AT151_PHANO
ID AT151_PHANO Reviewed; 594 AA.
AC Q0V1P1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Putative lipase ATG15-1;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15-1; ORFNames=SNOG_02073;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445327; EAT90285.1; -; Genomic_DNA.
DR RefSeq; XP_001792692.1; XM_001792640.1.
DR AlphaFoldDB; Q0V1P1; -.
DR STRING; 13684.SNOT_02073; -.
DR ESTHER; phano-at151; Lipase_3.
DR EnsemblFungi; SNOT_02073; SNOT_02073; SNOG_02073.
DR GeneID; 5969542; -.
DR KEGG; pno:SNOG_02073; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_1_1; -.
DR InParanoid; Q0V1P1; -.
DR OMA; WFGCKDE; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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.
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..594
FT /note="Putative lipase ATG15-1"
FT /id="PRO_0000317968"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 34..594
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 447..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 299
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 594 AA; 66120 MW; F8F5746260553008 CRC64;
MRRRPLCTSA SRVTASLLLS FLAVSSAAEL PILPAPPISP QPHSSEKDFS LRHIFHHGTY
KYPELHRRLD VPENAAVWAA EHLHSEHREP VPRLRVKAEP MSIQRLADRS KEAIDGILEW
GRMKGRAVQL AEDDWTIDEI AGPNVTDRET VLSFARMASN AYILEPNTGE WEDVGGGFNY
TEDFGWESDG LRGHIFADTE NSTVVIGLKG TSPAMFDGSE TTTKDKENDN LFFSCCCGQG
GQFLWRQVCD CQTSAYTCNS TCLVTALREK NRYYYAAQDL YHNVTALYPH AEIWMAGHSL
GGAVSSFLSL TFGHPAVTFE AVPEAMPASR LGLPVPPGHE IGSLQKRKMT GGYHFGHTAD
PIYMGQCNQA TSVCTFGGYA LQSVCHTGKK CVYDTVKDLG WRVGIGTHKI VEVIKDVIEK
YDAPPICEPY INCTDCYTWK YFESNGTETT TTSTSKPTST SKSSKSNTRT RTETCKTPGW
WGCLDETTTG TQTSTSTPKH TSTSSTSTCK TPGWFGCKGR QRRANHNNNK VLAHNYPRPS
THRNNNILFL PNINFFMSVP RLVRRLSRRR RPSLPNKTEV VNSSANHFVY VLHA
