ATG15_CHAGB
ID ATG15_CHAGB Reviewed; 499 AA.
AC Q2H6M8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Putative lipase atg15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=atg15; ORFNames=CHGG_05687;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408031; EAQ89068.1; -; Genomic_DNA.
DR RefSeq; XP_001221782.1; XM_001221781.1.
DR AlphaFoldDB; Q2H6M8; -.
DR STRING; 38033.XP_001221782.1; -.
DR ESTHER; chagb-atg15; Lipase_3.
DR EnsemblFungi; EAQ89068; EAQ89068; CHGG_05687.
DR GeneID; 4390326; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_0_1; -.
DR InParanoid; Q2H6M8; -.
DR OMA; CYEKTYT; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000001056; 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.
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..499
FT /note="Putative lipase atg15"
FT /id="PRO_0000317960"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 31..499
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 436..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 170
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 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 54141 MW; 23AD1C9BC1CFC0AD CRC64;
MSIGEVSDSA GHLASLVLPI EVAPIAPLIP EPPATAEHIF TLRHVYHHGT HKHPSLHRKH
DVTPSNADVW LAAEDGYEAE RIGPLRARSN ALRIQRLVDR RPSVVDPMVA QSRQQGFVSV
LSPSAWTVDD VAGPDVTDKG TVLTMALMAA NAYVEGPGKA DWQDVGAPFN RSLDFGWEGD
GLRGHVFADE NNSTIVIGLK GTSPAVFDGD GTTTNDKVND NLFFSCCCAQ QGPWTWHQVC
DCATGTYTCN NTCVTQALRE ENRYYQAARE LYANVTEVYP DSHVWIAGHS LGGAVSSFLG
LTYGVPVVTF QAVPDALPAG RLGLPVPPGA DPNAPQSRDY TGAFHFGHTA DPIYMGSCNG
ATASCSFAGY ALESACHTGH ECVYDTVGDK GWRVGIGTHK IVAVIRDVIL KYDTVPECKF
TPECRDCGNW KMYESNGTET TTTSSAPTTT SISRTRTETC KTPHLKSQQQ RQRPRPRPLH
ALPQWEGGNP DSPERNEEM
