ID   ATG18_EMENI             Reviewed;         429 AA.
AC   Q5BH53; C8VQJ6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=atg18; ORFNames=AN0127;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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   -!- SEQUENCE CAUTION:
CC       Sequence=EAA65305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000004; EAA65305.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF90145.1; -; Genomic_DNA.
DR   RefSeq; XP_657731.1; XM_652639.1.
DR   AlphaFoldDB; Q5BH53; -.
DR   SMR; Q5BH53; -.
DR   STRING; 162425.CADANIAP00002619; -.
DR   EnsemblFungi; CBF90145; CBF90145; ANIA_00127.
DR   EnsemblFungi; EAA65305; EAA65305; AN0127.2.
DR   GeneID; 2875905; -.
DR   KEGG; ani:AN0127.2; -.
DR   VEuPathDB; FungiDB:AN0127; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_0_1; -.
DR   InParanoid; Q5BH53; -.
DR   OMA; PSRDFAW; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; 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: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..429
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000050866"
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          267..309
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..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  46877 MW;  9ACB092403ABBF5C CRC64;
     MTMNFVTFNQ DYSYLAVATS KGFRIFTTDP FAKSYETKDG NIAIIEMLFS TSLVALILSP
     RRLQITNTKR QSTICELTFP TTVLAVKLNR KRLVIVLEDQ IYLYDIQTMK LLYTIETSPN
     PNALCALSPS SENCYLAYPL PQKAAPSSFN PPAHAPPGNT HVSPTSGEVL IFDTLKLEAI
     NVIEAHRSPL ACITLNSDGT LIATASDKGT IIRVFSVPDG HKLYQFRRGS IPSRIFSMSF
     NTTSTLLCVS SSTETIHLFK LSQPSQLQET SSANTSSTGR RRSLSSLSQS PEREATEEDN
     GSSDLASRKH NGTLMGMLRR TSQNVGGAFA AKVGGYLPKG VSEMWEPARD FAWIKIPKPN
     QGQGPNANTG PLRSVVAMSS NTPQVMVVTS DGNFYVFSID LSKGGEGTLT KQYSVLESND
     RLGYSVADY