ID A0A1Y2X9Q4_9PEZI Unreviewed; 505 AA.
AC A0A1Y2X9Q4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=K445DRAFT_56259 {ECO:0000313|EMBL:OTB17786.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB17786.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB17786.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB17786.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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 preautophagosomal 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. {ECO:0000256|RuleBase:RU368080}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368080}.
CC Preautophagosomal structure membrane {ECO:0000256|RuleBase:RU368080};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU368080}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the ATG17 family.
CC {ECO:0000256|ARBA:ARBA00006259, ECO:0000256|RuleBase:RU368080}.
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DR EMBL; KZ112932; OTB17786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2X9Q4; -.
DR STRING; 1001832.A0A1Y2X9Q4; -.
DR OrthoDB; 1940609at2759; -.
DR Proteomes; UP000243732; Unassembled WGS sequence.
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; AUTOPHAGY-RELATED PROTEIN 17; 1.
DR PANTHER; PTHR28005:SF1; AUTOPHAGY-RELATED PROTEIN 17; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|RuleBase:RU368080};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368080};
KW Reference proteome {ECO:0000313|Proteomes:UP000243732}.
FT DOMAIN 44..450
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 57047 MW; 5A662CC7B53F7ABE CRC64;
MASIKSQHSS ASVSRPTSQH GVPGSADSVS VETLVRHLLD AKRSLNSMGL VLRANELVHL
AKEAHEESVV LAAQSGFIRQ GINEQIRLLQ HLRRSMNRTY DSGNREFKQI IKTLDAAHGR
LEDTINLLRD RTVDSTFRPP GEGKKNLLDF IDESQVERIN NALKENIQSL QTIQKSFDGD
LLRFDTDMRL LSKTLSGAPS SPSPSASSSE RLLPRLFSSM IQNSQAMAHL LSSLTKHFDL
CVTAVRTTEG GAALARIKAA ETVDSQSGVN VSISGVIAEQ ESHMPEDDPI SPEERAQMLE
VVMQDASEVD DVVRELNLRL QSMEADFATI DSQRNQVKTT YRSTIDAFKV LEDIGMRLPS
YISAEVEFRD RWDEEQSSIQ EKLREMDELR IFYESYSNSY DGLILEVERR RALQEKVVSI
WKKAKESVDK LYETDRKERE LFRQEVAEYL PTDLWPGMDD DMVRWEIMPV RDSRPARQYE
GGNSPNLEGS VVEATEPRYR PTSGV
//