ID   ATG13_PICST             Reviewed;         779 AA.
AC   A3LQY1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=ATG13; ORFNames=PICST_83006;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- FUNCTION: Activates the ATG1 kinase in a nutritional condition
CC       dependent manner through the TOR pathway, leading to autophagy. Also
CC       involved in cytoplasm to vacuole transport (Cvt) and more specifically
CC       in Cvt vesicle formation. Seems to play a role in the switching
CC       machinery regulating the conversion between the Cvt pathway and
CC       autophagy. Finally, ATG13 is also required for glycogen storage during
CC       stationary phase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ATG1 to form the ATG1-ATG13 kinase complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC       Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC   -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000497; ABN65294.2; -; Genomic_DNA.
DR   RefSeq; XP_001383323.2; XM_001383286.1.
DR   AlphaFoldDB; A3LQY1; -.
DR   SMR; A3LQY1; -.
DR   STRING; 4924.XP_001383323.2; -.
DR   PRIDE; A3LQY1; -.
DR   EnsemblFungi; ABN65294; ABN65294; PICST_83006.
DR   GeneID; 4838362; -.
DR   KEGG; pic:PICST_83006; -.
DR   eggNOG; KOG4573; Eukaryota.
DR   HOGENOM; CLU_366802_0_0_1; -.
DR   InParanoid; A3LQY1; -.
DR   OMA; YAKLHRP; -.
DR   OrthoDB; 1519629at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
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; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..779
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000317951"
FT   REGION          298..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  84521 MW;  F9AF3F4E4EA82A7D CRC64;
     MASQDISYQY KSQQEHYPNE KISDSYVQKQ NSKLTQVIQQ CFSKAVKIII QSRTVPPAAA
     SPLLNPALHD DSASGNKINR WFNLHIQNSQ DLPKDDLKLW KSNHLQSMPP MIIETYLDLR
     QLTSSQTIVL NDDNGNPWAV AKSGGKKQEV VLERWLIEFD HTDASGSIVD ELPLIYKQAI
     ILFRSIYGFA RLMPAFKLKK RLLINKSSTK LNKLTIGNKI LDGKQPISSK GRIGLSKTII
     PRQMLTTDSH MSQKHFQPIQ TSLGTLKISI AYRNHCDFCI HDNEEVLSTH FISMDSTPLT
     ESGHGHTKAN NTSMSVSPCS SGHPALREGS PTKRGTPPTA IQPFKVGSIS NSPPPASHTP
     NSGYGGSLER RISITSNRST SNASLFAMLR NPRSSTSSTH TTSNIPIAPS SSSNSTNATN
     MNNMSYPRSI SSSHGSNMQH DDSMFSNPDS TTNTPRFSSS FGSRASRRYS NTSVRQSTPV
     AASTLTGGSP LSGLYIDDDI SEFVRSIDSK ADLRFSNSYT AHNSGEPKNN MGSPSGGDAL
     NKFQMMKSHH QQLGDSVNAS LILQHNNAVS GSGSGFGVSN SRHSSTSRKS SHSIRSPSPS
     MSGLYDVVPG SYGRSERRSS SGAGVPGQLS LPSGGGLAAH SPSATEPTSA ATITPRETNF
     NFSNASFLRS ASKLSATPVT STTTAHATIH SVTGMATSPS LYQRTKVGSS IHYENVFEDD
     DDDEMVMKKP VVTSSGRDEE QLQHKQMKVV SIEKDAGANN FDDDDLLFTM SDMNLTKSS