ID ATG18_ASPCL Reviewed; 417 AA.
AC A1CBB8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Autophagy-related protein 18;
GN Name=atg18; ORFNames=ACLA_014730;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027049; EAW13036.1; -; Genomic_DNA.
DR RefSeq; XP_001274462.1; XM_001274461.1.
DR AlphaFoldDB; A1CBB8; -.
DR SMR; A1CBB8; -.
DR STRING; 344612.A1CBB8; -.
DR EnsemblFungi; EAW13036; EAW13036; ACLA_014730.
DR GeneID; 4706317; -.
DR KEGG; act:ACLA_014730; -.
DR VEuPathDB; FungiDB:ACLA_014730; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR OMA; SDHCYLA; -.
DR OrthoDB; 391429at2759; -.
DR Proteomes; UP000006701; 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; 2.
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..417
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000317995"
FT REPEAT 1..36
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 312..358
FT /note="WD 6"
FT REPEAT 370..410
FT /note="WD 7"
FT REGION 261..314
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 261..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 45374 MW; B5B5B357E80423F2 CRC64;
MAMNFVTFNQ DYSYLAVATS KGFRIFTTDP FAKSYETKEG HIAIIEMLFS TSLVALILSP
RRLQITNTKR QSTICELTFP TTVLAVKLNR KRLVIVLEDQ IYLYDIQTMK LLYTIQTSPN
PNAICALSPS SDNCYLAYPL PQKAPPSSFT PPSHAPPGNT HVSPTSGEVL IFDSLKLEAI
NVIEAHRSPL ACITLNSDGT LLATASDKGT IIRVFSVPDG HKLYQFRRGS MPSRIFSMSF
NTTSTLLCVS SSTETIHLFK LSQQTSSSRD TSPSSSTPAG RDRAFSQSSL GHSPDRSDVS
GEPDSSEFPA RKHNGTLMGI IRRTSQNVGS TVAAKVGGYL PKGVSEMWEP ARDFAWIKLP
KPSQNAGGSG NNGPLRSVVA MSNNTPQVMV ITSDGNFYVF SIDLSKGGEG TLTKQYS
//
