ATG18_NEOFI
ID ATG18_NEOFI Reviewed; 429 AA.
AC A1DE24;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Autophagy-related protein 18;
GN Name=atg18; ORFNames=NFIA_075610;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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|UniProtKB:P43601}.
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; DS027696; EAW17631.1; -; Genomic_DNA.
DR RefSeq; XP_001259528.1; XM_001259527.1.
DR AlphaFoldDB; A1DE24; -.
DR SMR; A1DE24; -.
DR STRING; 36630.CADNFIAP00006442; -.
DR EnsemblFungi; EAW17631; EAW17631; NFIA_075610.
DR GeneID; 4585990; -.
DR KEGG; nfi:NFIA_075610; -.
DR VEuPathDB; FungiDB:NFIA_075610; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR OMA; PSRDFAW; -.
DR OrthoDB; 1216824at2759; -.
DR Proteomes; UP000006702; 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 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..429
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000318003"
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 309..355
FT /note="WD 6"
FT REPEAT 367..407
FT /note="WD 7"
FT REGION 262..308
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 262..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 46744 MW; 223EA1FDC35DDE71 CRC64;
MAMNFVTFNQ DYSYLAVATS KGFRIFTTDP FAKSYETKEG NIAIIEMLFS TSLVALILSP
RRLQITNTKR QSTICELTFP TTVLAVKLNR KRLVIVLEDQ IYLYDIQTMK LLYTIQTSPN
PNAICALSPS SDNCYLAYPL PQKAPPSSFN PPSHTPPGST HVSPTSGEVL IFDTLKLEAI
NVIEAHRSPL ACITLNSDGT LLATASDKGT IIRVFSVPDG HKLYQFRRGS MPSRIFSMSF
NTTSTLLCVS SSTETIHLFK LSHPTSSPDA SPSSPVGRDR SLSQSSSGYS PDRGDLTGDV
GSSDFPARKH NGTLMGMIRR TSQNVGSTVA AKVGGYLPKG VSEMWEPTRD FAWFKLPKPN
QTSGGSVNNG PLRSVVAMSS NTPQVMVVTS DGNFYVFSID LSKGGEGTLT KQYSVLESND
RLGYSVTDY
