ID BECN1_GIBZE Reviewed; 487 AA.
AC I1S4N7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Vacuolar protein sorting-associated protein 30 {ECO:0000250|UniProtKB:Q02948};
DE AltName: Full=Autophagy-related protein 6 {ECO:0000303|PubMed:28894236};
GN Name=VPS30 {ECO:0000303|PubMed:28894236};
GN Synonyms=ATG6 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG00679, FGRAMPH1_01T01709;
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), autophagy,
CC nucleophagy, and mitophagy, as a part of the autophagy-specific VPS34
CC PI3-kinase complex I (By similarity). This complex is essential to
CC recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5
CC conjugate to the pre-autophagosomal structure (By similarity). Also
CC involved in endosome-to-Golgi retrograde transport as part of the VPS34
CC PI3-kinase complex II (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:Q02948,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Component of the autophagy-specific VPS34 PI3-kinase complex
CC I; and of the VPS34 PI3-kinase complex II (By similarity).
CC {ECO:0000250|UniProtKB:Q02948}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q02948};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q02948}. Vacuole
CC membrane {ECO:0000250|UniProtKB:Q02948}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q02948}. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q02948}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q02948}. Note=With the VPS34 PI3-kinase complex
CC I, localizes to the vacuole-isolation membrane contact site (VICS)
CC during isolation membrane (IM) expansion (By similarity). The IM is a
CC membrane sac generated from the pre-autophagosomal structure that
CC ultimately expands to become a mature autophagosome (By similarity).
CC {ECO:0000250|UniProtKB:Q02948}.
CC -!- DOMAIN: The C-terminal domain called the BARA domain is dispensable for
CC the construction of both VPS34 PI3-kinase complexes, but is
CC specifically required for autophagy through the targeting of complex I
CC to the pre-autophagosomal structure (By similarity).
CC {ECO:0000250|UniProtKB:Q02948}.
CC -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236). Causes only
CC mild infection in point-inoculated spikelets of flowering wheat heads
CC and impairs the spreading to nearby spikelets (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
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DR EMBL; HG970332; CEF72655.1; -; Genomic_DNA.
DR RefSeq; XP_011316376.1; XM_011318074.1.
DR AlphaFoldDB; I1S4N7; -.
DR SMR; I1S4N7; -.
DR STRING; 229533.I1S4N7; -.
DR GeneID; 23558624; -.
DR KEGG; fgr:FGSG_11805; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G01709; -.
DR eggNOG; KOG2751; Eukaryota.
DR HOGENOM; CLU_024219_3_1_1; -.
DR InParanoid; I1S4N7; -.
DR OrthoDB; 11439at2759; -.
DR Proteomes; UP000070720; Chromosome 1.
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: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 Gene3D; 6.10.250.3110; -; 1.
DR Gene3D; 1.10.418.40; Autophagy protein 6/Beclin 1; 1.
DR InterPro; IPR007243; Atg6/Beclin.
DR InterPro; IPR038274; Atg6/Beclin_C_sf.
DR InterPro; IPR041691; Atg6/beclin_CC.
DR InterPro; IPR040455; Atg6_BARA.
DR PANTHER; PTHR12768; BECLIN 1; 1.
DR PANTHER; PTHR12768:SF4; BECLIN-1; 1.
DR Pfam; PF04111; APG6; 1.
DR Pfam; PF17675; APG6_N; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..487
FT /note="Vacuolar protein sorting-associated protein 30"
FT /id="PRO_0000443878"
FT REGION 33..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..480
FT /note="BARA"
FT /evidence="ECO:0000250|UniProtKB:Q02948"
FT REGION 456..481
FT /note="Required for membrane-association, autophagic
FT function during starvation and normal autophagosome
FT morphology"
FT /evidence="ECO:0000250|UniProtKB:Q02948"
FT COILED 152..282
FT /evidence="ECO:0000255"
FT COMPBIAS 33..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54386 MW; 9BD36792A3492264 CRC64;
MNCQKCRQPL RLDGSLEDLN PAAYDVLVAS ASPQTLKKSS VPNPPLAQPQ DQSRKSIYDR
VSRNAGPPTF KRNHGSHPRD SSMSFVLLSE SQMARPTPSS DPPTTPTVLR RASSSKSNAD
NPDAPMGSEM DRINRLFDVL SARSDVDHPI CVECTEMLVE GLQKKLEIAS RERDSYAKHL
KEAKANKPSE EDMKTQEEAL RKAERDRAAA MEELKKLESE KTSLDEELVL LEEESRQLDK
EEEKFWRERN DFATRMADFQ AERDSINAKY SNDSQLLEKL QRSNVYNDTF CISHDGSFAT
INGLRLGRLS NKPVDWPEIN AAWGHALLLL VTVADKLAYR FDGYDPQPMG STSRIIRYEV
PSPSSSRLGT RAASVPPKRH ILELYSSGDM PLGLTFMHRR FDNAMVGFLE LVRQLGAFVH
RQTEATGTPL SLPYKIDGDK IGDVSIKLGI AQDDGWTKAC KLTLTCCKFL LAHASNVTSN
ARNGGSQ
//
