ID   ATG18_ASPCL             Reviewed;         417 AA.
AC   A1CBB8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=atg18; ORFNames=ACLA_014730;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027049; EAW13036.1; -; Genomic_DNA.
DR   RefSeq; XP_001274462.1; XM_001274461.1.
DR   AlphaFoldDB; A1CBB8; -.
DR   SMR; A1CBB8; -.
DR   STRING; 5057.CADACLAP00000823; -.
DR   EnsemblFungi; EAW13036; EAW13036; ACLA_014730.
DR   GeneID; 4706317; -.
DR   KEGG; act:ACLA_014730; -.
DR   VEuPathDB; FungiDB:ACLA_014730; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   OMA; PSRDFAW; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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; -; 2.
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..417
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000317995"
FT   REPEAT          1..36
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          312..358
FT                   /note="WD 6"
FT   REPEAT          370..410
FT                   /note="WD 7"
FT   REGION          261..314
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        261..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  45374 MW;  B5B5B357E80423F2 CRC64;
     MAMNFVTFNQ DYSYLAVATS KGFRIFTTDP FAKSYETKEG HIAIIEMLFS TSLVALILSP
     RRLQITNTKR QSTICELTFP TTVLAVKLNR KRLVIVLEDQ IYLYDIQTMK LLYTIQTSPN
     PNAICALSPS SDNCYLAYPL PQKAPPSSFT PPSHAPPGNT HVSPTSGEVL IFDSLKLEAI
     NVIEAHRSPL ACITLNSDGT LLATASDKGT IIRVFSVPDG HKLYQFRRGS MPSRIFSMSF
     NTTSTLLCVS SSTETIHLFK LSQQTSSSRD TSPSSSTPAG RDRAFSQSSL GHSPDRSDVS
     GEPDSSEFPA RKHNGTLMGI IRRTSQNVGS TVAAKVGGYL PKGVSEMWEP ARDFAWIKLP
     KPSQNAGGSG NNGPLRSVVA MSNNTPQVMV ITSDGNFYVF SIDLSKGGEG TLTKQYS