ATG15_GIBZE
ID ATG15_GIBZE Reviewed; 636 AA.
AC I1RFN8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Putative lipase ATG15 {ECO:0000250|UniProtKB:P25641};
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P25641};
DE AltName: Full=Autophagy-related protein 15 {ECO:0000303|PubMed:28894236};
GN Name=ATG15 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG02519, FGRAMPH1_01T06045;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28894236; DOI=10.1038/s41598-017-11640-z;
RA Lv W., Wang C., Yang N., Que Y., Talbot N.J., Wang Z.;
RT "Genome-wide functional analysis reveals that autophagy is necessary for
RT growth, sporulation, deoxynivalenol production and virulence in Fusarium
RT graminearum.";
RL Sci. Rep. 7:11062-11062(2017).
CC -!- FUNCTION: Lipase which is essential for lysis of subvacuolar cytoplasm
CC to vacuole targeted bodies and intravacuolar autophagic bodies (By
CC similarity). Involved in the lysis of intravacuolar multivesicular body
CC (MVB) vesicles (By similarity). The intravacuolar membrane
CC disintegration by ATG15 is critical to life span extension (By
CC similarity). Autophagy is required for proper vegetative growth,
CC asexual/sexual reproduction, and full virulence (PubMed:28894236).
CC Autophagy is particularly involved in the biosynthesis of
CC deoxynivalenol (DON), an important virulence determinant
CC (PubMed:28894236). {ECO:0000250|UniProtKB:P25641,
CC ECO:0000269|PubMed:28894236}.
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 Evidence={ECO:0000250|UniProtKB:P25641};
CC -!- SUBUNIT: Binds to both phosphatidylinositol (PI) and
CC phosphatidylinositol 3,5-bisphosphate (PIP2) (By similarity).
CC {ECO:0000250|UniProtKB:P25641}.
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 -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236). Strongly
CC reduces conidiation (PubMed:28894236). Reduces strongly the production
CC of deoxynivalenol (DON), an important virulence determinant
CC (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; HG970332; CEF74827.1; -; Genomic_DNA.
DR RefSeq; XP_011318453.1; XM_011320151.1.
DR AlphaFoldDB; I1RFN8; -.
DR STRING; 5518.FGSG_02519P0; -.
DR ESTHER; gibze-I1RFN8; Lipase_3.
DR GeneID; 23549891; -.
DR KEGG; fgr:FGSG_02519; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G06045; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_1_1; -.
DR InParanoid; I1RFN8; -.
DR PHI-base; PHI:1166; -.
DR Proteomes; UP000070720; Chromosome 1.
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.
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..636
FT /note="Putative lipase ATG15"
FT /id="PRO_0000443913"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25641"
FT TRANSMEM 20..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..636
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P25641"
FT REGION 478..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 636 AA; 69735 MW; 7F29E9F3ECBF4581 CRC64;
MYKYGTVVDP AMTTNRRSRL SGFRCASTAR VTATLLLSFL AFSPSSASSD FGDRFHDDIV
LPPGPVLPSA PEIPEPAEHT FSLRHIYHHG THLHPSLHRK RDVVHEQSRV YLAAEDDFSE
YDILRLKAKS RPEPIHRLAD RRPSVVDPMV AESRQRGYAA VLDASAWTMD QVSSPDIKDK
DTVLTLALMT ANAYVEHDTD ADWEDVGERW NRSADFGWES DGLRGHVFVD DTNSTIVIGL
KGTTTAVFDG EGTTTNDKVN DNLFFSCCCA QQGQWTWHQV CDCATGTYSC NNTCVVQALR
EENRYYGAAR ELYSNVTELY PDAQVWLTGH SLGGAVTSML GMTYGLPVVT FEAVPEALPA
SRLGLPVPPG ASAEYPQMRE NTGTFHFGHT ADPVYIGTCN GATASCTYGG YAMESTCHAG
YECVYDVVAD KGWRVGIGTH RIRSVIDDVI KKYDGVPECK RTPECRDCAQ WKMYESNGTE
TTTTSSPSTT STTRTRTRTS TCETPGWWGC LDKTTPVTTT TSTTSSSTST CKTPGWFGCK
DKTTSESSTT TTTEASPTTT CETPGRFWGC RDEVEATTTA KPGQVTNVPV TAAPTGTTDD
SLSTALPETQ RCLARNWFGI CKEWAIDDLE FATDEM
