ID   ATG17_ASPNC             Reviewed;         546 AA.
AC   A2QCV0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Autophagy-related protein 17;
GN   Name=atg17; ORFNames=An02g04820;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Autophagy-specific protein that functions in response to
CC       autophagy-inducing signals as a scaffold to recruit other ATG proteins
CC       to organize pre-autophagosomal structure (PAS) formation. Modulates the
CC       timing and magnitude of the autophagy response, such as the size of the
CC       sequestering vesicles. Plays particularly a role in pexophagy and
CC       nucleophagy (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC       structure membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG17 family. {ECO:0000305}.
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DR   EMBL; AM270009; CAK47659.1; -; Genomic_DNA.
DR   RefSeq; XP_001399620.1; XM_001399583.2.
DR   AlphaFoldDB; A2QCV0; -.
DR   SMR; A2QCV0; -.
DR   PaxDb; A2QCV0; -.
DR   EnsemblFungi; CAK47659; CAK47659; An02g04820.
DR   GeneID; 4978971; -.
DR   KEGG; ang:ANI_1_2516024; -.
DR   VEuPathDB; FungiDB:An02g04820; -.
DR   HOGENOM; CLU_028356_0_0_1; -.
DR   Proteomes; UP000006706; Chromosome 4R.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:UniProt.
DR   InterPro; IPR007240; Atg17.
DR   InterPro; IPR045326; ATG17-like_dom.
DR   PANTHER; PTHR28005; PTHR28005; 1.
DR   Pfam; PF04108; ATG17_like; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Cytoplasm; Membrane; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Autophagy-related protein 17"
FT                   /id="PRO_0000317980"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          312..341
FT                   /evidence="ECO:0000255"
FT   COILED          424..447
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   546 AA;  59779 MW;  F936024A06AD6CD0 CRC64;
     MSASASLSAG SDASGPGSPA GDQGNALPQL DSLISHLVAA KRSLSSINHV WRANEIVTSA
     RSALEESVVI SARTGFLRRG LNNQLRLLYS VRSEVEEVSL RGRSEFASVL KSLDTADARL
     RKTLDSLRDT IVHASFRPEG EEPRSLHDFV DERGVEELRA ALKSSIDRTN EAQAELDTSN
     SAFDDELQSI KQALGNYREA TKLASSSSSS SSASNSSLPS LSSMPPMLQS LEMHAQEMAN
     LLESLVQHFD LCVTAVKHTE GGGAAARSIT GDMPAAVTVS GRGVPNIEQG IHDNLNAPLD
     PLSESDYQEM VNVLIKDAAE AEDVVMEIQD RIGDMESILE NILSQRDVLL SIYNATIGVF
     RHLSSLATAR LPGYIAQAHS FTRVWGEEHD RINGGLADLS DLNTLYDGFL EAYDGLILEV
     ARRRHVRQRV EKVLRETKHK LDQLYEEDVN ARETFRVEQG DYLPSDIWPG IGREPMRIEF
     RRISGGILKG APPEQPDAQD QPAAEPNEPQ SGPSETTEEG EIIPHLPKSL VEEALHRLKA
     RNRQAM