ID   ATG13_YARLI             Reviewed;         715 AA.
AC   Q6C315;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=ATG13; OrderedLocusNames=YALI0F03432g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382132; CAG77754.1; -; Genomic_DNA.
DR   RefSeq; XP_504947.1; XM_504947.1.
DR   AlphaFoldDB; Q6C315; -.
DR   SMR; Q6C315; -.
DR   STRING; 4952.CAG77754; -.
DR   EnsemblFungi; CAG77754; CAG77754; YALI0_F03432g.
DR   GeneID; 2907738; -.
DR   KEGG; yli:YALI0F03432g; -.
DR   VEuPathDB; FungiDB:YALI0_F03432g; -.
DR   HOGENOM; CLU_007151_0_0_1; -.
DR   InParanoid; Q6C315; -.
DR   OMA; MHQHPRS; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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..715
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000157971"
FT   REGION          329..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  76855 MW;  32E01C803B0F84F7 CRC64;
     MSFQGTSSGS SHSSKSKLNQ VVQNFFSKAT QVVVQARLNP RLREQRQSGD KHKLNKWFNL
     ETDELEAYRE DLKLWRTIDI YNMDKMPPVV VETYLDMRHL SPNQTLVLED AFGKRWNASF
     GGRKTEVVLE RWVIEIQRPD PQAGGATTSP ASSTELPMAY KKCILLFRSL YTYCRLLPAW
     TLQKRLSKSK LSTSPLRIGC RVLNGSQPIS SRGRVGLSKL IAGSSESQHL QTFSFDPVEI
     PSGVFKISVS YRVNCNFAVD DSEAMLSSQF LRIDEEKPVV PPSPPVKHPS MAAPNLHYIT
     GLPRRHSHSQ GVGVSGAAIV PTSVSSVTDY MERRRSSGAS GVGATGGGLA GTSGGSGGVS
     GGVSGGSGGS GGSGGWGGEE GSPGPAATSA SPSTPPFARV PSSSSLAALR IPRRTISNSS
     TSSTNNARVV TTPGYTPSAY EQAISSSGGS SRSGSVPKYS SSFGTRQWNR SGSISSTRRR
     NSMLVGSAES AMSSGSSLME PGSGFIDIED PTDVSDFVKM VDSIKPGSPY SLPSPRKGSD
     PLARFQQLKG SHAGIADSIT SSIYHHQPSP PYVRSKLSGE ANLEAISSLP RPVTVPPSPR
     KLETQMQPIS LADQHTSEYH QLQQRTSARP QAHSYSERDQ LDNSHYKALE RYDLVGASPS
     VVGSRYYTEH DRGRGEKRYS VAPLPGLEFD EDDDLLFAMS DMAMGDSASG GNVRT