ATG15_CRYNJ
ID ATG15_CRYNJ Reviewed; 522 AA.
AC P0CO60; Q55V69; Q5KL13;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; OrderedLocusNames=CNC01140;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Single-pass type II membrane protein
CC {ECO:0000250}. Endosome, multivesicular body membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Prevacuolar
CC compartment membrane {ECO:0000250}; Single-pass type II membrane
CC protein {ECO:0000250}. Note=From ER, targeted to vacuolar lumen at the
CC MVB vesicles via the Golgi and the prevacuolar compartment (PVC).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AE017343; AAW42129.1; -; Genomic_DNA.
DR RefSeq; XP_569436.1; XM_569436.1.
DR AlphaFoldDB; P0CO60; -.
DR STRING; 5207.AAW42129; -.
DR ESTHER; cryne-q5kl13; Lipase_3.
DR PaxDb; P0CO60; -.
DR PRIDE; P0CO60; -.
DR EnsemblFungi; AAW42129; AAW42129; CNC01140.
DR GeneID; 3256692; -.
DR KEGG; cne:CNC01140; -.
DR VEuPathDB; FungiDB:CNC01140; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_1_1_1; -.
DR InParanoid; P0CO60; -.
DR OMA; LESKCHT; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000002149; Chromosome 3.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0034496; P:multivesicular body membrane disassembly; IBA:GO_Central.
DR GO; GO:0046461; P:neutral lipid catabolic process; IBA:GO_Central.
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; IBA:GO_Central.
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; Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Putative lipase ATG15"
FT /id="PRO_0000317963"
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..522
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 481..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..506
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 522 AA; 57210 MW; D140C3E99EABE3FA CRC64;
MYIPGPLRLS SYLLPFLSSP SPPAQSSPDT RTISFKPVHA HGHAFVDNAS TPTLLFLDQS
PSASLYAHDY PIGAFGDDYV 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 LADPWPEEGE GKSGVWEKAV EGWYRAADRV RAALDESVVR DDVNVWWGWG
RRGPKRQPGG EDPGWRKHGG VPKPVSEEDC VDCYKWEFGE WN
