ID   ATG13_YEAS7             Reviewed;         738 AA.
AC   A6ZX59;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=ATG13; Synonyms=APG13; ORFNames=SCY_5886;
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: Activates the ATG1 kinase in a nutritional condition
CC       dependent manner through the TOR pathway, leading to autophagy.
CC       Required for autophosphorylation of ATG1 at 'Thr-226' and its
CC       dimerization. May also be involved in the regulation of autophagy
CC       through SNF1. Involved in ATG9 and ATG23 cycling through the pre-
CC       autophagosomal structure. Also involved in cytoplasm to vacuole
CC       transport (Cvt) and more specifically in Cvt vesicle formation. Seems
CC       to play a role in the switching machinery regulating the conversion
CC       between the Cvt pathway and autophagy. Finally, ATG13 is also required
CC       for glycogen storage during stationary phase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Hypophosphorylated form interacts with ATG1 to form the ATG1-
CC       ATG13 kinase complex. The ATG1-ATG13 complex interacts with the ATG17-
CC       ATG29-ATG31 complex through direct interaction with ATG17. Interacts
CC       with VAC8. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC       Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC   -!- PTM: Phosphorylated; hyperphosphorylated by the TORC1 kinase complex to
CC       repress the induction of autophagy. Starvation and TOR inactivation
CC       results in ATG13 partial dephosphorylation leading to ATG1-binding.
CC       Rephosphorylated by ATG1 during prolonged nitrogen starvation. Also
CC       phosphorylated by TPK1; TPK1 phosphorylation regulates the association
CC       of ATG13 with the PAS. Within this regulatory network, mitochondrial
CC       respiratory deficiency suppresses autophagic flux. Hyperphosphorylation
CC       in rich medium is impaired in the absence of VAC8. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFW02000135; EDN61301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZX59; -.
DR   SMR; A6ZX59; -.
DR   PRIDE; A6ZX59; -.
DR   EnsemblFungi; EDN61301; EDN61301; SCY_5886.
DR   HOGENOM; CLU_411076_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:InterPro.
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; 3.30.900.10; -; 1.
DR   InterPro; IPR040182; ATG13.
DR   InterPro; IPR018731; Atg13_N.
DR   InterPro; IPR036570; HORMA_dom_sf.
DR   PANTHER; PTHR13430; PTHR13430; 1.
DR   Pfam; PF10033; ATG13; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Phosphoprotein; Protein transport; Transport.
FT   CHAIN           1..738
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000317954"
FT   REGION          279..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..520
FT                   /note="Interaction with ATG1"
FT                   /evidence="ECO:0000250"
FT   REGION          521..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         344
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         348
FT                   /note="Phosphoserine; by TORC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         437
FT                   /note="Phosphoserine; by TORC1 and PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         438
FT                   /note="Phosphoserine; by TORC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         535
FT                   /note="Phosphoserine; by TORC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         541
FT                   /note="Phosphoserine; by TORC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         554
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         581
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         646
FT                   /note="Phosphoserine; by TORC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
FT   MOD_RES         649
FT                   /note="Phosphoserine; by TORC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q06628"
SQ   SEQUENCE   738 AA;  83316 MW;  F113E53F89E3E9EA CRC64;
     MVAEEDIEKQ VLQLIDSFFL KTTLLICSTE SSRYQSSTEN IFLFDDTWFE DHSELVSELP
     EIISKWSHYD GRKELPPLVV ETYLDLRQLN SSHLVRLKDH EGHLWNVCKG TKKQEIVMER
     WLIELDNSSP TFKSYSEDET DVNELSKQLV LLFRYLLTLI QLLPTTELYQ LLIKSYNGPQ
     NEGSSNPITS TGPLVSIRTC VLDGSKPILS KGRIGLSKPI INTYSNALNE SNLPAHLDQK
     KITPVWTKFG LLRVSVSYRR DWKFEINNTN DELFSARHAS VSHNSQGPQN QPEQEGQSDQ
     DIGKRQPQFQ QQQQPQQQQQ QQQQQQRQHQ VQTQQQRQIP DRRSLSLSPC TRANSFEPQS
     WQKKVYPISR PVQPFKVGSI GSQSASRNPS NSSFFNQPPV HRPSMSSNYG PQMNIEGTSV
     GSTSKYSSSF GNIRRHSSVK TTENAEKVSK AVKSPLQPQE SQEDLMDFVK LLEEKPDLTI
     KKTSGNNPPN INISDSLIRY QNLKPSNDLL SEDLSVSLSM DPNHTYHRGR SDSHSPLPSI
     SPSMHYGSLN SRMSQGANAS HLIARGGGNS STSAFNSRRN SLDKSSNKQG MSGLPPIFGG
     ESTSYHHDNK IQKYNQLGVE EDDDDEDDRL LNQMGNSATK FKSSISPRSI DSISSSFIKS
     RIPIRQPYHY SQPTTAPFQA QAKFHKPANK LIDNGNRSNS NNNNHNGNDA VGVMHNDEDD
     QDDDLVFFMS DMNLSKEG