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
//