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_2_1; -.
DR InParanoid; A3LV34; -.
DR OMA; CYEKTYT; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000002258; Chromosome 5.
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:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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..628
FT /note="Putative lipase ATG15"
FT /id="PRO_0000317971"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..53
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 54..628
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 540..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 70605 MW; 9EF132D20C6DB3E4 CRC64;
MLAAEKRRLL HKTRPVSASE KPGSIYPQRA LYLLVCFSIA TISLGYLHFI GAIDIGRFGI
SSVISDLTKQ DAVSEPFSLH KEQTSSVHTE SDEQTFELKH IFHHGTGPEN YRLHRRLDIT
PSYLAKHSSY FADFSQRLAQ KRDDSSVDSE NLEDIYNLMD WPDVHKHKNP FTIQLPIKKD
HKKGKVVRLK DRHEPGFLDS YLSYALQVKG DPKILNRIAL EWEDEIEIDI PNMKDKDTLV
SLATISSNAY VKFPKDENEK NKSDWIDVGQ WEPDQENVDL NFGWEDIGLR GHVFVSKDNK
TVVIGIKGTS GAGLPGGGSD ETAGNDKDND NLLFSCCCAR VGYMWTTVCN CYEKTYTCNQ
DCLEKELLRE DKYYQAVLDL YRNVSAIYPP ETTNVWVTGH SLGGALASLL GRTYGLPVVA
FEAPGEMLAT KRLHLPQPPG IPKFMENIWH VGNTADPIYM GVCNGASSTC NVAGYAMETA
CHTGYQCVYD VVTDLGWRVN LLNHRIHTVI DDIILAYNDT AQCIEQPPCR DCFNWRFTSH
DDDVPDEPEM PNPLRPKPKP KPSSSTSDGK NNRISSTATT TISPTSRKAD PTSSDISEPS
ESPKKCLERT WYGWCSKWGY DGDVDDDQ
