ID ATG18_YEAS7 Reviewed; 500 AA.
AC A7A258;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=Autophagy-related protein 18;
DE AltName: Full=Cytoplasm to vacuole targeting protein 18;
DE AltName: Full=Needed for premeiotic replication protein 1;
DE AltName: Full=Swollen vacuole phenotype protein 1;
GN Name=ATG18; Synonyms=AUT10, CVT18, NMR1, SVP1; ORFNames=SCY_1768;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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 May negatively regulate FAB1 activity by sequestering or masking VAC7
CC from FAB1. Necessary for proper vacuole morphology. Plays an important
CC role in osmotically-induced vacuole fragmentation. Required for
CC cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and
CC starvation-induced autophagy. Involved in correct ATG9 trafficking to
CC the pre-autophagosomal structure. Might also be involved in premeiotic
CC DNA replication. With ATG2, protects ATG8 from ARG4-mediated cleavage
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex, composed of
CC ATG18, FIG4, FAB1, VAC14 and VAC7 (By similarity). VAC14 nucleates the
CC assembly of the complex and serves as a scaffold (By similarity).
CC Interacts with ATG2, ATG9 and VAC17. The ATG2-ATG18 complex is
CC essential for autophagosome formation (By similarity). {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}. Note=Requires VAC7 for vacuole membrane localization.
CC Under mid-log phase growth, localizes to the vacuolar membrane; but
CC when cells are starved, is almost completely released from the vacuole
CC membrane (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The 377 first amino acids might form a beta-propeller domain
CC involved in specific binding to phosphatidylinositol 3,5-bisphosphate
CC (PIP2), leading to the association of the protein to the membrane.
CC Association to the membrane can also occur through binding to
CC phosphatidylinositol 3-monophosphate (PI3P). {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; AAFW02000176; EDN59169.1; -; Genomic_DNA.
DR AlphaFoldDB; A7A258; -.
DR SMR; A7A258; -.
DR HOGENOM; CLU_025895_5_2_1; -.
DR Proteomes; UP000007060; 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; 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.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Membrane; Phosphoprotein; Protein transport; Repeat;
KW Transport; Vacuole; WD repeat.
FT CHAIN 1..500
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000318011"
FT REPEAT 3..41
FT /note="WD 1"
FT REPEAT 243..283
FT /note="WD 2"
FT REPEAT 288..327
FT /note="WD 3"
FT REGION 174..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 284..288
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 340..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43601"
SQ SEQUENCE 500 AA; 55102 MW; 06B2DFAF842AE933 CRC64;
MSDSSPTINF INFNQTGTCI SLGTSKGFKI FNCEPFGKFY SEDSGGYAIV EMLFSTSLLA
LVGIGDQPAL SPRRLRIINT KKHSIICEVT FPTSILSVKM NKSRLVVLLQ EQIYIYDINT
MRLLHTIETN PNPRGLMAMS PSVANSYLVY PSPPKVINSE IKAHATTNNI TLSVGGNTET
SFKRDQQDAG HSDISDLDQY SSFTKRDDAD PTSSNGGNSS IIKNGDVIVF NLETLQPTMV
IEAHKGEIAA MAISFDGTLM ATASDKGTII RVFDIETGDK IYQFRRGTYA TRIYSISFSE
DSQYLAVTGS SKTVHIFKLG HSMSNNKLDS DDSNMEEAAA DDSSLDTTSI DALSDEENPT
RLAREPYVDA SRKTMGRMIR YSSQKLSRRA ARTLGQIFPI KVTSLLESSR HFASLKLPVE
TNSHVMTISS IGSPIDIDTS EYPELFETGN SASTESYHEP VMKMVPIRVV SSDGYLYNFV
MDPERGGDCL ILSQYSILMD
//
