ATG13_GIBZE
ID ATG13_GIBZE Reviewed; 927 AA.
AC I1RW37;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Autophagy-related protein 13 {ECO:0000303|PubMed:28894236};
GN Name=ATG13 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG08491, FGRAMPH1_01T10093;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28894236; DOI=10.1038/s41598-017-11640-z;
RA Lv W., Wang C., Yang N., Que Y., Talbot N.J., Wang Z.;
RT "Genome-wide functional analysis reveals that autophagy is necessary for
RT growth, sporulation, deoxynivalenol production and virulence in Fusarium
RT graminearum.";
RL Sci. Rep. 7:11062-11062(2017).
CC -!- FUNCTION: Activates the ATG1 kinase in a nutritional condition
CC dependent manner through the TOR pathway, leading to autophagy (By
CC similarity). Involved in ATG9 and ATG23 cycling through the pre-
CC autophagosomal structure (By similarity). Also involved in cytoplasm to
CC vacuole transport (Cvt) and more specifically in Cvt vesicle formation
CC (By similarity). Seems to play a role in the switching machinery
CC regulating the conversion between the Cvt pathway and autophagy (By
CC similarity). Finally, ATG13 is also required for glycogen storage
CC during stationary phase (By similarity). Autophagy is required for
CC proper vegetative growth, asexual/sexual reproduction, and full
CC virulence (PubMed:28894236). Autophagy is particularly involved in the
CC biosynthesis of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). {ECO:0000250|UniProtKB:Q06628,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Hypophosphorylated form interacts with ATG1 to form the ATG1-
CC ATG13 kinase complex (By similarity). The ATG1-ATG13 complex interacts
CC with the ATG17-ATG29-ATG31 complex through direct interaction with
CC ATG17 (By similarity). {ECO:0000250|UniProtKB:Q06628}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC -!- DISRUPTION PHENOTYPE: Does not significantly decrease the growth rate
CC under nutrient-rich conditions (PubMed:28894236). Strongly reduces
CC conidiation (PubMed:28894236). Causes only mild infection in point-
CC inoculated spikelets of flowering wheat heads and impairs the spreading
CC to nearby spikelets (PubMed:28894236). Reduces also strongly the
CC production of deoxynivalenol (DON), an important virulence determinant
CC (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC {ECO:0000305}.
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DR EMBL; HG970333; CEF76849.1; -; Genomic_DNA.
DR RefSeq; XP_011320271.1; XM_011321969.1.
DR AlphaFoldDB; I1RW37; -.
DR SMR; I1RW37; -.
DR STRING; 5518.FGSG_08491P0; -.
DR GeneID; 23555493; -.
DR KEGG; fgr:FGSG_08491; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G10093; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_007151_1_0_1; -.
DR InParanoid; I1RW37; -.
DR Proteomes; UP000070720; Chromosome 2.
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..927
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000443907"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 99944 MW; DA5B7A1378DF479D CRC64;
MHQQPRGPAR VSSPGATTQP NLPSRSNSTR EAALGSRPRA GSNLVGRDVP NSPSLESPPI
PAPPADSVRK LDQIIQNFYA KAAVLVLDSR IKSRPARGAN GARKPNKWFQ IETDEIDDFR
DELKIWKNCG SLDNRPPPMV IEVYLDASRL KDSQSLVIVD ENGKRWDVME QLNSYGSSTD
SSGASRRNNE VVIERWQVEL KHSGMTSVDF GPILPTVYKK AIVFFRSLFI TTRLLPAWKF
ASQGAAKNSH PALIPRCRIR LSQPDRPRYD QLRLPIDGRP DPVTEYVFGD LEVPVGRLST
LVTYRSDCNF RVDDSEALLS SRFMGVDENF FRPSLPQQHA TSRAPAAEAG SLRDHRSKPN
LNDIQQAYGS LSTFHGNVPI GTSPISALRS VRQPGSDTSS PPESIPAQHD VGGPSSLPVR
QGTARPHLPA LEGLGRRPSV SFQPFKAGSL SGSPVPRQLD AEPASPQSLT RPGIPSLRQA
GNRTSLTAGM PASLRGGPPT SSGETAVAGS PRPASTSRYS SSFTHRRGRL SFGGASKAGD
DEQGSSGRQS LASSVAQPGS GLLAEVAGTS SESLRDDNEQ LEDFIKALDS KKTLQSFGPS
KTGESATNKT VAQLSRFHMM RDSNNALTES MTSSVQMQRS SSSSSRQLTS VPGMTAPASV
SASSSPGKPL SPHTPHTPAI PSRLSENSII DYSGQGRITS RQGRTSDNTQ PGTIRENTIT
QDGTTAIDIP LSPRLATYQR RASSVAIQNR SMADDDDTDS AFAHRSISLG ADDREPPTLS
ILLGRQMQLE EDSTQRPSDR LEPAADTGST ETPDMLRQGL SEENPPEGLI PAATSSSPFG
RRRYMGMASH KQTPPQSSRG SFNGSLNRQV RGDDDSVNEE PLVFDLSEMD PQGRRSIEEA
RSGASGGPNI GPDRGGYESR NASRRGW
