ATG29_GIBZE
ID ATG29_GIBZE Reviewed; 397 AA.
AC A0A098DPY0; A0A0E0SBS2; A0A1C3YM03;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Autophagy-related protein 29 {ECO:0000303|PubMed:28894236};
GN Name=ATG29 {ECO:0000303|PubMed:28894236}; ORFNames=FGRAMPH1_01T27149;
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: Plays a role in autophagy (By similarity). Functions at the
CC preautophagosomal structure (PAS) in order to form normal
CC autophagosomes under starvation conditions (By similarity). Also plays
CC a role in mitophagy (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:Q12092,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Forms a stable complex with ATG17 and ATG31 (By similarity).
CC Interacts directly with ATG31 (By similarity). The ATG17-ATG29-ATG31
CC complex interacts with the ATG1-ATG13 complex (By similarity). Note=The
CC interaction with the ATG1-ATG13 complex is induced by starvation (By
CC similarity). {ECO:0000250|UniProtKB:Q12092}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000250|UniProtKB:Q12092}. Note=Localizes also to other
CC perivacuolar punctate structures (By similarity).
CC {ECO:0000250|UniProtKB:Q12092}.
CC -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG29 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SCB65453.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HG970335; SCB65453.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A0A098DPY0; -.
DR SMR; A0A098DPY0; -.
DR eggNOG; ENOG502S3V4; Eukaryota.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.2570; -; 1.
DR InterPro; IPR039113; ATG29.
DR InterPro; IPR040666; Atg29_N.
DR InterPro; IPR039362; ATG29_sf.
DR PANTHER; PTHR40012; PTHR40012; 1.
DR Pfam; PF18388; ATG29_N; 1.
PE 3: Inferred from homology;
KW Autophagy; Protein transport; Reference proteome; Transport.
FT CHAIN 1..397
FT /note="Autophagy-related protein 29"
FT /id="PRO_0000443926"
FT REGION 71..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 42453 MW; 6873095C3829DE1F CRC64;
MPRGDFVDPP PVNWDLVKDE ALWKILSGAA ERQIDCKNAD RFEVSVDFLL QQVAWLTERH
ASQVRAQVRK ATAAVRNSGP SPVPSGEPAG SGHQRAHSAL SFRRDSPRNE AGSGTGTPLH
SSMRPLVARN TSTNTTVLRD MTGAPASPRP GVGLASRAGD RRRLSSLPIT SVPDKSLEQT
AQPELSPEER SPSPGPAEDS SPTSSDDESI PAQSRIIRRP PRYQPPDGGQ YEDDDDDESE
PAFQPYTSPS SKTSAQDLGS TLRGDKPVSG KRPHKSHGKP AIHKSNTSDS SASSAAIIQK
PDKTDRSTEQ RTPGPLSPHR PAELTGRSPG GKDKGYSREG SEGTPSMGSS YSDLDDASVT
QSALEEALAS HMNSRGAGSR FSISQAFRSR YTSSSNQ
