ID   ATG18_BOTFB             Reviewed;         434 AA.
AC   A6SJ85;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=atg18; ORFNames=BC1G_12821;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN18537.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH476947; EDN18537.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_001548677.1; XM_001548627.1.
DR   AlphaFoldDB; A6SJ85; -.
DR   SMR; A6SJ85; -.
DR   VEuPathDB; FungiDB:Bcin13g04280; -.
DR   OrthoDB; 1216824at2759; -.
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; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endosome; Membrane; Protein transport; Repeat; Transport;
KW   Vacuole; WD repeat.
FT   CHAIN           1..434
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000317999"
FT   REPEAT          1..34
FT                   /note="WD 1"
FT   REPEAT          183..223
FT                   /note="WD 2"
FT   REPEAT          228..267
FT                   /note="WD 3"
FT   REPEAT          367..407
FT                   /note="WD 4"
FT   REGION          262..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           224..228
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
SQ   SEQUENCE   434 AA;  46985 MW;  5A700E3301B012E5 CRC64;
     MNYVTFNQDY SCLAVGTAKG FRIYHTEPFS KIFTGDNENV TIIEMLFSTS LVAIKQSPRH
     IVIQNTKRGT VICELTFPSA VLAVRLNRKR FAVLLEEEIY LYDIQNMGLL YTISTSANPN
     AICSLSASSD NCYLAYPLPK PREETGDKRP AHAPPLSPYV APTSGEVLIF DAKSLKAVNV
     IEAHRAPLSC IALNNDGTLL ATASETGTII RVFSVPDGQK LYQFRRGTYP SSIFSLSFNM
     SSTLLCVSSN SDTIHIFRLG GPVTGLPESP QSPGDKDKWR RSRSFDSENG SPPAGISPGS
     EMADVPAEKS KSSGTFGSMI RRSSQMVGKG VAGVVGGYLP QAVTEMWEPA RDFAFIKLPK
     GGMGVTPRSG PVKSVVAMSS SSPQVMVVTS DGGFYIYSID METGGEGVLV KQYSVLESDD
     SLEPPPINYV SYRT