ID   ATG18_YARLI             Reviewed;         400 AA.
AC   Q6C044;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   02-SEP-2026, entry version 124.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; OrderedLocusNames=YALI0F27907g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Dipodascomycetes;
OC   Dipodascales; Dipodascales incertae sedis; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382132; CAG78780.1; -; Genomic_DNA.
DR   RefSeq; XP_505968.2; XM_505968.3.
DR   AlphaFoldDB; Q6C044; -.
DR   SMR; Q6C044; -.
DR   FunCoup; Q6C044; 579.
DR   STRING; 284591.Q6C044; -.
DR   EnsemblFungi; CAG78780; CAG78780; YALI0_F27907g.
DR   KEGG; yli:2908106; -.
DR   VEuPathDB; FungiDB:YALI0_F27907g; -.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q6C044; -.
DR   OMA; NIAILEM; -.
DR   OrthoDB; 122366at4891; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0061723; P:glycophagy; IBA:GO_Central.
DR   GO; GO:0044804; P:nucleophagy; IBA:GO_Central.
DR   GO; GO:0000425; P:pexophagy; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   FunFam; 2.130.10.10:FF:000965; Autophagy-like protein 18 Atg18; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR048720; PROPPIN.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR11227; WD-REPEAT PROTEIN INTERACTING WITH PHOSPHOINOSIDES WIPI -RELATED; 1.
DR   Pfam; PF21032; PROPPIN; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 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_0000050873"
FT   REPEAT          193..233
FT                   /note="WD 1"
FT   REPEAT          238..277
FT                   /note="WD 2"
FT   MOTIF           234..238
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
SQ   SEQUENCE   400 AA;  43565 MW;  1C14722C0F67BBC0 CRC64;
     MSDSINFVSF NQDYSCVSVG TPQGYKIYNC DPFGKCFSKA DGGMGIVEML FCTSLIAVVG
     MGDQPQNSPR RLKIVNTKRQ STICELTFPT AVLGVRLNRQ RLVVLLQDQI YIYDISNMKL
     VHTIETSPNP GAVCALSASS SDNNNYLVYP FPAPSSTAFN PGENNINDSS PNRKGDVTIF
     DCNSLQPVNV VEAHKTPLAC LSLNSDGTLL ATASDKGTII RVFSVPKAQK LYEFRRGTYP
     AQIFSINFNL ASNLMAVSSA TETVHIFQLE AGVSSTPEVP QDTELAIPTR TPQQKGMASV
     FRKSSRSLGK GLAGAVGSYL PQTFTGMWEP LRDFAFIKQT SLPGTRSVVS VTSTNPPQVL
     VVTLEGYFYQ YTLDLEKGGE CDLIRQYSLL DNVEGSLYGP
//