ID   ATG18_PICST             Reviewed;         563 AA.
AC   A3GFE3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; ORFNames=PICST_52962;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAVQ01000001; EAZ63740.2; -; Genomic_DNA.
DR   RefSeq; XP_001387763.2; XM_001387726.1.
DR   AlphaFoldDB; A3GFE3; -.
DR   SMR; A3GFE3; -.
DR   STRING; 4924.XP_001387763.2; -.
DR   EnsemblFungi; EAZ63740; EAZ63740; PICST_52962.
DR   GeneID; 4850992; -.
DR   KEGG; pic:PICST_52962; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; A3GFE3; -.
DR   OMA; PSRDFAW; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..563
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000318007"
FT   REPEAT          36..74
FT                   /note="WD 1"
FT   REPEAT          247..287
FT                   /note="WD 2"
FT   REPEAT          292..331
FT                   /note="WD 3"
FT   REGION          329..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           288..292
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
FT   COMPBIAS        346..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..391
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  61538 MW;  10ECF748B8168041 CRC64;
     MLKAQSAAAG SLHQTLSQYS ASIATDGSSS VTGSFKTDDS VNFITFNQDA SCIAVGLNNG
     YKIFNCKPKF GKCYQIRKEE SVGIIEMLYC TSLLAIVALG EEPGSSPRKL KIVNTKRQTT
     ICDLIFPSTI LQVKLTKSRL IVLLEEQIYI YDITTMKLLH TIETSPNSIG LCALSTTPDN
     DGNNYLAYPS PPKTITHDSL LASGINTNGG TNSVVNNISS VSNSPNRVGD VIMFNLNTLQ
     PMSVIEAHKS ALAAITLSSD GSLLATASDK GTIVRVFSVA TGVKLFQFRR GTYSTKIYSL
     SFSSDNNYVV ATSSSETVHI FRLGESEALE NKHKKKKAST PKPTQPETIE EEDATLLQER
     PSQESTQDDD EFADDGDDSD EAVEGDDNDD ESLEVISNKQ RKLSQGSSNS FASFNSGTDD
     SSQAAKNEPL IDQNRLSVAR LIRRSSQTLG RKAAQRMGDF LPSRFSSILE PTRHFASLKI
     NAIGKDVKSI AVMNNELQED LVPQAFLMRK DSDSYLSKEM LSLNLLHIYV VTSEGFFYTY
     GLDPERGGDC ILLHQYSLID ESN