ID U4LQ52_PYROM Unreviewed; 495 AA.
AC U4LQ52;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=PCON_02563 {ECO:0000313|EMBL:CCX34085.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX34085.1};
RN [1] {ECO:0000313|EMBL:CCX34085.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX34085.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX34085.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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; HF936296; CCX34085.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LQ52; -.
DR STRING; 1076935.U4LQ52; -.
DR eggNOG; ENOG502RYHP; Eukaryota.
DR OMA; WRANDIV; -.
DR OrthoDB; 1940609at2759; -.
DR Proteomes; UP000018144; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368080}.
FT DOMAIN 46..443
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 133..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 56521 MW; 395B2B6B6B9BCBE4 CRC64;
MPPPLSPSQY SDPHLDLRRS MNPDIPQIHI PPEELTTWFL NAKRSLTHVT LCSRAHVLVD
NARGALQEAN VISSRCGFLR SNLGDQLRIS KEINKMMHKT TDVAHERIQE TITKLEAAHF
HLNQTLQHLK SFPVDPAFTN PTTPDDSEYR SDEHSQHRPD RLDRLDRSVH RGKQPAQPSP
PRRSLDDFVS HKGTEQISNA LRDLIDDSEK CHSDFTNSLG LFDSSLSFLA NSLASVPNLD
PRDEPFHPPL NALEQRTEAM ASLIQSLTQH FDRCGLALKG SESDMQVDPD LFLVLSRDAA
QVDDVVAELK EILEEMEDIS VGIDSKLGEL RRFEDGIIRI LVAFEDHQIE LAAYLDGLRM
FESRQKELKY DMEARLEELK AFREFYDGFK GAYDAMVVEV GRRQGVQVRM ENIVKEAMRQ
VKELYDEDQE KREIFLEDNS DLLPVDIWAG IRDPPVRWEI TRDLQGGTEL PQLGKDVIEK
AMRRHNAAKA ATRKL
//
