ID   ATG15_VANPO             Reviewed;         565 AA.
AC   A7TG13;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Putative lipase ATG15;
DE            EC=3.1.1.3;
DE   AltName: Full=Autophagy-related protein 15;
GN   Name=ATG15; ORFNames=Kpol_1028p44;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480385; EDO18770.1; -; Genomic_DNA.
DR   RefSeq; XP_001646628.1; XM_001646578.1.
DR   AlphaFoldDB; A7TG13; -.
DR   STRING; 436907.A7TG13; -.
DR   ESTHER; vanpo-atg15; Lipase_3.
DR   EnsemblFungi; EDO18770; EDO18770; Kpol_1028p44.
DR   GeneID; 5547084; -.
DR   KEGG; vpo:Kpol_1028p44; -.
DR   eggNOG; KOG4540; Eukaryota.
DR   HOGENOM; CLU_028295_0_2_1; -.
DR   InParanoid; A7TG13; -.
DR   OMA; WFGCKDE; -.
DR   OrthoDB; 937562at2759; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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..565
FT                   /note="Putative lipase ATG15"
FT                   /id="PRO_0000317973"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        22..42
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        43..565
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   REGION          488..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        347
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   565 AA;  63915 MW;  77BD72FDCD694A1F CRC64;
     MISNDYTKFS SKRRSLRYSN RILLLMGTIL LIVVYFYSDI LVDKSIIMFR NENKGQMLSG
     SFTLRHIYRH GVDKGHRTQE VLDITKQNED AFGRYFKREL DEFNANAVGL NTDDPLRELW
     TSDKQFITDN PFNFKFGLKG NKQILHRMVD RDPSFIEPYL DFARESPDMA AKVTIDWVEG
     GEVVVVPDIT DKNTVVSLAL MSSNAYVRLP YTDDWRNVSL PWDSNDTPGY GWESNGIRGH
     VFVNDLENIV VISIKGTSAQ GLPGSGEDET TGNDKLNDNL LFSCCCARVS YLWTTVCDCY
     LKSYTCDETC LEQAIKEKDH YYQAAMDIYK DTLRQYPHAT IWLTGHSLGG ALASLVGRTY
     GLPTVAFESP GELLAAKRLH LPFPPGLPSY DEGIWHIGHT ADPIYMGTCN GASSTCSIAG
     YAMETGCHSG KQCVYDVVRD KGWHVNMLNH RIHTVIDGIL TKYDKVATCH EPDPCVDCYN
     WNFMPHGKKP KKQTTSSSSE KVDTSTTKSI DRTTITTRTN EKKWHPNPKD PSTTTTDDKT
     LMSSCLHRNW VGICTEYTTF TKRLI