ID   ATG15_PICAN             Reviewed;         536 AA.
AC   A7KAJ9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Putative lipase ATG15;
DE            EC=3.1.1.3;
DE   AltName: Full=Autophagy-related protein 15;
GN   Name=ATG15;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(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       ECO:0000269|PubMed:17204848}.
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; EF107721; ABO31059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KAJ9; -.
DR   ESTHER; pican-atg15; Lipase_3.
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; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..536
FT                   /note="Putative lipase ATG15"
FT                   /id="PRO_0000317969"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        9..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        32..536
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        309
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        516
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   536 AA;  60260 MW;  0CDAF454A79D4330 CRC64;
     MGNPTLMRWP VTRILVLGLV VTVLYKAMAI YSSRRAPVQV CFTSPSSAFK IKHIFHNAAD
     GRTHKRLDID DEFLSIYNSA RSQMAHIEDM DLFTVSPFEQ ELVIRHTEGQ TVRLADRSPD
     FVESYLDYAL ENGPASRMIE FDWQQESLLI PNMSDKETIV SLALMSSDAY VGLPTDADWN
     DVGDKYNESE RFGWENGGVR GHVFTDPEET IVIISIKGTS AAGLNTGGDG QTVEQDKTND
     NLLFSCCCAR VSSLWKTVCD CYEESYTCNQ NCLEQELRRP DRYYKAVLEI YRNVTHMYPE
     SEIWVTGHSL GGSLSSLLGR TFGLPAVSFE AVGELLATRR LHLPMPPGLP EEMENIWHVG
     NTADPIFMGV CNGASSTCSL AGYALETQCH SGKKCVYDVV NDLGWHVNLL NHRIRTIISD
     VLMVYNDTAE CVKPPPCYDC YNWRFVDHSG DRYRTTASSP SPIPSDPPGR RCLKRTWYGR
     CYEWADDPSA VKTTFATSTI YRKTSDISTS THTGGNTTCI RRSWLGYCLE YGPELR