ATG17_ASHGO
ID ATG17_ASHGO Reviewed; 413 AA.
AC Q757A7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Autophagy-related protein 17;
GN Name=ATG17; OrderedLocusNames=AER106C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG17 family. {ECO:0000305}.
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DR EMBL; AE016818; AAS52790.1; -; Genomic_DNA.
DR RefSeq; NP_984966.1; NM_210320.1.
DR AlphaFoldDB; Q757A7; -.
DR SMR; Q757A7; -.
DR STRING; 33169.AAS52790; -.
DR PRIDE; Q757A7; -.
DR EnsemblFungi; AAS52790; AAS52790; AGOS_AER106C.
DR GeneID; 4621171; -.
DR KEGG; ago:AGOS_AER106C; -.
DR eggNOG; ENOG502QQDW; Eukaryota.
DR HOGENOM; CLU_051526_0_0_1; -.
DR InParanoid; Q757A7; -.
DR OMA; YLPENIW; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IEA:EnsemblFungi.
DR GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0045772; P:positive regulation of autophagosome size; IEA:EnsemblFungi.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
DR InterPro; IPR007240; Atg17.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR28005; PTHR28005; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..413
FT /note="Autophagy-related protein 17"
FT /id="PRO_0000124555"
FT COILED 262..300
FT /evidence="ECO:0000255"
SQ SEQUENCE 413 AA; 47998 MW; 7F94482AA8877A39 CRC64;
MSSSNQVKGF YFNAQRRLSR AQALCQNSQD TLHNMQLLLV RWQRTVSKLQ FTIHCICNQT
VFLAECILKK TVGQQLIETE WKRMLLDELQ GEMQRSQEEI TGKIDALRRT KNELDGSGAT
LADFISMENI FLLGDKLKDV PVVQEQVEHI KVQYESLVDK VVEQLQNNRV RKLEADFAAA
FRSGKNDFNA FSMKYLQKIR QLETDLADIL KSLTDHYDKC SLLKAGDLPA AEQAELFEVV
KNDDQELDSI MGVLEVIVRD IKSLAKNVSI RLRQKERDKQ QLKNAMGKAH SELLKYEEHL
TVFQGIDDLI RNFKASCLHN VSKVRELCEF YDNFLNSYQV LLREVERRRR VAKQMEDILQ
ACEGQLMALS DTDLKQRQQF LMRHGDYLPE NIWPGNIDDL SPLYDLEYRI KKV