ID   ATG13_PENRW             Reviewed;         974 AA.
AC   A7KAM4; B6GWT6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=atg13; ORFNames=Pc12g10930;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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       ECO:0000269|PubMed:17204848}.
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; EF107746; ABO31084.1; -; Genomic_DNA.
DR   EMBL; AM920427; CAP80720.1; -; Genomic_DNA.
DR   RefSeq; XP_002557913.1; XM_002557867.1.
DR   AlphaFoldDB; A7KAM4; -.
DR   SMR; A7KAM4; -.
DR   STRING; 1108849.XP_002557913.1; -.
DR   EnsemblFungi; CAP80720; CAP80720; PCH_Pc12g10930.
DR   GeneID; 8313155; -.
DR   KEGG; pcs:Pc12g10930; -.
DR   VEuPathDB; FungiDB:PCH_Pc12g10930; -.
DR   eggNOG; KOG4573; Eukaryota.
DR   HOGENOM; CLU_007151_1_0_1; -.
DR   OMA; MHQHPRS; -.
DR   OrthoDB; 1519629at2759; -.
DR   BioCyc; PCHR:PC12G10930-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c12.
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..974
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000317947"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..844
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..871
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  104030 MW;  E8DF0336DBC744F9 CRC64;
     MHQHPRSSVP SPAPNFPPRP TARDDRREQE AAPSSPTVDM GSNSARGLGI EPGPQPSEQG
     RNAALGREAL TRLNQIISNY HTKAALIILH SRVALPPSFN KGSESPRVNR WFNVELDDTD
     VLREPLRPWR TCDATDNRPP PLVIETYLDT KGLTNNQSLV ILDENGKRWD VRESLAALQG
     ARAKPYQSEN DEIILERWRI ELGESSSRLP ADLGSILPTV YKKSIVLFRS LFTYSKFLPA
     WRFSKRNKKL RQSPALQIKY RVVDGSVARD DLSLDHLTAP LSEGSEKVVD TYSFGVTESP
     AGPFSVQVTY RTNCDFRVDD SEALLSSRFM GADDEIFRPS LPSDDVNRPN PEIGSVPVER
     KAVENPDCTR AYGSLSTFHQ VGPTTGASPI STLRAMRDSG AGSPSPTDSP KRLLPPAKVV
     PSGRAGQIAG EGGSSNFQRR PSVSFQPFKA PPLSASPALA DSPLGMSPRN MSSRIPTGTS
     ADSRVMPPPS SAASARRPTT IASEQAISSS NSASPKPAPI SRYSSSFSHR RGRLSAGANR
     LEDDNSSGRA SATSSNAQPG SGLLTEATGT SAESIQADDE NISEFLKMLD SKKDLMNSST
     SASIQPGPST TAAALARFRG MRDSNAALSD SMSQSMHMHR SSISSSKQLS GVPPMVAGTS
     ISTASSPGKP MSPHTPHTPH TPAIRSRLSS NSVADDIETD HHSRLPRIHH DPPLEEHSSA
     ENTRAPSSTA GAIDIPTSPR IFNPAYRRSS SAAVRRPIVT SDDDEIFPFG IRSLSLGADE
     SANATLGATQ QQNESQKDQQ SPAEDRSGPS VSTTGPYRDS ASLRGQMSGP TSASASSNPH
     VYQPRFASSR GRGYSGGHSL SSASSSLARG ANLTPHLAER DQDRDGNASG SNSGNSTLEI
     RRGSGQRPST GRTLSGQAPE DDEPLLFAMS DFGASRRSLD EGRHGNHGGT ESAAGSRRGS
     GRRGAGLPGF HVWS