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Database: UniProt
Entry: A0A0D2F3U9_9EURO
LinkDB: A0A0D2F3U9_9EURO
Original site: A0A0D2F3U9_9EURO 
ID   A0A0D2F3U9_9EURO        Unreviewed;       506 AA.
AC   A0A0D2F3U9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN   ORFNames=PV04_10722 {ECO:0000313|EMBL:KIW62558.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW62558.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW62558.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW62558.1,
RC   ECO:0000313|Proteomes:UP000054266};
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 Capronia semiimmersa CBS27337.";
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; KN846963; KIW62557.1; -; Genomic_DNA.
DR   EMBL; KN846963; KIW62558.1; -; Genomic_DNA.
DR   EMBL; KN846963; KIW62559.1; -; Genomic_DNA.
DR   STRING; 5601.A0A0D2F3U9; -.
DR   HOGENOM; CLU_028356_0_0_1; -.
DR   OrthoDB; 1940609at2759; -.
DR   Proteomes; UP000054266; 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}.
FT   DOMAIN          48..453
FT                   /note="Autophagy protein ATG17-like"
FT                   /evidence="ECO:0000259|Pfam:PF04108"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          167..205
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          302..329
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   506 AA;  56652 MW;  14A92B048D97C750 CRC64;
     MAQSPHLPTA QRHDLSARSS PSQSLRATSP SQTSVEVLVS YLVASKRSLG SIHLVHRATT
     ILSEARISIE STTALLAKAT YLRRSLTSQL KVLRGVQFEL ETAAQGIQLE FQAVIRELDE
     TGARLLQCID LLKQTKVEHA FKTAIEGELQ DAAGKDTLHD FVDDNGVETI KQAMEVAIDN
     VQSAQQEMND SIQALEADLQ SINEVLNSRA ELSGTESELQ QPFTVAGTLA LLENHAHEMA
     RSLESLVKHF DLCVTAIKHT EGGGEAVFQT MNAEEVDAVG LGMDELQAPA QPMNDEERVE
     MLQVLENDAQ EVDEVVMELQ DRNAEMESQL DKIHRWRERQ ENAYADVATA FKLLDKISGR
     LSGYVAEIAR HAMRWNEEKA KIEDGIGGME ELCEYYAHFL HAYDGLIVEV ARRRTVKKQM
     ERIVAEAHAQ LEQMYESDRQ LRLEFKTDHG EYLPSDIWSG VNTLPPRYAI TRADEEDATS
     VPELPRRTVE EALRRLKNDN SARAGR
//
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