ID   ATG15_PENRW             Reviewed;         673 AA.
AC   A7KAM5; B6HSF9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Putative lipase atg15;
DE            EC=3.1.1.3;
DE   AltName: Full=Autophagy-related protein 15;
GN   Name=atg15; ORFNames=Pc22g21230;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; EF107747; ABO31085.1; -; Genomic_DNA.
DR   EMBL; AM920437; CAP99411.1; -; Genomic_DNA.
DR   RefSeq; XP_002566020.1; XM_002565974.1.
DR   AlphaFoldDB; A7KAM5; -.
DR   STRING; 1108849.XP_002566020.1; -.
DR   ESTHER; pencw-atg15; Lipase_3.
DR   EnsemblFungi; CAP99411; CAP99411; PCH_Pc22g21230.
DR   GeneID; 8305265; -.
DR   KEGG; pcs:Pc22g21230; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g21230; -.
DR   eggNOG; KOG4540; Eukaryota.
DR   HOGENOM; CLU_028295_0_1_1; -.
DR   OMA; WFGCKDE; -.
DR   OrthoDB; 937562at2759; -.
DR   BioCyc; PCHR:PC22G21230-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
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.
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..673
FT                   /note="Putative lipase atg15"
FT                   /id="PRO_0000317967"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        29..673
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        311
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   673 AA;  72414 MW;  0804919E2F352AC2 CRC64;
     MPRKRSRFEL SIHSLLLSVA VLSGAAYASG YYPPSQQVPI IPPQVPLKGA EATPDIHEFS
     LRHIFHRGTY EQPDFHARLD VKPDTRLRTV SEDGHEEEYI ASESSLLASS SPLTIQRLAD
     RRLPVIQGHL AAARSSGFAA ALSPQEWALD TLPGPNITDK PTVLTFAQMT ANDYIEEPGT
     GQWHTINGKF NYSGSFGWQK DGLRGHIYSD KTNGTVVISL KGTSPALFDG AGTTTNDKVN
     DNLYFSCCCG QGGSYLWRQS CDCQSATFTA NLTCIIESMT DEDRYYRAAI DLYSNVTEIY
     PDANIWMTGH SLGGAMTSLV GLTFGLPVVT FEAVPEALPA ARLGLPSPPG YDPRFPQSRQ
     YTGAYHFGHT ADPVFMGTCN GINSICTWGG YAMESVCHTG QVCTYDTVAD KGWRVGLGTH
     KIENVISDVL MTYDSVPSCV AEEECFDCEL WKFFRSNGSE ITTTTTTTTT TTSPTRTSTC
     KTPGWWGCLD ESTTATTTTT TTTTSTATTT TCMTPGWFGC NDPTTTTATP APTVTTTLPT
     VTSTTTSCHD PGWFGCRDET STVATTTANP ASPTSTACHS PGIFWGCWDE PTSTTAVTSL
     PAFTSAPIST TCHSPGIFWG CWDEPTSTTA VTSLPAITST PISTTCHIPG IFWGCWDEPT
     NTPAVTSAPT PTS