VEA_GIBZE
ID VEA_GIBZE Reviewed; 399 AA.
AC I1S537; A0A098D3S4; A0A140TG13;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Developmental and secondary metabolism regulator ve1 {ECO:0000305};
DE AltName: Full=Velvet complex subunit 1 {ECO:0000305};
GN Name=ve1 {ECO:0000303|PubMed:22013911};
GN Synonyms=veA {ECO:0000303|PubMed:22140571};
GN ORFNames=FGRRES_11955, FGSG_11955;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22140571; DOI=10.1371/journal.pone.0028291;
RA Jiang J., Liu X., Yin Y., Ma Z.;
RT "Involvement of a velvet protein FgVeA in the regulation of asexual
RT development, lipid and secondary metabolisms and virulence in Fusarium
RT graminearum.";
RL PLoS ONE 6:E28291-E28291(2011).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=22713714; DOI=10.1016/j.fgb.2012.06.005;
RA Jiang J., Yun Y., Liu Y., Ma Z.;
RT "FgVELB is associated with vegetative differentiation, secondary metabolism
RT and virulence in Fusarium graminearum.";
RL Fungal Genet. Biol. 49:653-662(2012).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22013911; DOI=10.1111/j.1364-3703.2011.00755.x;
RA Merhej J., Urban M., Dufresne M., Hammond-Kosack K.E., Richard-Forget F.,
RA Barreau C.;
RT "The velvet gene, FgVe1, affects fungal development and positively
RT regulates trichothecene biosynthesis and pathogenicity in Fusarium
RT graminearum.";
RL Mol. Plant Pathol. 13:363-374(2012).
RN [7]
RP INTERACTION WITH LAEA AND VELB.
RX PubMed=23874628; DOI=10.1371/journal.pone.0068441;
RA Kim H.K., Lee S., Jo S.M., McCormick S.P., Butchko R.A., Proctor R.H.,
RA Yun S.H.;
RT "Functional roles of FgLaeA in controlling secondary metabolism, sexual
RT development, and virulence in Fusarium graminearum.";
RL PLoS ONE 8:E68441-E68441(2013).
CC -!- FUNCTION: Component of the velvet transcription factor complex that
CC controls sexual/asexual developmental ratio in response to light,
CC promoting sexual development in the darkness while stimulating asexual
CC sporulation under illumination (By similarity). The velvet complex hat
CC acts as a global regulator for secondary metabolite gene expression
CC (PubMed:22140571). Controls the expression of the aurofusarin and
CC trichothecene gene clusters (PubMed:22013911). Controls also the
CC expression of the deoxynivalenol (DON) gene cluster (PubMed:22140571).
CC Regulates hyphal growth and pigment formation (PubMed:22140571). Acts
CC as a positive regulator of virulence (PubMed:22013911,
CC PubMed:22140571). {ECO:0000250|UniProtKB:C8VTV4,
CC ECO:0000269|PubMed:22013911, ECO:0000269|PubMed:22140571}.
CC -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC laeA, ve1 and velB; Ve1 acting as a bridging protein between laeA and
CC velB (By similarity). Interacts directly with laeA and velB
CC (PubMed:23874628). {ECO:0000250|UniProtKB:C8VQG9,
CC ECO:0000269|PubMed:23874628}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VTV4}. Cytoplasm
CC {ECO:0000250|UniProtKB:C8VTV4}. Note=Enriched in the nucleus in the
CC dark (By similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC -!- DOMAIN: The C-terminal PEST domain is a region rich in proline,
CC glutamic acid, serine and threonine residues that is required for the
CC light-dependent regulation of development and secondary metabolism (By
CC similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC -!- DISRUPTION PHENOTYPE: Impairs aurofusarin and trichothecene
CC biosynthesis (PubMed:22013911). Reduces deoxynivalenol (DON)
CC biosynthesis (PubMed:22140571). Results in highly reduced sporulation
CC (PubMed:22013911). Reduces the hydrophobicity of the cell surface
CC (PubMed:22140571, PubMed:22013911). Shows increased resistance to
CC osmotic stress and cell wall-damaging agents, but increased sensitivity
CC to iprodione and fludioxonil fungicides (PubMed:22140571,
CC PubMed:22713714). {ECO:0000269|PubMed:22013911,
CC ECO:0000269|PubMed:22140571, ECO:0000269|PubMed:22713714}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; DS231663; ESU06761.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF73578.1; -; Genomic_DNA.
DR RefSeq; XP_011317246.1; XM_011318944.1.
DR AlphaFoldDB; I1S537; -.
DR SMR; I1S537; -.
DR EnsemblFungi; ESU06761; ESU06761; FGSG_11955.
DR GeneID; 23558774; -.
DR KEGG; fgr:FGSG_11955; -.
DR eggNOG; ENOG502S0HV; Eukaryota.
DR HOGENOM; CLU_022491_2_0_1; -.
DR InParanoid; I1S537; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.3960; -; 1.
DR InterPro; IPR021740; Velvet.
DR InterPro; IPR037525; Velvet_dom.
DR InterPro; IPR038491; Velvet_dom_sf.
DR PANTHER; PTHR33572; PTHR33572; 1.
DR Pfam; PF11754; Velvet; 2.
DR PROSITE; PS51821; VELVET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..399
FT /note="Developmental and secondary metabolism regulator
FT ve1"
FT /id="PRO_0000435769"
FT DOMAIN 26..220
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 219..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..330
FT /note="PEST"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..45
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:22013911"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 44644 MW; C31B21A0DAA48B40 CRC64;
MATPSAIPTN SKRDTTAQFH RVTRGNRSLW YQLTVLQQPE RARACGSGMK ANSDRRPVDP
PPVVELRIVE GPTLEEGKDV TFDYNANFFL YASLEHARPI ASCRVSTPTT NNPPILTGVP
ASGMAYLDRP SEAGYFIFPD LSVRHEGLYR LTFSLFETTK EEQDFDIQPA DGDLPPGVDF
RMEIKTDPFS VFSAKKFPGL MESTQLSKTV ADQGCRVRIR RDVRMRKRDT KSGGNNNNNN
NAGNNAGNNG FERREEDFGR RRTSTSTYVP PSPSVYSTEG HYRRDSQASY PPTPAAAPLP
RMNTEPSRGS IKISALVEPM PVIEPQVDPL PELPPVNVGG KRKHESVFAQ NTRPLFNGQR
QMDPHYGRSH RGYSPDHDQG SYSRADGQIS VIQFNKYEY
