ATG14_GIBZE
ID ATG14_GIBZE Reviewed; 457 AA.
AC I1RAY1; A0A098D2G7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Autophagy-related protein 14 {ECO:0000303|PubMed:28894236};
GN Name=ATG14 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG00675, FGRAMPH1_01T01699;
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: Required for cytoplasm to vacuole transport (Cvt) and
CC autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex
CC I (By similarity). This complex is essential to recruit the ATG8-
CC phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-
CC autophagosomal structure (By similarity). ATG14 mediates the specific
CC binding of the VPS34 PI3-kinase complex I to the preautophagosomal
CC structure (PAS) (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:P38270,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Component of the autophagy-specific VPS34 PI3-kinase complex I
CC (By similarity). {ECO:0000250|UniProtKB:P38270}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P38270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P38270}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P38270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P38270}.
CC -!- DOMAIN: Coiled-Coils at the N-terminal half are essential for autophagy
CC (By similarity). {ECO:0000250|UniProtKB:P38270}.
CC -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236). Strongly
CC reduces conidiation (PubMed:28894236). Causes only mild infection in
CC point-inoculated spikelets of flowering wheat heads and impairs the
CC spreading to nearby spikelets (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG14 family. {ECO:0000305}.
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DR EMBL; HG970332; CEF72650.1; -; Genomic_DNA.
DR RefSeq; XP_011316371.1; XM_011318069.1.
DR AlphaFoldDB; I1RAY1; -.
DR SMR; I1RAY1; -.
DR STRING; 229533.I1RAY1; -.
DR GeneID; 23548156; -.
DR KEGG; fgr:FGSG_00675; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G01699; -.
DR eggNOG; ENOG502S2VB; Eukaryota.
DR HOGENOM; CLU_021590_1_0_1; -.
DR InParanoid; I1RAY1; -.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR Pfam; PF10186; ATG14; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Membrane; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..457
FT /note="Autophagy-related protein 14"
FT /id="PRO_0000443910"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..109
FT /evidence="ECO:0000255"
FT COMPBIAS 55..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 51224 MW; 64D35A08EEE41888 CRC64;
MDCDICHRSH DAKRLPFLCT VDARAALYDG RIENVMALIE NEDLQKQISD LLDETNAPTK
DRKDALQAQQ RTAEDRTTQI LAAADKLRND IKAAKEEIQT RRAALSRRKS DIAAVSDGLI
ERRVKRQKSV ERETGMHKYR WTKCADELAR TRSFLCIEAA QLYGLKRIKE GSPSKYEYYL
GGIPVVDLTA MNSSTPEMIS TSLSHICQIL ILVSHYLSIR LPAAITLPHR DYPRPTIFNL
SASYRPGDPV FPSQASVSSP SSTTDTESQR VSRPRPLFID KPLSQLAKED PATFSYFIEG
VTLLAYNIAW ACNTQGVSIG DKALFEDMSN MGRNLYNLLI NHQSAGKDPD TLKNEADGQT
SRFGQYSHGT TFYHLGGAEG TEFSKTFKLP SPMKLADKLK KKLLSEAPTP DWEVLDDDAW
KVEEELADGS QVNKNLLMGD KSSPRRGTSG WMRVKNR