ATG15_CANAL
ID ATG15_CANAL Reviewed; 597 AA.
AC Q5A4N0; A0A1D8PPQ8; O94004;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; OrderedLocusNames=CAALFM_C601740CA;
GN ORFNames=Ca20C1.17, CaO19.10915, CaO19.3412;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1161;
RA Oliver K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; AL033391; CAA21938.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30111.1; -; Genomic_DNA.
DR RefSeq; XP_716721.1; XM_711628.2.
DR AlphaFoldDB; Q5A4N0; -.
DR STRING; 237561.Q5A4N0; -.
DR ESTHER; canal-ATG15; Lipase_3.
DR GeneID; 3641641; -.
DR KEGG; cal:CAALFM_C601740CA; -.
DR CGD; CAL0000191921; ATG15.
DR VEuPathDB; FungiDB:C6_01740C_A; -.
DR HOGENOM; CLU_028295_0_2_1; -.
DR InParanoid; Q5A4N0; -.
DR OrthoDB; 937562at2759; -.
DR PRO; PR:Q5A4N0; -.
DR Proteomes; UP000000559; Chromosome 6.
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: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:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
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..597
FT /note="Putative lipase ATG15"
FT /id="PRO_0000090365"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..597
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 507..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 364
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 106
FT /note="E -> K (in Ref. 1; CAA21938)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="D -> Y (in Ref. 1; CAA21938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 67469 MW; 3B8130FA04964AB4 CRC64;
MTLEKNRHAN KGTSWTWMIY KFVVGVITVA ILVLFITQKS VSQAQDKLRV EQQAIFSDQD
TLQLKHIFHH GTGPKNYRLH RRLDITSEYL AKHQPYFTTL TQQLSEPVLE EHIASDNLDK
IYQQSDWPEI HKGKNPFSIE LPFKKADSEA TRLKERNTLN FIESYLNYAR DIKGDAQILN
RINLDWIHDE IKVPNVTDRD TVVTLATISS NAYVRYPKDD DEKRKSDWID LGDWDPNRED
DDVNFGWDDI GLRGHVFVSK DNKTVVIGIK GTSGAGLPGG GSDETGGNDK TNDNLLFSCC
CARISYMWTT VCDCYEKTYT CNQDCLEKEL RKEDKYYQAV LELYRNVTDI YPPESTDIWV
TGHSLGGALA SLLGRTFGLP AVAFEAPGEM LATRRLHLPS PPGLPQHMEN IWHFGNTADP
IYMGVCNGAS STCNLAGYAM ETTCHTGLQC VYDVVTDKGW SVNLLNHRIH TVIDDIILTY
NETAPCAPSP PCRDCFNWRF VAHDDNEKDE PKLPNPLRSS SKSTLSTKTT SLKSSSTYSG
STSSSTVTKT TQTSPISSAS PTDQDPPKKC LKRTWYGWCT KWGYDDDDDD EDTFERK
