ATG13_PHANO
ID ATG13_PHANO Reviewed; 929 AA.
AC Q0UPX4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13; ORFNames=SNOG_06190;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT86021.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445333; EAT86021.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001796572.1; XM_001796520.1.
DR AlphaFoldDB; Q0UPX4; -.
DR SMR; Q0UPX4; -.
DR STRING; 321614.Q0UPX4; -.
DR PRIDE; Q0UPX4; -.
DR GeneID; 5973451; -.
DR KEGG; pno:SNOG_06190; -.
DR eggNOG; KOG4573; Eukaryota.
DR InParanoid; Q0UPX4; -.
DR OMA; MHQHPRS; -.
DR OrthoDB; 1519629at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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..929
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000317948"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 100605 MW; 5E897C2CC9796F05 CRC64;
MNPYQRASPR TASPASNLQT NPTRTNNPRH SADRNSYFDN PPYNDRGSED GEDDMASRGD
HMAETDQRQY QKINQVIQNF FTKSALSIVS SRVILPTSFN KNGDIRQNKW FNVILDDSDE
LQLRLTEWKT MDAMAGQHPP LYIEVYLDIS GLGHKQSLVV HDEDGKRWDV AAALNAAQPT
SRASSRPARP TQIVIERWKI YVGDIDSVHP SDLTEPLPNV YKKAVVLFRG LYANLRLLPA
FKYNKSMAKQ PANHTSLKLN YRILNGASER PQLDTLSLPL CPSTDPITET AHIGSTNSPI
GPLCISVEYR DACEFSVEDS ESLLSDQFMG LDDTYLEQKP RAAAPVPGSL PVDKLNTQET
PDVGQAYGSL STFHQVGPPT GTSPISALRA ARDMPSSSPI ETPPQKLPPN HRTAQGSKSS
LRSNDTSSFQ RRTSVSFQPF KAGSLSSSPA PGPAGPASPS SSLGRPTSAF GRNINIVPNS
LNQPRNRTSL NALPQAALRA PSLPNDNAIA SSASSSPKPA PITRYSSSFG HRRGKFSTGG
SKTEEDALSS GKGSATSSLQ RGSDTLNDGE GGSSGEMRSE DDNISDFLKL LEAKKDLKSF
NRSDSSTRDA TMRKTTAQLG KYQRMRDSHA QLSDSVSSST MLHRSSSSSS RQLSSVPAMI
HGTSISTASS PGKPISPHTP HTPAIPSRLS ANSIIEYDQP HRSRNHRSRS RSGRTARGQG
PENLEEQSEV EDDAAGIDIP LSPRPWNYQR RSSSVAQQNR NLPEDEPDMF GVRAASLPVE
EGDRARDLHR ITSTDLTSSG LFAQTESLAS ASRDNQAPDD GDSRDDLPRA SSTSNTPAKR
GTYSSNLRGR GGFFSQGSST TGSTGGTSST ERQSRYNFNS RAANLDDDEP LLFQMSEIGA
GGSRRSLEEA RGGSSTGSAR GRNSPWGGR
