ID   ATG18_AJECN             Reviewed;         400 AA.
AC   A6QTX7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; ORFNames=HCAG_00833;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476655; EDN02969.1; -; Genomic_DNA.
DR   RefSeq; XP_001543787.1; XM_001543737.1.
DR   AlphaFoldDB; A6QTX7; -.
DR   SMR; A6QTX7; -.
DR   STRING; 339724.A6QTX7; -.
DR   EnsemblFungi; EDN02969; EDN02969; HCAG_00833.
DR   GeneID; 5449810; -.
DR   KEGG; aje:HCAG_00833; -.
DR   VEuPathDB; FungiDB:HCAG_00833; -.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   OMA; PSRDFAW; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000009297; 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; -; 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..400
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000317994"
FT   REPEAT          163..203
FT                   /note="WD 1"
FT   REPEAT          208..247
FT                   /note="WD 2"
FT   REPEAT          295..341
FT                   /note="WD 3"
FT   REPEAT          353..393
FT                   /note="WD 4"
FT   REGION          241..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           204..208
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
FT   COMPBIAS        248..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   400 AA;  43336 MW;  D3B62FB4E20C87B1 CRC64;
     MAMNFVTFNQ DYSYLAVGNI AILEMLFSTS LVALILSPRR LQITNTKRQS TICELTFPTT
     VLAVRLNRKR LVIVLEDQIY LYDIQTMKLL YTIETSPNPN AICALSPSSE NCYLAYPLPQ
     KAPPSSFTPP SHAPPSSAHI SPTSGEVLIF DTLKLEAINV VEAHKSPLSC LAINTEGTLL
     ATASDKGTII RVFSVPDAQK LYQFRRGSMP SRIFSMSFNI TSTLLCVSSA TETIHIFKLG
     HQDPSEDLPT SPIGTDSRKT NSTPRERAFS QGSSTLSGGD NSPTDGDPSD ISSRKHNGTL
     MGMIRRTSQN VGNSFAATVG GYLPKGVTEI WEPARDFAWI RLPKTAGYGG PGSNAGPVRS
     VVAMSSNTPQ VMVVTSDGNF YVYNVDLSKG GEGTLTKQYS