ID   ATG18_ASPTN             Reviewed;         414 AA.
AC   Q0CW30;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=atg18; ORFNames=ATEG_02104;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37066.1; -; Genomic_DNA.
DR   RefSeq; XP_001211282.1; XM_001211282.1.
DR   AlphaFoldDB; Q0CW30; -.
DR   SMR; Q0CW30; -.
DR   STRING; 341663.Q0CW30; -.
DR   EnsemblFungi; EAU37066; EAU37066; ATEG_02104.
DR   GeneID; 4316965; -.
DR   VEuPathDB; FungiDB:ATEG_02104; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   OMA; PSRDFAW; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000007963; 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; 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..414
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000317998"
FT   REPEAT          1..36
FT                   /note="WD 1"
FT   REPEAT          69..114
FT                   /note="WD 2"
FT   REPEAT          185..225
FT                   /note="WD 3"
FT   REPEAT          230..269
FT                   /note="WD 4"
FT   REPEAT          309..355
FT                   /note="WD 5"
FT   REPEAT          367..407
FT                   /note="WD 6"
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..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  45085 MW;  C088527061C595C9 CRC64;
     MAMNFVTFNQ DYSYLAVATS KGFRIFTTDP FAKSYETKEG NIAIIEMLFS TSLVALILSP
     RRLQITNTKR QSTICELTFP TTVLAVKLNR KRLVIVLEDQ IYLYDIQTMK LLYTIETSPN
     PNAICALSPS SDNCYLAYPL PQKAPPSSFN PPSHAPPGST HVSPTTGEVL IFDALKLEAI
     NVIEAHRSPL ACITLNSDGT LIATASDKGT IIRVFSVPDG HKLYQFRRGS IPSRIYSMSF
     NTTSTLLCVS SSTETIHLFK LSHQTSSREG SPSSALSRER AASQSSLGTS PDPDDPTDDM
     ESSEIASRKH NGTLMGMIRR TSQNVGSSFA AKVGGYLPKG VSEMWEPARD FAWIKLPKTN
     QTAGANGNAG SLRSVVAMSN NTPQVMVVTS DGNFYVFNID LSKGGEGTLT KQYS