ATG15_CANGA
ID ATG15_CANGA Reviewed; 504 AA.
AC Q6FPI6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; OrderedLocusNames=CAGL0J03542g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380956; CAG60807.1; -; Genomic_DNA.
DR RefSeq; XP_447858.1; XM_447858.1.
DR AlphaFoldDB; Q6FPI6; -.
DR STRING; 5478.XP_447858.1; -.
DR ESTHER; canga-q6fpi6; Lipase_3.
DR EnsemblFungi; CAG60807; CAG60807; CAGL0J03542g.
DR GeneID; 2889699; -.
DR KEGG; cgr:CAGL0J03542g; -.
DR CGD; CAL0132884; CAGL0J03542g.
DR VEuPathDB; FungiDB:CAGL0J03542g; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_2_1; -.
DR InParanoid; Q6FPI6; -.
DR OMA; WFGCKDE; -.
DR Proteomes; UP000002428; Chromosome J.
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..504
FT /note="Putative lipase ATG15"
FT /id="PRO_0000090366"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..504
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 458..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 504 AA; 56503 MW; 1AFC76CEF0B16FEB CRC64;
MLGRQVTMLL KVIVAVAVLF VWHRSRDSSR GDGSNGDGLS DSSGNGFRLE HIWAYDPEDV
VSSCVDVSEE MRVSADEYVS MESGSEFVES WWAKTGARPF SHVFDLRSRS MDIQRLQDRD
PVSMEKYIDF SLENPELART IELEWETAKI QVPDVRNRNT VLALALMSSN AYVRTPYTGD
WRNLSSSWGH TGEEKFGWDK DGLRGHIFVN KITKVVVIAI KGTSSQGLFG SGEEDTITND
KINDNLLFSC CCARISYLWT TVCDCYMKSY TCDENCVEAE LKRKDRYYAA TLKLYKQVTE
MYPDSAIWLT GHSLGGALAA LLGRTYGVPA VTFEAPGELL PAKRLHLPLP PGLPDYEEAI
WHFGHNADPI FMGTCNGASS SCSIGGYAME TACHSGQYCM YDVVNDKGWR VNLLNHRIHR
VIDEVILEYG RPAKCQRAPT CIDCYNWKFV NKRRNRREES SSSIASSSQL TSSHSESETL
TSTDAPEKTC IGRNWLGICT DYGV
