ID A0A2G5HQU4_CERBT Unreviewed; 509 AA.
AC A0A2G5HQU4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=CB0940_08725 {ECO:0000313|EMBL:PIA94917.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA94917.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA94917.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA94917.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) 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:PIA94917.1}.
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DR EMBL; LKMD01000104; PIA94917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HQU4; -.
DR OrthoDB; 1940609at2759; -.
DR Proteomes; UP000230605; Chromosome 6.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368080}.
FT DOMAIN 43..464
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 COILED 320..368
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 509 AA; 56834 MW; DEFB23B0F6EFA7CA CRC64;
MSSDSSSAEL SASPSPSPPR SPVTHHLPGL QDLVVHFVDA KKSLSATSHV YRANEVVTNS
RALIEEIAVL NAKNTYARRG LDEQVSTLEA IREALVDDGT KISDEFDVTI ADLDKAHARL
DKTLSQLRKT IVAERHSLSR QRTNDTVTNA AEKSDEDENK TLFDFVDEDT HENLLSTLRS
LIDQYNDARG DLNDNLSSFE SSIHSIKDKL LENAGGASTL KPEKPTIYDN PPPSISSIFE
GMEEHATEMA GLLENLVNHY DLCVSALKHT EGGGEAARAA TADMKEATPG TEESLYDKTV
AEAISDEERV EMLQVLLKDA QEVDDVVAEI RDRASEMEDQ YSLLTKYAKK ARAQHQSLQQ
VLETMREIRA AIPGHLDAAG HFRERWQSIS VDIRAKTQEL AELSVFYEQF LAGYGKLLRE
VERRKVSELA MKKIVEKARK DLDRLHETDR VAREEFMEDV GAYLPRDLGV WHGLDEEPLR
WDVRPVYDER SLGEEDVGGQ GSPRLLDGS
//
