ID   ATG11_GIBZE             Reviewed;        1429 AA.
AC   A0A098D065; A0A0E0RM29; A0A1C3YI63;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Autophagy-related protein 11 {ECO:0000303|PubMed:28894236};
GN   Name=ATG11 {ECO:0000303|PubMed:28894236};
GN   ORFNames=FG00382, FGRAMPH1_01T01003;
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), pexophagy,
CC       mitophagy and nucleophagy (By similarity). Recruits mitochondria for
CC       their selective degradation via autophagy (mitophagy) during
CC       starvation, through its interaction with ATG32 (By similarity). Works
CC       as scaffold proteins that recruit ATG proteins to the pre-autophagosome
CC       (PAS), the site of vesicle/autophagosome formation (By similarity).
CC       Required for ATG9 anterograde transport from the mitochondria to the
CC       PAS (By similarity). Recruits also the ATG19-prAPE1 complex to the PAS
CC       (By similarity). Required for the Cvt vesicles completion (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:Q12527,
CC       ECO:0000269|PubMed:28894236}.
CC   -!- SUBUNIT: Homodimer and potential homooligomers (By similarity).
CC       Interacts with ATG1 kinase and the ATG19 and ATG34 cargo protein
CC       transporters (By similarity). Interacts with ATG9, ATG17 and ATG20 (By
CC       similarity). {ECO:0000250|UniProtKB:Q12527}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:Q12527}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q12527}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:Q12527}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q12527}. Note=During pexophagy, accumulates in
CC       the vacuolar membrane region, where the peroxisomes contact the vacuole
CC       (By similarity). {ECO:0000250|UniProtKB:Q12527}.
CC   -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC       colonies under nutrient-rich conditions (PubMed:28894236). Strongly
CC       reduces conidiation (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC   -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SCB64046.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; HG970332; SCB64046.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0A098D065; -.
DR   SMR; A0A098D065; -.
DR   STRING; 5518.FGSG_00382P0; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR040040; ATG11.
DR   InterPro; IPR019460; Atg11_C.
DR   InterPro; IPR045326; ATG17-like_dom.
DR   PANTHER; PTHR13222; PTHR13222; 1.
DR   Pfam; PF10377; ATG11; 1.
DR   Pfam; PF04108; ATG17_like; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..1429
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000443901"
FT   REGION          574..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1205..1224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1333..1405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          540..579
FT                   /evidence="ECO:0000255"
FT   COILED          616..808
FT                   /evidence="ECO:0000255"
FT   COILED          842..985
FT                   /evidence="ECO:0000255"
FT   COILED          1106..1135
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        577..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1333..1384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1389..1403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1429 AA;  162227 MW;  B43E6FC9CF2E1734 CRC64;
     MALQVLIAHT GLRLEVDTAQ FSILDDLKTW VSKKTSIPPQ HIVALNPHGR TVKITNLHTE
     KEIFVYDIRI SSPGNTNLIT PIPLPKRYAV PNAPNTIDDV QSITSWQELY KDRRNWAMRL
     VEDSGQMSSA TLARYSEIDV IIKCLDAAVA NLEISIKQIE PKYNDLKKWV APALEEHGNL
     VERWEQYLDL AKSTPVSPSM VKFMTGREIN KARPTLEDLI ELDTAKKAGK LAPTAHRRFS
     DKANQLGNTA SQMYQSLESL IANFETLMSR SALSHSTDSA QLLEDIEAVV KQMDSDYRAA
     LGYGNTQRDV AQASKTASVH TEHLVPTLKK RVKEMEELLH YGTDARNSVA SESAKFMRHV
     TEITSLHSNV KSQINVLNQS EDDMTTFDYL RLIHQLPYMY AAFVAEAVRR REWVDKVKTD
     SSTLANEMAL FQDEESKRRR KWQKMIGSMY GPDLDTNVMG LEVNLLGEDT PWPALTKEDL
     TDFIQILQEQ PVDQTVLDDI VKLVQELDSP TKQQSKRLKA FKNGSIHEAA LGRSGLMIRG
     DDDLLQSLQE DKGKLENKLK TAESRVRRLE DLLHRQSQAS RPGNLFQPQG SQQRERVNSA
     SSVRSSRFDD RRRSSEGIDP LMRRITQLEN ELREEKQRSV NLQQELTTQS NNHEDVKGQH
     EDLKAQHEDL KGQMAEINTT KQDLLENMEA LEREFVEERK NLEIEIKTLK ARLEDTEDEI
     EQFDESRQHE KAGLVVRVEE LEAELEQVNK QRQDDALKAQ GQVEFLRKET RIQREQQEAL
     EQQIQSAQEE VQNVSRKLSV AEEALDDHWQ ALTRLFSELS PDGTIPDNVV DLSNLLLTQA
     GTLVEKSRNS EADIELLKTQ VEHFSSAISE LREQVSQKDA KLSEDEMTVI HLRENIAEEQ
     AKVSALEQEL ADGREQLTEL RAKLSDGETG PEALQTRLED EEKKVMTLTE EVASKQSHVG
     SLEEELRMFQ EKVESLQGKI SHMNSHYEHR DEKTKDLTQR LYSQNDRMCR LLERVGYAVT
     RKDGEMTVNK IPRAERNAQN LADSTDPSAS IRKSGTLSRV LGDSVDLELL YWFNNSDMQA
     EDEKYEEFMN NLGKFDMELF SETVYRRIKE VEHMARKWQK EARSYRERAH ILQKDSHEKI
     AFKHFREGDL ALFLPTRNQQ AGAWAAFNVG FPHYFLREQD AHRLRHREWL VARISRIQER
     VVDLSKSLQP SSETESINDE ENDNPFQLSD GLHWYLIDAL EDKPGAPSTP GMGKSTVAAN
     TVEATANIHA HGVGGKGKSR ESVTSIEGIN KTLSKSLESR RSSTNSKKAL PFQLGGTTLL
     KNSALASETN SLRAHNADTP SGTSPTQGGH LTSTNASLGQ KNQRVDGPIR QPSDESSTQG
     GGAKADEQPR SVVQREDSVE SPTRRSVVWD SLWSVDYNYE SGSRRWLGG