ATG18_GIBZE
ID ATG18_GIBZE Reviewed; 459 AA.
AC I1RKA1; A0A1C3YN51;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Autophagy-related protein 18 {ECO:0000303|PubMed:28894236};
GN Name=ATG18 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG04297, FGRAMPH1_01T14949;
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: Component of the PI(3,5)P2 regulatory complex that regulates
CC both the synthesis and turnover of phosphatidylinositol 3,5-
CC bisphosphate (PtdIns(3,5)P2) (By similarity). Plays an important role
CC in osmotically-induced vacuole fragmentation (By similarity). Required
CC for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy
CC and starvation-induced autophagy (By similarity). Involved in correct
CC ATG9 trafficking to the pre-autophagosomal structure (By similarity).
CC With ATG2, protects ATG8 from ATG4-mediated cleavage (By similarity).
CC Autophagy is required for proper vegetative growth, asexual/sexual
CC reproduction, and full virulence (PubMed:28894236). Autophagy is
CC particularly involved in the biosynthesis of deoxynivalenol (DON), an
CC important virulence determinant (PubMed:28894236).
CC {ECO:0000250|UniProtKB:P43601, ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex (By similarity).
CC Interacts with ATG2 and ATG9 (By similarity). The ATG2-ATG18 complex is
CC essential for autophagosome formation (By similarity).
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P43601}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P43601}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P43601}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P43601}. Endosome membrane
CC {ECO:0000250|UniProtKB:P43601}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- DOMAIN: The 377 first amino acids might form a beta-propeller domain
CC involved in specific binding to phosphatidylinositol 3,5-bisphosphate
CC (PIP2), leading to the association of the protein to the membrane (By
CC similarity). Association to the membrane can also occur through binding
CC to phosphatidylinositol 3-monophosphate (PI3P) (By similarity).
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole
CC transport (Cvt) pathway, for the recruitment of ATG8 and ATG16 to the
CC PAS in nutrient-rich medium, and for its recruitment to and
CC dissociation from the PAS under starvation conditions (By similarity).
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- DISRUPTION PHENOTYPE: Does not significantly decrease the growth rate
CC under nutrient-rich conditions (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SCB65938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HG970333; SCB65938.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011321319.1; XM_011323017.1.
DR AlphaFoldDB; I1RKA1; -.
DR SMR; I1RKA1; -.
DR STRING; 5518.FGSG_04297P0; -.
DR GeneID; 23551555; -.
DR KEGG; fgr:FGSG_04297; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR InParanoid; I1RKA1; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..459
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000443918"
FT REPEAT 1..39
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 188..228
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 233..272
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 393..433
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REGION 229..232
FT /note="Necessary for proper localization to vacuole
FT membrane"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT REGION 264..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 229..233
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 322..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 49247 MW; 6F2304978E3D1A3E CRC64;
MTSPALNFIT FNQDHSCLAV GTSKGFRIYH TDPFSRIFSS DDGNIAIIEM LFSTSLVALI
LSPRHLIIQN TKRASTICEL TFPSAVLAVR LNRKRLAVVL EEEIYLYDIS NMSLLHTIAT
SPNPSAICAL SPSSENCFIA YPLPKPREDP DANRPAHAPP QSTFVAPTSG EVLIFDTLSL
KAVNVIEAHR SPLCCICLNN EGTLLATASE TGTIIRVFSV PKGKKLYQFR RGTYPSTIYS
MSFNLSSTLL CVSSTSDTIH IFRLGAPPGN TTPAGAPIES PASQRQDRWS RARSYDDSES
PGASAADSPK NEPAELNGPG AGNNQGGHTR GSGSFSSMLR RSSQIMGRGV AGVMGSYLPQ
SVTEMWEPLR DFAYIKIPKS AAASGASRTL RDAPGGPLRS VVAMSSSSPQ VMVVTSDGGF
YVYNIDMEHG GEGYLVKQFS VNHSVLEGDD KSDASGYGS
