ID A0A1V6TH59_9EURO Unreviewed; 542 AA.
AC A0A1V6TH59;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=PENSTE_c006G08363 {ECO:0000313|EMBL:OQE25516.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE25516.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
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:OQE25516.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLKD01000006; OQE25516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TH59; -.
DR STRING; 303698.A0A1V6TH59; -.
DR OrthoDB; 1940609at2759; -.
DR Proteomes; UP000191285; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT DOMAIN 40..457
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 483..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60163 MW; 4B595DA159384FA4 CRC64;
MSSQSSSASI ARGGTGYSEQ DALPSLETLV SYLIVAKRGL SSYHYVWRAN EIVTEARTAL
EDSVVVSSRT TFLRRGLNSQ LRLLYNIRSE VADISKRGRS EFSDALKNLD AADARLRDTL
DLLRETIVHA SFRPKEEQPR SLHDFVDERG VEELHTAMKD SIDRTNTARG DLDTSNREFD
DELESIRQAL HRYRSATKLA SSRASVSSSS PSASESDLQA VSSMPGMLQS LEEHARKMAR
NLESLANHFD LCVKVLKHTE GGGAAARSIT GDMPTDVSGE GVLKIEEALD APQAPISEKA
YRDMLEVIVN DTPVAEDVVI EFQDRINEME TIFEQVMVQR DALISISNAS LDVHRHLSNL
ASTGLPRYIA QAHNFTRVWN EENERINSGL IELSDLHALY EGFLNAYDSL ILEVARRSQV
RKRVEKVLQD TQHKLSQLHE EDVIAREAFR IEQGDFLPSD IWPGIGRAPM QVEFLRVSGG
QLESARGNED GNQTQDADAG ASTKITTTGD TSEGEIIPAL PKDVIEQAFS RVRARTRDLA
QG
//
