ID A0A1Q8RGS0_9PEZI Unreviewed; 523 AA.
AC A0A1Q8RGS0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=CCHL11_03076 {ECO:0000313|EMBL:OLN83363.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN83363.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN83363.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN83363.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLN83363.1}.
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DR EMBL; MPGH01000204; OLN83363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RGS0; -.
DR STRING; 708187.A0A1Q8RGS0; -.
DR OrthoDB; 1940609at2759; -.
DR Proteomes; UP000186583; 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:UP000186583}.
FT DOMAIN 60..466
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..523
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"
FT COMPBIAS 509..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 58426 MW; 08505C9142E85A68 CRC64;
MANSPSHKSS RSPASSTSAD RESLSHSRDR RDAPSSTSVS AADAVPVETL VEHLLAAKRS
LSSMTAVLRA NEIATEARQA HEEAVVLYAE SQFLQRAISE QLAILARVRR GLKKTYDAGK
RDFKNLVKTM DATNEKLQDT MAMLKNTTVE AVFRPPGEGR RNLMDFVDEK SVHVMVEALK
QSLGELQAIQ TSFDGDLLRF DDDLRALKKT IAASPLRRTP SDSSSYDPIP ERLGSLVDHS
HAMAQLLTSL TKHFDLCVTA VRTTEGGAAL ARRRAAEVTQ SQGGDGVSIS GVIADQESHM
PDLEPTTTQD RADMLEIVVS DASEVDSVIQ EINERLHAME DDFAEMTQET EQIKAAFLGT
LDAFAALEDM GGRMSSYIAS EAEFLQRWED ERYTIYGKLG EMDDLRDFYE KYSGAYDNLI
LEVERRRLVE DKIQNIWKKA KDNVDRLIEN DRRERDGFRQ DIGEFIPTDL WPGMDAGMKR
WEIVAVDDGM ADEDNTGTQR STPALDRSVV DAARDRLERS QQR
//