ID ATG18_PHANO Reviewed; 414 AA.
AC Q0U2J8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Autophagy-related protein 18;
GN Name=ATG18; ORFNames=SNOG_14035;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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}.
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DR EMBL; CH445353; EAT78660.2; -; Genomic_DNA.
DR RefSeq; XP_001804234.1; XM_001804182.1.
DR AlphaFoldDB; Q0U2J8; -.
DR SMR; Q0U2J8; -.
DR STRING; 321614.Q0U2J8; -.
DR EnsemblFungi; SNOT_14035; SNOT_14035; SNOG_14035.
DR GeneID; 5981157; -.
DR KEGG; pno:SNOG_14035; -.
DR VEuPathDB; FungiDB:JI435_140350; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_0_1; -.
DR InParanoid; Q0U2J8; -.
DR OrthoDB; 391429at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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:0044804; P:nucleophagy; 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; 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:SF17; WD REPEAT DOMAIN PHOSPHOINOSITIDE-INTERACTING PROTEIN 2; 1.
DR PANTHER; PTHR11227; WD-REPEAT PROTEIN INTERACTING WITH PHOSPHOINOSIDES WIPI -RELATED; 1.
DR Pfam; PF21032; PROPPIN; 2.
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..414
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000318005"
FT REPEAT 1..34
FT /note="WD 1"
FT REPEAT 69..114
FT /note="WD 2"
FT REPEAT 139..182
FT /note="WD 3"
FT REPEAT 185..225
FT /note="WD 4"
FT REPEAT 230..269
FT /note="WD 5"
FT REPEAT 317..359
FT /note="WD 6"
FT REPEAT 367..407
FT /note="WD 7"
FT REGION 267..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 226..230
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 267..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 45103 MW; 7CE5C19C25EC0505 CRC64;
MNFVTFNQDH SHLGVGTSNG YRVYTTDPFN KQSESREGDV SSLEMLFSTS LVALTLSPRV
LRIQNTKGKR HSTICEMTFR TAILAMRLNR KRLVVVLESE LYIYDISNMQ MLRTEKTSPN
PNAICALSAS SENNYLIYPL PTKAAPATFQ PPSHAPPKSD HIAPTSGEIL IYDATKMEAV
NVIEAHNSPL SCIALNNDGT LLATASEKGT IIRVFSIPDA QKLYQFRRGS IPARIFSMSF
NSTSTLLSVS SATETVHIFR LGAPNTSRSN SISSGPTTLL STSHQRSSSR TSEDISDEFG
SSTADMAASE RKPLNPTFAS MIRRTSQTVG KSFAATVGGY LPSAVAEIWE PSRDFAWVKV
PRSPNAASAG PVRTVVALSN NGPQIMVVTS EGNYYVFNVD LEKGGEGTLY KQYS
//
