ATG15_PASFU
ID ATG15_PASFU Reviewed; 661 AA.
AC O13444;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; Synonyms=pSI-7;
OS Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX NCBI_TaxID=5499;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Race 4;
RX PubMed=9390425; DOI=10.1094/mpmi.1997.10.9.1106;
RA Coleman M., Henricot B., Arnau J., Oliver R.P.;
RT "Starvation-induced genes of the tomato pathogen Cladosporium fulvum are
RT also induced during growth in planta.";
RL Mol. Plant Microbe Interact. 10:1106-1109(1997).
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 -!- INDUCTION: During starvation and plant infection.
CC {ECO:0000269|PubMed:9390425}.
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; Y14554; CAA74888.1; -; mRNA.
DR AlphaFoldDB; O13444; -.
DR ESTHER; clafu-PSI7; Lipase_3.
DR OMA; WFGCKDE; -.
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 2: Evidence at transcript level;
KW Autophagy; Endosome; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..661
FT /note="Putative lipase ATG15"
FT /id="PRO_0000317961"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 25..661
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 492..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 661 AA; 71955 MW; 94006D2206657847 CRC64;
MIWNGRLVLA CVLLIAGCSG QVDAARTREQ RKAFGSPNIV LPPGPAHEVA SAKPARALGE
KTFTLRHVYH HGTHNYPNLH RYIDIQPESK LQVSYDDGTT YEEAEVAFKA KAQSRIVQRM
AHRSHSDIDA VQVHYFTYGQ PADVEWTEDE IAGPNISDKS TVLTFAKMAA NAYIFSRKDG
EWQPVKGGFN YTDDFGWEQD GLRGHIFADE ANSTVVIGLK GTSPAIFDGA DTTGNDKLND
NLFGSCCCAQ GGPFTWKKVC DCAGSSAYTC NNTCLVKSLR EKGHYYWAVK DLYRNVTERY
PDSEVWLSGH SLGGVVSSLL GLTYGLPTLT FEAFPDAMAA SRLGLPTPPG YKIGSHQARP
MTGIHHFGHT ADPIYMGSCN GGTSFCSIGG YAFEGVCHTG ETCTYDTVRD LGWRVGIGTH
KIVSVIKDVI KVYDQPPSCE QDVECVDCYN WKYFENNGTE TTTSKASTAT STTTRTRTET
CKTPGWWGCL DESTTSAPTT STSTSSSTSS TRTCETPGWF GCKDETTTTS SSSSISSPSA
TPAPTITTTS SLPTSTSTST CKTPGWFGCY DESTTTSATP KPSSTARTVT KTKTTTSDDD
DCTSREWFGL ICVDPSPTTA SGSSPSSTNL PTTRRKMCTK RHWYGTCKQW RFDDFDPKND
L
