ID   ATG18_VANPO             Reviewed;         558 AA.
AC   A7TPY4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; ORFNames=Kpol_1008p20;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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   -!- SEQUENCE CAUTION:
CC       Sequence=EDO15682.1; Type=Erroneous gene model prediction; Evidence={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; DS480449; EDO15682.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001643540.1; XM_001643490.1.
DR   AlphaFoldDB; A7TPY4; -.
DR   SMR; A7TPY4; -.
DR   STRING; 436907.A7TPY4; -.
DR   EnsemblFungi; EDO15682; EDO15682; Kpol_1008p20.
DR   GeneID; 5543781; -.
DR   KEGG; vpo:Kpol_1008p20; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; A7TPY4; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000000267; 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   Pfam; PF00400; WD40; 2.
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..558
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000318010"
FT   REPEAT          4..42
FT                   /note="WD 1"
FT   REPEAT          290..330
FT                   /note="WD 2"
FT   REPEAT          335..374
FT                   /note="WD 3"
FT   REGION          176..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           331..335
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
SQ   SEQUENCE   558 AA;  61146 MW;  7BCEC1C9A06369F4 CRC64;
     MLIDYPPTIN FINFNQTGSC ISIATDDGFS IYNCDPFGKF YSQKNYSIVE MLFSTSLLAV
     VGLGDQPALS QRRLTMINTK TYSIICEVTF PSAILSVKMN KSRLVVLLRD QIYIYDINNM
     RLLHTIETTS NKLGIISISS SPSPDHNMYL AYPSPPKFIN SDIKSNLTTN NISIASSSSS
     QVEPPLNPQQ RSNFSGNTLE TIQDGKSYDG SNNSNNGNNN NNNNNNNNNN NNNNNNNNNN
     NNNSNNEENS NSKSFQQTGI TGSSNSTIMK NGDVILFDLQ TLQPTMVIEA HKGPIAALTL
     SFDGSLLATA SEKGTIIRVF NVETGAKIYQ FRRGTYPTEV YSLAFSKDNQ FLAATSSSKT
     VHIFKLGKIM ETSSDDNNNN TDDDSLNAGN IDSEIVTNLS SESLTESQSK DPHVDTSRST
     VGRMIRKSSQ QLSRQAAKKL GQIFPLKVAS ILESSRHFAS FKLPTTGSGG GNSTGAGGQI
     KSISCFGEEI ELDSSEYPEL FNQGQDTTSN ISQSKNPKLM KMQPIRIVSS DGNYYNYILD
     PERGGDCLLL SQYSILTN