ATG15_YARLI
ID ATG15_YARLI Reviewed; 549 AA.
AC Q6C2N7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; OrderedLocusNames=YALI0F06358g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382132; CAG77882.2; -; Genomic_DNA.
DR RefSeq; XP_505075.2; XM_505075.2.
DR AlphaFoldDB; Q6C2N7; -.
DR STRING; 4952.CAG77882; -.
DR ESTHER; yarli-atg15; Lipase_3.
DR EnsemblFungi; CAG77882; CAG77882; YALI0_F06358g.
DR GeneID; 2908407; -.
DR KEGG; yli:YALI0F06358g; -.
DR VEuPathDB; FungiDB:YALI0_F06358g; -.
DR HOGENOM; CLU_028295_0_2_1; -.
DR InParanoid; Q6C2N7; -.
DR OMA; CYEKTYT; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0034496; P:multivesicular body membrane disassembly; IBA:GO_Central.
DR GO; GO:0046461; P:neutral lipid catabolic process; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
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..549
FT /note="Putative lipase ATG15"
FT /id="PRO_0000090371"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..549
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 474..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 549 AA; 61062 MW; 1B426DD67E8D4298 CRC64;
MKQDLYKESS PPPSTTKSKG LYVIVAALVT TAIYLLYSQG YSNTHGEKDM PSVVPNLVLP
ANPSSDHSFA VKHIYHHNTE ADANHGRMDV SGEWVRAAQK AQHLNLGQDT HRYMASNARD
PYTNLPLKSR TQKVKRWRQR DPDHVESYLE AARLNPQLYG AMDFDWVEED ILVPDVTDRD
TVVSLAVMAS NAYVDVPFTG DWTNVSWKET GGIGWQSDGV RGHIFVDQTP GSPLVVIALK
GTSAAIFDSG GDTVINDKTN DNLLFSCCCA RVSYLWNTVC DCYTGESYTC DQECLEKELY
AEDRYYRAVL DIYRNVTHLY PQKQIWVTGH SLGGALSAML GRTYGIPAVG YEAPGELLPT
KRLHLPSPPG IPWSQEHIWH FGHTADPIFM GVCNGASSSC SIGGYAMETS CHSGLQCMYD
VVTDKGWHLS MVNHRIHTVI DEVLLAYNET AACVPPPPCQ DCFNWNFVMG NDKDDDDKDK
KKKKKTSTSS SVVSKTKTST SSTVATNTMP SLPDPTCVER NWYGKCIRYD PEIKQQYGDS
HTVTHVTMA
