ID   ATG5_GIBZE              Reviewed;         254 AA.
AC   I1S039;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Autophagy-related protein 5 {ECO:0000303|PubMed:28894236};
GN   Name=ATG5 {ECO:0000303|PubMed:28894236};
GN   ORFNames=FG10053, FGRAMPH1_01T07167;
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: Involved in cytoplasm to vacuole transport (Cvt) and
CC       autophagic vesicle formation (By similarity). Autophagy is essential
CC       for maintenance of amino acid levels and protein synthesis under
CC       nitrogen starvation (By similarity). Required for selective autophagic
CC       degradation of the nucleus (nucleophagy) (By similarity). Also required
CC       for mitophagy, which eliminates defective or superfluous mitochondria
CC       in order to fulfill cellular energy requirements and prevent excess ROS
CC       production (By similarity). Conjugation with ATG12, through a
CC       ubiquitin-like conjugating system involving ATG7 as an E1-like
CC       activating enzyme and ATG10 as an E2-like conjugating enzyme, is
CC       essential for its function (By similarity). The ATG12-ATG5 conjugate
CC       acts as an E3-like enzyme which is required for lipidation of ATG8 and
CC       ATG8 association to the vesicle membranes (By similarity). ATG12-ATG5
CC       rearranges the ATG3 catalytic center and enhances its E2 activity (By
CC       similarity). Autophagy is required for proper vegetative growth,
CC       asexual/sexual reproduction, and full virulence (PubMed:28894236).
CC       Autophagy is particularly involved in the biosynthesis of
CC       deoxynivalenol (DON), an important virulence determinant
CC       (PubMed:28894236). {ECO:0000250|UniProtKB:Q12380,
CC       ECO:0000269|PubMed:28894236}.
CC   -!- SUBUNIT: Conjugated with ATG12 (By similarity). The ATG5-ATG12
CC       conjugate forms a complex with several units of ATG16 (By similarity).
CC       The ATG12-ATG5 conjugate associates also with ATG3 (By similarity).
CC       {ECO:0000250|UniProtKB:Q12380}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:Q12380}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q12380}. Note=Localizes to the isolation
CC       membrane (IM), a membrane sac which is generated from the pre-
CC       autophagosomal structure (PAS) (By similarity). Ultimately, the IM
CC       expands to become a mature autophagosome (By similarity). Localizes
CC       also to a dot at the junction between the IM and the vacuolar membrane,
CC       termed the vacuole-IM contact site (VICS) (By similarity). Correct
CC       localization to the PAS requires ATG21 (By similarity).
CC       {ECO:0000250|UniProtKB:Q12380}.
CC   -!- PTM: Conjugated to ATG12; which is essential for autophagy (By
CC       similarity). Conjugation with ATG12 involves ATG7 as an E1-like
CC       activating enzyme and ATG10 as an E2-like conjugating enzyme (By
CC       similarity). {ECO:0000250|UniProtKB:Q12380}.
CC   -!- DISRUPTION PHENOTYPE: Blocks autophagy (PubMed:28894236). Significantly
CC       decreases the radial growth of colonies under nutrient-rich conditions
CC       (PubMed:28894236). Strongly reduces conidiation and completely fails to
CC       form any perithecia (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC   -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR   EMBL; HG970332; CEF75388.1; -; Genomic_DNA.
DR   RefSeq; XP_011318981.1; XM_011320679.1.
DR   AlphaFoldDB; I1S039; -.
DR   SMR; I1S039; -.
DR   STRING; 5518.FGSG_10053P0; -.
DR   GeneID; 23556976; -.
DR   KEGG; fgr:FGSG_10053; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G07167; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   HOGENOM; CLU_051894_2_0_1; -.
DR   InParanoid; I1S039; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.246.190; -; 1.
DR   Gene3D; 3.10.20.620; -; 1.
DR   InterPro; IPR007239; Atg5.
DR   InterPro; IPR042526; Atg5_HR.
DR   InterPro; IPR042527; Atg5_UblA_dom.
DR   PANTHER; PTHR13040; PTHR13040; 1.
DR   Pfam; PF04106; APG5; 1.
PE   3: Inferred from homology;
KW   Autophagy; Isopeptide bond; Membrane; Reference proteome; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..254
FT                   /note="Autophagy-related protein 5"
FT                   /id="PRO_0000443875"
FT   CROSSLNK        102
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12380"
SQ   SEQUENCE   254 AA;  28023 MW;  6D2539EF3FF5AC9D CRC64;
     MSSPIPQALW SAQIPLHITH PASPTTPFIT SIPRFSYLAL LIPRLSTFFN SPCSSFHFED
     VQLRNLAVGL LVDLYQPALP WKLTVNDGVG WDIADTFLNC VKEADFVRNG NANQIMKMSK
     ENTTQLWNAV IDNDHPSFNR INSHLLNAPT ALKHVPIRIY VPTSGPDSSA THPEHATFKV
     IQSLMAATSS DRRPKLLGQA LKEVLPGLFP SSRDPILAKV VMHGAGVPFD APLEDLMREA
     AYPDGWLCLV VIVL