ID   ATG18_MAGO7             Reviewed;         469 AA.
AC   Q524W4; A4R7V5; G4NAU7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; ORFNames=MGG_03139;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC       and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC       Necessary for proper vacuole morphology. Plays an important role in
CC       osmotically-induced vacuole fragmentation. Required for cytoplasm to
CC       vacuole transport (Cvt) vesicle formation, pexophagy and starvation-
CC       induced autophagy. Involved in correct ATG9 trafficking to the pre-
CC       autophagosomal structure. Might also be involved in premeiotic DNA
CC       replication (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Endosome membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminus might form a beta-propeller domain involved in
CC       specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2),
CC       leading to the association of the protein to the membrane.
CC       {ECO:0000250}.
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.
CC       {ECO:0000250|UniProtKB:P43601}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; CM001234; EHA50539.1; -; Genomic_DNA.
DR   RefSeq; XP_003716858.1; XM_003716810.1.
DR   AlphaFoldDB; Q524W4; -.
DR   SMR; Q524W4; -.
DR   STRING; 318829.MGG_03139T0; -.
DR   EnsemblFungi; MGG_03139T0; MGG_03139T0; MGG_03139.
DR   GeneID; 2676412; -.
DR   KEGG; mgr:MGG_03139; -.
DR   VEuPathDB; FungiDB:MGG_03139; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q524W4; -.
DR   OMA; PSRDFAW; -.
DR   OrthoDB; 1216824at2759; -.
DR   PHI-base; PHI:2084; -.
DR   Proteomes; UP000009058; Chromosome 4.
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..469
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000050868"
FT   REPEAT          188..228
FT                   /note="WD 1"
FT   REPEAT          233..272
FT                   /note="WD 2"
FT   REGION          285..348
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        307..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  50451 MW;  EDFBFD8546B5DBF7 CRC64;
     MATATLNFIT FNQDHGCLAV GTSRGFRIYH TEPFSKIFSS EDGNVSIIEM LFSTSLVALI
     LSPRHLIIQN TKRGSVICEL TFPSAVLAVR LNRKRLAVVL EDEIYLYDIA NMSLLFTIAT
     SPNPSAICAL SPSSENCFLA YPLPKPREDK DDKRPSHAPP LPTYIPPTSG DVLIFDAITL
     KAVNVIEAHR SPLSCIAINS EGTLLATASE TGTIIRVFTV PKGQKLYQFR RGTYPSTIYS
     MSFNLSSTLL CVSSTSDTVH IFRLGGPNNG ASGAAGAGSA GEVLAASPGQ DITGSPRADR
     WSRSRSYDSG NESPGSGSEA NDIAGSPSPR DRPTAANRRQ SGSFSNILRR SSQIMGRSVA
     GVVGSYLPQT VTEMWEPARD FAFIKIPKSS AARQHNNPGA TPSLPIAGEP LRSVVAMSSS
     SPQVMVVTSD GKFYVYNINM ETGGEGYLVR QYSILENDDK HDSSSTYES