ATG15_CRYNB
ID ATG15_CRYNB Reviewed; 519 AA.
AC P0CO61; Q55V69; Q5KL13;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; OrderedLocusNames=CNBC6140;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAEY01000017; EAL21576.1; -; Genomic_DNA.
DR RefSeq; XP_776223.1; XM_771130.1.
DR AlphaFoldDB; P0CO61; -.
DR ESTHER; cryne-q5kl13; Lipase_3.
DR EnsemblFungi; EAL21576; EAL21576; CNBC6140.
DR GeneID; 4935280; -.
DR KEGG; cnb:CNBC6140; -.
DR VEuPathDB; FungiDB:CNBC6140; -.
DR HOGENOM; CLU_028295_1_1_1; -.
DR Proteomes; UP000001435; Chromosome 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:0005775; C:vacuolar lumen; IEA:EnsemblFungi.
DR GO; GO:0004620; F:phospholipase activity; IEA:EnsemblFungi.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0034496; P:multivesicular body membrane disassembly; IEA:EnsemblFungi.
DR GO; GO:0046461; P:neutral lipid catabolic process; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0006660; P:phosphatidylserine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0006624; P:vacuolar protein processing; IEA:EnsemblFungi.
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..519
FT /note="Putative lipase ATG15"
FT /id="PRO_0000410136"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 27..519
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 481..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 519 AA; 56915 MW; B0C1D7911BEAAEF2 CRC64;
MYIPGPLRLS SYLLPFLSSP SPPAQSSPDT RTISFKPVHA HGHAFVDNAS TPTLLFLDQS
PSASLYAHDY PIGAFGDDYM LPRLTSDVLE IRTRKKLIRR PKVRPPRIIS WAQSYRAQAL
HFNGINNNND NSNKSISLPE SWLAPDLANP SDEWSDVEVT VPDLTDRQTV ITLAKMSSNA
YVTPGGAGWY TLNDWNASMP FGWEPDADGL RGHVFADEKN ETVIISIKGT SAGVLGSGGP
TAKNDKFNDN LLFSCCCARV DFSWTPVCDC YAGGYKCGQT CLEDALVSES VYATVGTNLY
NNITYMYPNA TIWLTGHSLG GAVSSLIGLS FGAPAVTYES PGELLPASRL HLPLPPGMPA
NLSGITHVYH TADPIAMGVC NGPYSSCYAA GFAMESKCHT GETILYDTVR VKGWSVDVRT
HRIEEVIDKV LADPWPEEEE GKSGVWEKAV EGWYRAADRV RAALDESVVR DDVNVWWGWG
RRGPKRQPGG EDPKHGGVPK PVSEEDCVDC YKWEFGEWN
