ATG20_GIBZE
ID ATG20_GIBZE Reviewed; 617 AA.
AC A0A098DRQ4; A0A0E0SDM7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Autophagy-related protein 20 {ECO:0000303|PubMed:28894236};
GN Name=ATG20 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG06950, FGRAMPH1_01T23585;
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), pexophagy
CC and mitophagy (By similarity). Also involved in endoplasmic reticulum-
CC specific autophagic process and is essential for the survival of cells
CC subjected to severe ER stress (By similarity). Functions in protein
CC retrieval from the endocytic pathway. Required for proper sorting of
CC the v-SNARE protein SNC1 (By similarity). Autophagy is required for
CC proper vegetative growth, asexual/sexual reproduction, and full
CC virulence (PubMed:28894236). Autophagy is particularly involved in the
CC biosynthesis of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). {ECO:0000250|UniProtKB:Q07528,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Forms a complex with SNX4/ATG24 and ATG17 (By similarity).
CC {ECO:0000250|UniProtKB:Q07528}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q07528};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q07528}.
CC Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q07528};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q07528}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization of ATG20 to the
CC perivacuolar punctate structures (By similarity).
CC {ECO:0000250|UniProtKB:Q07528}.
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). Reduces strongly the
CC production of deoxynivalenol (DON), an important virulence determinant
CC (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; HG970335; CEF84540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098DRQ4; -.
DR STRING; 5518.FGSG_06950P0; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G23585; -.
DR eggNOG; KOG2273; Eukaryota.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; -; 2.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR044106; PX_Snx41/Atg20.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..617
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000443920"
FT DOMAIN 89..209
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 403..440
FT /evidence="ECO:0000255"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
SQ SEQUENCE 617 AA; 69125 MW; 5362A94C5D36CA63 CRC64;
MWNDEDNNPY GTSFDRRDSQ SSSINPTSPS TREYQRFEPP QTPTSDSDNE HNHGVIHDDS
DDDDEDLTQD AGPKRKPGGY DSRIEQILYE NPKLSILITD AGKSIESGGR YIVYTIKTGD
LEVRRRYSEF ASLRDALTRL HPTLIVPPIP EKHTMADYAA NPTNAKQDQQ IIDLRKRMLA
VFLNRCRRME EIRTDGVWWR FFDPNASWSE VLHSHPVASI PKSILKAPPL NPANPTPAHN
YLPIPAASAK LKTVAGTNHD NSSGHIQAGP HAFGRFPPEG HNLGEQELDP YFISYESSIK
DLEQLLTGPM EKVNRRTLSH LSSLAADLCE LGSVYNAFAV SEQAPSLGPA IERIGQAADL
SYIATEELSG SLGASFAEPM REHAQFAGVV RSVLKYRVLK RVQQDLTTEE LSKKRALLDQ
LEQSEAEARR IENYLSSSQQ ISPPPKRSTS LREPPSHQRR DGSQEDTESI DSDFPGTHGD
FSSHTPSASQ GLPERSTSVP SHKKMPSGNS ITNKIFGPIR HAVQGVVDVD PERTRRDLIG
KTRESIGQLE QAQVVSEKDV KEASASVLKD MKRFQKDKED DLRRYMLAYA QSQIEWAKKS
KQQWEEARAE VEKIDES
