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ATG18_PHANO
ID   ATG18_PHANO             Reviewed;         414 AA.
AC   Q0U2J8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; ORFNames=SNOG_14035;
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: 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; CH445353; EAT78660.2; -; Genomic_DNA.
DR   RefSeq; XP_001804234.1; XM_001804182.1.
DR   AlphaFoldDB; Q0U2J8; -.
DR   SMR; Q0U2J8; -.
DR   STRING; 13684.SNOT_14035; -.
DR   EnsemblFungi; SNOT_14035; SNOT_14035; SNOG_14035.
DR   GeneID; 5981157; -.
DR   KEGG; pno:SNOG_14035; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_0_1; -.
DR   InParanoid; Q0U2J8; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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; 2.
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..414
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000318005"
FT   REPEAT          1..34
FT                   /note="WD 1"
FT   REPEAT          69..114
FT                   /note="WD 2"
FT   REPEAT          139..182
FT                   /note="WD 3"
FT   REPEAT          185..225
FT                   /note="WD 4"
FT   REPEAT          230..269
FT                   /note="WD 5"
FT   REPEAT          317..359
FT                   /note="WD 6"
FT   REPEAT          367..407
FT                   /note="WD 7"
FT   REGION          267..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           226..230
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
FT   COMPBIAS        267..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  45103 MW;  7CE5C19C25EC0505 CRC64;
     MNFVTFNQDH SHLGVGTSNG YRVYTTDPFN KQSESREGDV SSLEMLFSTS LVALTLSPRV
     LRIQNTKGKR HSTICEMTFR TAILAMRLNR KRLVVVLESE LYIYDISNMQ MLRTEKTSPN
     PNAICALSAS SENNYLIYPL PTKAAPATFQ PPSHAPPKSD HIAPTSGEIL IYDATKMEAV
     NVIEAHNSPL SCIALNNDGT LLATASEKGT IIRVFSIPDA QKLYQFRRGS IPARIFSMSF
     NSTSTLLSVS SATETVHIFR LGAPNTSRSN SISSGPTTLL STSHQRSSSR TSEDISDEFG
     SSTADMAASE RKPLNPTFAS MIRRTSQTVG KSFAATVGGY LPSAVAEIWE PSRDFAWVKV
     PRSPNAASAG PVRTVVALSN NGPQIMVVTS EGNYYVFNVD LEKGGEGTLY KQYS
 
 
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