ID   ATG12_GIBZE             Reviewed;         160 AA.
AC   A0A0E0SC50;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Ubiquitin-like protein ATG12 {ECO:0000250|UniProtKB:P38316};
DE   AltName: Full=Autophagy-related protein 12 {ECO:0000303|PubMed:28894236};
GN   Name=ATG12 {ECO:0000303|PubMed:28894236}; ORFNames=FGRAMPH1_01T27403;
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 protein involved in cytoplasm to vacuole
CC       transport (Cvt), autophagy vesicles formation, mitophagy, and
CC       nucleophagy (By similarity). Conjugation with ATG5 through a ubiquitin-
CC       like conjugating system involving also ATG7 as an E1-like activating
CC       enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its
CC       function (By similarity). The ATG12-ATG5 conjugate acts as an E3-like
CC       enzyme which is required for lipidation of ATG8 and ATG8 association to
CC       the vesicle membranes (By similarity). ATG12-ATG5 rearranges the ATG3
CC       catalytic center and enhances its E2 activity (By similarity).
CC       Autophagy is required for proper vegetative growth, asexual/sexual
CC       reproduction, and full virulence (PubMed:28894236). Autophagy is
CC       particularly involved in the biosynthesis of deoxynivalenol (DON), an
CC       important virulence determinant (PubMed:28894236).
CC       {ECO:0000250|UniProtKB:P38316, ECO:0000269|PubMed:28894236}.
CC   -!- SUBUNIT: Forms a conjugate with ATG5 (By similarity). Forms a thioester
CC       bond with the 'Cys-196' of ATG10 (By similarity). Interacts with the
CC       ATG7 C-terminal 40 amino acids domain (By similarity). The ATG12-ATG5
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:P38316}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:P38316}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P38316}. 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).
CC       {ECO:0000250|UniProtKB:P38316}.
CC   -!- DISRUPTION PHENOTYPE: Does not significantly decrease the growth rate
CC       under nutrient-rich conditions (PubMed:28894236). Causes only mild
CC       infection in point-inoculated spikelets of flowering wheat heads and
CC       impairs the spreading to nearby spikelets (PubMed:28894236). Reduces
CC       strongly the production of deoxynivalenol (DON), an important virulence
CC       determinant (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC   -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
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DR   EMBL; HG970335; CEF84013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E0SC50; -.
DR   SMR; A0A0E0SC50; -.
DR   STRING; 5518.FGSG_13550P0; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G27403; -.
DR   eggNOG; KOG3439; Eukaryota.
DR   Proteomes; UP000070720; Chromosome 4.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007242; Atg12.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13385; PTHR13385; 1.
DR   Pfam; PF04110; APG12; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Autophagy; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..160
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000443904"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        160
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-102 in ATG5)"
FT                   /evidence="ECO:0000250|UniProtKB:P38316"
SQ   SEQUENCE   160 AA;  16880 MW;  DC709548E34B5D1E CRC64;
     MSETPKDQGP SSPSPSPSPS AASPMPLADN EVAGSGASSP NLPLTMSASV VLADLPRDAT
     AALEAAGSFK TDKIVVRFKP VGSAPLLAQD VCKISATRRF EEVVRYLRKK LRCKETDSVF
     LYVNSAFAPS LDEVVGNLHQ CFKNSHGQLV VAYSLTPAFG