ID   ATG29_YEAS7             Reviewed;         209 AA.
AC   A6ZW87;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Autophagy-related protein 29;
GN   Name=ATG29; ORFNames=SCY_5564;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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   -!- SUBUNIT: Forms a stable complex with ATG17 and ATG31. Interacts
CC       directly with ATG31. The ATG17-ATG29-ATG31 complex interacts with the
CC       ATG1-ATG13 complex. Note=The interaction with the ATG1-ATG13 complex is
CC       induced by starvation. {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; AAFW02000135; EDN60979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZW87; -.
DR   SMR; A6ZW87; -.
DR   EnsemblFungi; EDN60979; EDN60979; SCY_5564.
DR   HOGENOM; CLU_121102_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
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; 1.
DR   Pfam; PF18388; ATG29_N; 1.
PE   3: Inferred from homology;
KW   Autophagy; Phosphoprotein; Protein transport; Transport.
FT   CHAIN           1..209
FT                   /note="Autophagy-related protein 29"
FT                   /id="PRO_0000318061"
FT   REGION          156..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12092"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12092"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12092"
SQ   SEQUENCE   209 AA;  24172 MW;  97B6E1C52DBD75D8 CRC64;
     MNSTNTVVYI KVKGKRPQGF LDPPKFEWNG TKERQLWTMV SNLNYSQDQI DWQNLSKIFE
     TPEFFLKKRT YKLFAEHLEL LQLQLEKKRD LEKYSNDQVN EGMSDLIHKY IPTLQNDNLL
     NVSASPLTTE RQDSEEVETE VTNEALQHLQ TSKILNIHKK TSDSENKPND KLDKDGINKE
     MECGSSDDDL SSSLSVSKSA LEEALMDRL