ID   ATG8_GIBZE              Reviewed;         118 AA.
AC   I1S1W5;
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 8 {ECO:0000303|PubMed:28894236};
DE   AltName: Full=Autophagy-related ubiquitin-like modifier ATG8 {ECO:0000250|UniProtKB:P38182};
DE   Flags: Precursor;
GN   Name=ATG8 {ECO:0000303|PubMed:28894236};
GN   ORFNames=FG10740, FGRAMPH1_01T20343;
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: Ubiquitin-like modifier involved in cytoplasm to vacuole
CC       transport (Cvt) vesicles and autophagosomes formation (By similarity).
CC       With ATG4, mediates the delivery of the vesicles and autophagosomes to
CC       the vacuole via the microtubule cytoskeleton (By similarity). Required
CC       for selective autophagic degradation of the nucleus (nucleophagy) as
CC       well as for mitophagy which contributes to regulate mitochondrial
CC       quantity and quality by eliminating the mitochondria to a basal level
CC       to fulfill cellular energy requirements and preventing excess ROS
CC       production (By similarity). Participates also in membrane fusion events
CC       that take place in the early secretory pathway (By similarity). Also
CC       involved in endoplasmic reticulum-specific autophagic process and is
CC       essential for the survival of cells subjected to severe ER stress (By
CC       similarity). The ATG8-PE conjugate mediates tethering between adjacent
CC       membranes and stimulates membrane hemifusion, leading to expansion of
CC       the autophagosomal membrane during autophagy (By similarity). Moreover
CC       not only conjugation, but also subsequent ATG8-PE deconjugation is an
CC       important step required to facilitate multiple events during
CC       macroautophagy, and especially for efficient autophagosome biogenesis,
CC       the assembly of ATG9-containing tubulovesicular clusters into
CC       phagophores/autophagosomes, and for the disassembly of PAS-associated
CC       ATG components (By similarity). Autophagy is required for proper
CC       vegetative 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:P38182,
CC       ECO:0000269|PubMed:28894236}.
CC   -!- SUBUNIT: Conjugation to phosphatidylethanolamine (PE) leads to
CC       homodimerization (By similarity). Interacts with ATG1, ATG3, ATG4, ATG7
CC       and ATG12 (By similarity). {ECO:0000250|UniProtKB:P38182}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, cvt vesicle membrane
CC       {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Cytoplasmic vesicle, autophagosome
CC       membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Note=Membrane-associated through a
CC       lipid anchor (By similarity). This association needs the 2 ubiquitin-
CC       like systems required for cytoplasm to vacuole transport and autophagy
CC       (By similarity). Localizes to both the isolation membrane (IM) and the
CC       vacuole-isolation membrane contact site (VICS) during IM expansion (By
CC       similarity). The IM is a membrane sac generated from the pre-
CC       autophagosomal structure that ultimately expands to become a mature
CC       autophagosome (By similarity). {ECO:0000250|UniProtKB:P38182}.
CC   -!- PTM: The C-terminal Glu-117 and Ala-118 residues of ATG8 are removed by
CC       ATG4 to expose Gly-116 at the C-terminus (By similarity). This Gly-116
CC       forms then a thioester bond with the 'Cys-550' of ATG7 (E1-like
CC       activating enzyme) before being transferred to the 'Cys-244' of ATG3
CC       (the specific E2 conjugating enzyme), in order to be finally amidated
CC       with phosphatidylethanolamine (By similarity). This lipid modification
CC       anchors ATG8 to membranes and can be reversed by ATG4, releasing
CC       soluble ATG8 (By similarity). {ECO:0000250|UniProtKB:P38182}.
CC   -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC       colonies under nutrient-rich conditions (PubMed:28894236). Strongly
CC       reduces conidiation (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 ATG8 family. {ECO:0000305}.
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DR   EMBL; HG970334; CEF88089.1; -; Genomic_DNA.
DR   RefSeq; XP_011325668.1; XM_011327366.1.
DR   AlphaFoldDB; I1S1W5; -.
DR   SMR; I1S1W5; -.
DR   STRING; 5518.FGSG_10740P0; -.
DR   GeneID; 23557625; -.
DR   KEGG; fgr:FGSG_10740; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G20343; -.
DR   eggNOG; KOG1654; Eukaryota.
DR   HOGENOM; CLU_119276_0_1_1; -.
DR   InParanoid; I1S1W5; -.
DR   Proteomes; UP000070720; Chromosome 3.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033110; C:Cvt vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004241; Atg8-like.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10969; PTHR10969; 1.
DR   Pfam; PF02991; ATG8; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasmic vesicle; Lipoprotein; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway; Vacuole.
FT   CHAIN           1..118
FT                   /note="Autophagy-related protein 8"
FT                   /id="PRO_0000443885"
FT   PROPEP          117..118
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000443886"
FT   SITE            116..117
FT                   /note="Cleavage; by ATG4"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT   LIPID           116
FT                   /note="Phosphatidylethanolamine amidated glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
SQ   SEQUENCE   118 AA;  13720 MW;  8689307255E14793 CRC64;
     MRSKFKDEHP FEKRKAEAER IRQKYADRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF
     VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGEA