ID   ATG29_ASHGO             Reviewed;         172 AA.
AC   Q75F26;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Autophagy-related protein 29;
GN   Name=ATG29; OrderedLocusNames=AAL098W;
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: Plays a role in autophagy. Functions at the preautophagosomal
CC       structure (PAS) in order to form normal autophagosomes under starvation
CC       conditions. Also plays a role in mitophagy and regulation of
CC       filamentous growth (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure {ECO:0000250}.
CC       Note=Localizes also to other perivacuolar punctate structures.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG29 family. {ECO:0000305}.
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DR   EMBL; AE016814; AAS50268.1; -; Genomic_DNA.
DR   RefSeq; NP_982444.1; NM_207797.1.
DR   AlphaFoldDB; Q75F26; -.
DR   SMR; Q75F26; -.
DR   STRING; 33169.AAS50268; -.
DR   EnsemblFungi; AAS50268; AAS50268; AGOS_AAL098W.
DR   GeneID; 4618524; -.
DR   KEGG; ago:AGOS_AAL098W; -.
DR   eggNOG; ENOG502S1W0; Eukaryota.
DR   HOGENOM; CLU_121102_0_0_1; -.
DR   InParanoid; Q75F26; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.2570; -; 1.
DR   InterPro; IPR039113; ATG29.
DR   InterPro; IPR040666; Atg29_N.
DR   InterPro; IPR039362; ATG29_sf.
DR   PANTHER; PTHR40012; PTHR40012; 2.
DR   Pfam; PF18388; ATG29_N; 1.
PE   3: Inferred from homology;
KW   Autophagy; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..172
FT                   /note="Autophagy-related protein 29"
FT                   /id="PRO_0000232993"
FT   REGION          87..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   172 AA;  19337 MW;  6C495832D924D141 CRC64;
     MNSKNTIVYV KVPGRQREGF VDPPPFEWNQ HQDRKLWAHI STIEDKDDID WQLLSNQTNA
     PEFFIRKRVY QLFRVHLKSI EQEIYSHTSA DRAPNRSSQA GDEPAASVGV LNGYGQNIND
     IHDLSSLQTP PTCRGKANKD EDGGNSSGIS ELSSLSVSKS ALEEALMDRL QL