ATG3_GIBZE
ID ATG3_GIBZE Reviewed; 349 AA.
AC I1RX50;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Autophagy-related protein 3 {ECO:0000303|PubMed:28894236};
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3 {ECO:0000303|PubMed:28894236};
GN Name=ATG3 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG08900, FGRAMPH1_01T11121;
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: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt) and autophagy (By similarity). Required for selective
CC autophagic degradation of the nucleus (nucleophagy) as well as for
CC mitophagy which contributes to regulate mitochondrial quantity and
CC quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production (By
CC similarity). Responsible for the E2-like covalent binding of
CC phosphatidylethanolamine to the C-terminal Gly of ATG8 (By similarity).
CC The ATG12-ATG5 conjugate plays a role of an E3 and promotes the
CC transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE) (By
CC similarity). This step is required for the membrane association of ATG8
CC (By similarity). The formation of the ATG8-phosphatidylethanolamine
CC conjugate is essential for autophagy and for the cytoplasm to vacuole
CC transport (Cvt) (By similarity). The ATG8-PE conjugate mediates
CC tethering between adjacent membranes and stimulates membrane
CC hemifusion, leading to expansion of the autophagosomal membrane during
CC autophagy (By similarity). Autophagy is required for proper vegetative
CC growth, asexual/sexual reproduction, and full virulence
CC (PubMed:28894236). Autophagy is particularly involved in the
CC biosynthesis of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). {ECO:0000250|UniProtKB:P40344,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with ATG8 through an
CC intermediate thioester bond between Cys-244 and the C-terminal Gly of
CC ATG8 (By similarity). Interacts with the C-terminal region of the E1-
CC like ATG7 enzyme (By similarity). Interacts also with the ATG12-ATG5
CC conjugate (By similarity). {ECO:0000250|UniProtKB:P40344}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC binding and is required for ATG8-PE conjugation (By similarity).
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The flexible region (FR) is required for ATG7-binding (By
CC similarity). {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The handle region (HR) contains the ATG8 interaction motif
CC (AIM) and mediates binding to ATG8 (By similarity). It is crucial for
CC the cytoplasm-to-vacuole targeting pathway (By similarity).
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236). Causes only
CC mild infection in point-inoculated spikelets of flowering wheat heads
CC and impairs the spreading to nearby spikelets (PubMed:28894236).
CC Reduces strongly the production of deoxynivalenol (DON), an important
CC virulence determinant (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; HG970333; CEF77363.1; -; Genomic_DNA.
DR RefSeq; XP_011319806.1; XM_011321504.1.
DR AlphaFoldDB; I1RX50; -.
DR SMR; I1RX50; -.
DR STRING; 5518.FGSG_08900P0; -.
DR GeneID; 23555878; -.
DR KEGG; fgr:FGSG_08900; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G11121; -.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_2_0_1; -.
DR InParanoid; I1RX50; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..349
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000443868"
FT REGION 95..173
FT /note="Flexible region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT REGION 248..325
FT /note="Handle region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT MOTIF 306..309
FT /note="ATG8 interaction motif (AIM)"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT ACT_SITE 244
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 349 AA; 39046 MW; 6363674868877586 CRC64;
MNFLYSTVNT LRDRYTPVSH KSTFRQTGQI TPEEFVAAGD YLVYKFPTWS WGDADSPERR
VSHLPPGKQF LVTRNVPCHR RLNDDFAGDA GHEEALVNDG DDFKGNAGDD EDGWLRTGGL
ASSQPLKVKE VRTVDDSGNV GDREVVEDDE IPDMEDEDDD EAIIRDSGAD SKNSAHRTYT
LYIMYSPYYR TPRLYLSGYL ANGQPLPPTD MTEDIVGDYK DKTVTLEDFP FFANNIKMAS
VHPCKHASVM KTLLDRADAA LRLRREKLRA GNASSSQAPS GMEGLVDEIG KLDVKGAQEA
ADKDEWEEVQ EAEIDDQEVA IRVDQYLVVF LKFMASVTPG IEHDFTMGV
