ATG15_LODEL
ID ATG15_LODEL Reviewed; 552 AA.
AC A5E567;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; ORFNames=LELG_04756;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981530; EDK46575.1; -; Genomic_DNA.
DR RefSeq; XP_001523943.1; XM_001523893.1.
DR AlphaFoldDB; A5E567; -.
DR STRING; 379508.A5E567; -.
DR ESTHER; lodel-atg15; Lipase_3.
DR EnsemblFungi; EDK46575; EDK46575; LELG_04756.
DR GeneID; 5231224; -.
DR KEGG; lel:LELG_04756; -.
DR VEuPathDB; FungiDB:LELG_04756; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_2_1; -.
DR InParanoid; A5E567; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000001996; 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..552
FT /note="Putative lipase ATG15"
FT /id="PRO_0000317964"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 27..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 50..552
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 552 AA; 63136 MW; 141395528854882B CRC64;
MLHITEKEQT RGLRQLEKRG KRLLPPLIKF IWFCLISAAC VAATTFYWLR LSPVHNIHKH
SLNSSFEDKG EDGTLQLKHI FHHGVGEKDY KIHKRLDVTQ EYLIKHSAYF QNMVNEQQQE
VQEIQEIHKR HEKQEIQVKY GPDQEYNQTN TALNSVGTEY KSRLSTNEYD WPDVHRGKNP
FDIQLPFKNK QSIARRIKHR NEPFFIESYL DYARSVNGDA LILNRINLEW IDDDINIPNI
TDKDTIVTLA TISSNAYVRF PQNDDDKKKS DWTDVGGGWI PDEENNDVNF GWEDVGLRGH
IFVSKDNKTV VIGIKGTSGA GLPGGGSDET TKNDKTNDNL LFSCCCARVG YMWTTVCDCY
EKAYTCNQDC LEKELRRKDR YYEAALDIYK NVTAIYPPET TDIWVTGHSL GGALASLLGR
TYGLPTVAYE APGEMLALKR LHLPQAPGLP RHLEHIWHIG NTADPIYMGV CNGASSSCSL
GGYAMETACH TGYQCVYDVV TDYGWRVNLL NHRIHTVIDD IILVYNETAP CVYQAPCRDC
FNWRFVSHDD KE
