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Database: UniProt
Entry: A0A0D1YIU9_9EURO
LinkDB: A0A0D1YIU9_9EURO
Original site: A0A0D1YIU9_9EURO 
ID   A0A0D1YIU9_9EURO        Unreviewed;       495 AA.
AC   A0A0D1YIU9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN   ORFNames=PV08_07651 {ECO:0000313|EMBL:KIW14866.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW14866.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW14866.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW14866.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-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 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. {ECO:0000256|ARBA:ARBA00024948}.
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; KN847496; KIW14866.1; -; Genomic_DNA.
DR   RefSeq; XP_016235082.1; XM_016381980.1.
DR   AlphaFoldDB; A0A0D1YIU9; -.
DR   STRING; 91928.A0A0D1YIU9; -.
DR   GeneID; 27334734; -.
DR   VEuPathDB; FungiDB:PV08_07651; -.
DR   HOGENOM; CLU_028356_0_0_1; -.
DR   OrthoDB; 1940609at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT   DOMAIN          43..447
FT                   /note="Autophagy protein ATG17-like"
FT                   /evidence="ECO:0000259|Pfam:PF04108"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          296..323
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   495 AA;  55195 MW;  A9AE293000EA06F5 CRC64;
     MAQSPYLAQQ RSAQPSPSQS LHAASPPVNI ETIVSYLVAS KRSLGSIHLV HRATSILAEA
     RASIESTTAL LAKTTYLRRA LASQLKTLRG VLEELDSAAQ GIQHEFETII QELDDTGARL
     LQCIDFLKET AIEEAFRSST EAEGNTGKVT LHDFVDDNGV EQIKHAMRAA IDNVQNDQHE
     INQSIQTLEE DLQSINDVLV NRVNDSGGES DLKQPVSATL SILEHHAKEM AQGLESLVKH
     FDLCVTAIKH TEGGGEAVVQ TMNANAEDLP DKVGMGMEEL QAAAQPMNEE ERTEMLQVLE
     NDANEVDEVV MELQDRHAEM EAQLDRIAQW REQQEIVYAD VTTAFRLMDK ISGRLSGYVA
     ETARHASRWN EEKAKIEDGI GGMEELCDYY ANFLHAYDGL IVEVDRRRAA KKAMERVVAQ
     AHGQLDQLYE SDRQLRIKFR ENLGEYLPGD IWPGVNDLPP RFEINRVDAG FEASVPDIPR
     RTVDEAARRF SKGRS
//
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