ID   ATG17_BOTFB             Reviewed;         500 AA.
AC   A6SG03;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Autophagy-related protein 17;
GN   Name=atg17; ORFNames=BC1G_11270;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476929; EDN32858.1; -; Genomic_DNA.
DR   RefSeq; XP_001549800.1; XM_001549750.1.
DR   AlphaFoldDB; A6SG03; -.
DR   SMR; A6SG03; -.
DR   PRIDE; A6SG03; -.
DR   GeneID; 5430276; -.
DR   KEGG; bfu:BCIN_07g06790; -.
DR   VEuPathDB; FungiDB:Bcin07g06790; -.
DR   OMA; SSINHVW; -.
DR   OrthoDB; 1496047at2759; -.
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.
FT   CHAIN           1..500
FT                   /note="Autophagy-related protein 17"
FT                   /id="PRO_0000317983"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          157..181
FT                   /evidence="ECO:0000255"
FT   COILED          292..322
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  56338 MW;  52797C21773EAFE1 CRC64;
     MASSPNAPGS HSHTSISTVN PPPPAHTNQG LEIPLETLVS HLLASKRSLS SISTVWRANE
     IVTSAKNALE ESAILQAKTR FLQSGINEQM KTLLKVRKTV EFVYNDGQED FSNVLHNLDA
     ADARLESTMN MLRSTMVDAA FRPAGEEPRN LLDFVDEQGV EKMRDGLKEL IDESKEAEAA
     FGTSILSFDS DIRSLKSGFK NSKRKTSSYS PIPNHLYTLE GHAQEMASLL SSLSSHFDLC
     LNAIRHTEGG YAAVRNAASN PPPGAEPVSV SGVMSNSHDD INEAPLTEHE REEMFSILEK
     DAAEVEDVVM ELHDRQNEME AKHDAILDHV SHLAEQFRHT ASVYKTLEGV YQRLPRYILA
     GHDFRARWED TKVHINEQMN ELEGMRLFYE NYLSSYDGLI LEVHRRTVAE EKARSIAKKA
     MEQINKIYDI DVKERNDFKF DVGDYLPVDL YPGISEAPPK WDFRLVEDEE GGSSTPLLER
     SVVKESFKRD RERHRNSKDN