ID   ATG18_NEUCR             Reviewed;         436 AA.
AC   Q96U88; Q1K5B1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=apg-10; Synonyms=atg18; ORFNames=B12F1.070, NCU03441;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 apg-7/atg9 trafficking to the
CC       pre-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 apg-6/atg8 and atg16 to
CC       the 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; AL390091; CAD11327.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA27491.2; -; Genomic_DNA.
DR   PIR; T51055; T51055.
DR   RefSeq; XP_956727.2; XM_951634.3.
DR   AlphaFoldDB; Q96U88; -.
DR   SMR; Q96U88; -.
DR   STRING; 5141.EFNCRP00000002731; -.
DR   EnsemblFungi; EAA27491; EAA27491; NCU03441.
DR   GeneID; 3872878; -.
DR   KEGG; ncr:NCU03441; -.
DR   VEuPathDB; FungiDB:NCU03441; -.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q96U88; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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..436
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000050869"
FT   REPEAT          1..39
FT                   /note="WD 1"
FT   REPEAT          188..228
FT                   /note="WD 2"
FT   REPEAT          233..272
FT                   /note="WD 3"
FT   REPEAT          374..414
FT                   /note="WD 4"
FT   REGION          272..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           229..233
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
FT   COMPBIAS        301..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  47092 MW;  28A37677FB2FBE8B CRC64;
     MTGGTLNFIT FNQDYSCLAV GTSKGFRFYH TDPFSKIFSS DEGNVSIIEM LFSTSLVALI
     LTPRQLEIQN TKRASVICEL TFPSAVLAVR LNRKRLAVVL ECQIYLYDVS NMNLVQTIDT
     SPNPNAICAL SPSSDSCYLV YPRPNPREDV GAKAPAHLPP PSQYVPPKRG DVLVYDALNL
     KTVNVVEAHK SPLCAIALNH DGSMLATASE TGTIIRVFSL PQGQKLFQFR RGTVPTSIYS
     MSFNLSSTLL CVSSTSDTVH IFRLLNTQKN ANALPGGGPA QGTRSRSFDV NDPSPHKGEV
     PSAGNGNNGS GSHKREPSGS FGNMLRRSSQ MMVRGVAGVA SSYLPQSVAE MWEPERDFAF
     IKIPKSSNNR AGGLSATPLR SVVAMSSSSP QVMVVTSDGG FYVYNIDMEK GGEGYLVKQF
     SVLDGDDKLT NSDYGA