ID   ATG13_PICGU             Reviewed;         669 AA.
AC   A5DQA8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=ATG13; ORFNames=PGUG_05459;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408161; EDK41361.2; -; Genomic_DNA.
DR   RefSeq; XP_001482439.1; XM_001482389.1.
DR   AlphaFoldDB; A5DQA8; -.
DR   SMR; A5DQA8; -.
DR   STRING; 4929.XP_001482439.1; -.
DR   PRIDE; A5DQA8; -.
DR   EnsemblFungi; EDK41361; EDK41361; PGUG_05459.
DR   GeneID; 5124188; -.
DR   KEGG; pgu:PGUG_05459; -.
DR   VEuPathDB; FungiDB:PGUG_05459; -.
DR   eggNOG; KOG4573; Eukaryota.
DR   HOGENOM; CLU_366802_0_0_1; -.
DR   InParanoid; A5DQA8; -.
DR   OMA; MHQHPRS; -.
DR   OrthoDB; 1519629at2759; -.
DR   Proteomes; UP000001997; 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; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..669
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000317950"
FT   REGION          239..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  74106 MW;  46ACC6E951E48B21 CRC64;
     MEKPKQKLTQ VTVNFFLKTS QMILQARSLD EHGKGKLNKW FNLHTFNSDD LRSELRLWRS
     TIDLTAVPPM IVETYLDLGN LPQGHTLALK DEHGNLWPVT KGGSKKTEVV LERWLVEFDP
     NEFGTIEELP YIYKQAIILC RSIYTIIRIM PAASLRNQSP HYVLANKIVD GSKPISSKGR
     IGLSKTIIPH QMLTDTHVRH RTFSPIETSL GTLKVSVAYR SHCEFTELAE WDHRELGREK
     EPREDLRQVE SKGEEDHSIE SIPYEEKAYK TDEEKSDKTP EHVQYKPFKP EFKQLEAVKL
     EGSDFKSELH EGTSPLSLSG SPSSPPRDDK KRPSIQPFRV GSIGNSPPPA SSSLERRISI
     TSNKSTSNAS LAAVLRNPRS SFSIPIAGSI GTGAPVTGGF PRSVSSSHGY GYEDSDSAAN
     TPRFSSSFGS RASRRFSNTS VRHGSLHDTT SPLGTSAGSA TSIPLSGLYI DDDISDFVRM
     IDSKQDLRFG HDSGGSGSQS GSQYEVLNRF HQLKSQHQQL GDSVNASVMM HRKSSSPPGS
     YESHVPSIHS RLRESSEPHP APATAPAPGP LIKPASKMMS SPVISTTSAH AMSQTASATT
     RDEIVGLATT PSTYRKHLHY ENVFDDDDED EDHHGYFKAK ARSKSLSRSH FDDDDDLLFT
     MSDTNLAKH