ATG15_ASPTN
ID ATG15_ASPTN Reviewed; 613 AA.
AC Q0CXU6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Putative lipase atg15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=atg15; ORFNames=ATEG_01488;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476595; EAU38245.1; -; Genomic_DNA.
DR RefSeq; XP_001208853.1; XM_001208853.1.
DR AlphaFoldDB; Q0CXU6; -.
DR STRING; 341663.Q0CXU6; -.
DR ESTHER; asptn-atg15; Lipase_3.
DR EnsemblFungi; EAU38245; EAU38245; ATEG_01488.
DR GeneID; 4315897; -.
DR VEuPathDB; FungiDB:ATEG_01488; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_1_1; -.
DR OMA; WFGCKDE; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000007963; 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: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; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..613
FT /note="Putative lipase atg15"
FT /id="PRO_0000317959"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 44..613
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 472..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 613 AA; 66953 MW; 199F93FF8C2DE22D CRC64;
MKSHQGHQKK RRMREMGFST LLLGASLLLP VSVSASAPPS IYSRPYDSSP FLSPQIPLED
LSSLSGTHEF TLRHIFHRGT YQHPDLHRRL DIQPHTQLWV LSEDGTDKEA AEFDTPLIAS
SHPVTIQRLA DRRPSVIEEH LLAARMSGSA SVLSESDWVM DTLAGPDVTD KNSVLTFAKM
TANDYIQEPD TEDWQDIHGR FNYSSSFGWQ TDGLRGHIYA DKTNSTIVIS LKGTSPALFD
GAGTTTNDKL NDNLYFSCCC GQGGSYLWRQ VCDCQKSAFT ANLTCIIEAM NDENRYYRAA
LDLYSNVTEL YPDANVWLTG HSLGGAMTSL LGLTYGLPAV TFEAVPEALP AARLGLPSPP
GHDPRLPQSR RYTGAYHFGH TADPVYMGTC NGVSSVCTWG GYAMESACHT GQMCVYDTVD
DKGWRVAIGT HRIKAVISDV LEVYDDVPQC APEEECYDCE LWKFFRSNGS EHTTTTTTTT
TTTTTPPSTS TSTCKTPGWW GCLDESTTTT ATSTSTTSTS TTTCKTPGWF GCKDPTTSTT
ATPEPSLTTT LPLMTSTTCA HPGWFGCRDP TSPTSTPTQT PPPGDTTSCE SPGFFWGCWD
PKTTSDHPIT TPP
