ID   ATG17_SCLS1             Reviewed;         492 AA.
AC   A7EM16;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Autophagy-related protein 17;
GN   Name=atg17; ORFNames=SS1G_06363;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
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; CH476628; EDO03882.1; -; Genomic_DNA.
DR   RefSeq; XP_001592124.1; XM_001592074.1.
DR   AlphaFoldDB; A7EM16; -.
DR   SMR; A7EM16; -.
DR   STRING; 665079.A7EM16; -.
DR   GeneID; 5488443; -.
DR   KEGG; ssl:SS1G_06363; -.
DR   VEuPathDB; FungiDB:sscle_13g092360; -.
DR   InParanoid; A7EM16; -.
DR   OMA; SSINHVW; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
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; Cytoplasm; Membrane; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Autophagy-related protein 17"
FT                   /id="PRO_0000317988"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  55103 MW;  489BFB17409A7F64 CRC64;
     MASPTNAPGS QSQTSVSSAN HPDPIIHGRE ILETLVSHLL ASKRSLSSIS TVWRANEIVT
     SAKTALEESV ILNARTGFLQ SGINEQMKVL MKVRNSIECV YNDGQKDFKN VLHTLDAANA
     RLESTMDVLR STMVDAAFRP AGEEPRSLLD FVDEQGVEGM RDGLKELIRE SKETQKEFDT
     SLLSFDDDLR SLRSGFKNTK VSPPSYSPIP SHLATLEGHA QEMAALLSSL SSHFDLCLNA
     IRHTEGGYAA VRNAASNPPP GAEPVSVSGV MNTSHDDINE EPLTEHEREE MLFVLEKDAA
     EVEDVVMELR DRQNEMEIKH DAILDHVSHL TEQFKQTTSI YKILEGVYER LPGYIIAGQD
     FRARWEDTKA QICGQMDDLE GMRLFYENYL SSYDGLILEV RRRKVAEEKA KTIAKKAMEQ
     ISKIYDADMK ERHDFKHDVG DYLPVDLYPG INAAAPRWEF RLMEDEEAVN SSPSLERELV
     EVSSKRDGEA QG