VEA_BOTFB
ID VEA_BOTFB Reviewed; 575 AA.
AC L0PQS5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Developmental and secondary metabolism regulator VEL1 {ECO:0000305};
DE AltName: Full=Velvet complex subunit 1 {ECO:0000305};
GN Name=VEL1 {ECO:0000303|PubMed:23118899};
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=B05.10;
RX PubMed=23118899; DOI=10.1371/journal.pone.0047840;
RA Schumacher J., Pradier J.M., Simon A., Traeger S., Moraga J., Collado I.G.,
RA Viaud M., Tudzynski B.;
RT "Natural variation in the VELVET gene bcvel1 affects virulence and light-
RT dependent differentiation in Botrytis cinerea.";
RL PLoS ONE 7:E47840-E47840(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23147398; DOI=10.1016/j.fgb.2012.10.003;
RA Yang Q., Chen Y., Ma Z.;
RT "Involvement of BcVeA and BcVelB in regulating conidiation, pigmentation
RT and virulence in Botrytis cinerea.";
RL Fungal Genet. Biol. 50:63-71(2013).
RN [3]
RP IDENTIFICATION IN THE VELVET COMPLEX, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25625818; DOI=10.1094/mpmi-12-14-0411-r;
RA Schumacher J., Simon A., Cohrs K.C., Traeger S., Porquier A., Dalmais B.,
RA Viaud M., Tudzynski B.;
RT "The VELVET complex in the gray mold fungus Botrytis cinerea: impact of
RT BcLAE1 on differentiation, secondary metabolism, and virulence.";
RL Mol. Plant Microbe Interact. 28:659-674(2015).
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 (PubMed:23118899). The velvet complex
CC hat acts as a global regulator for secondary metabolite gene expression
CC (By similarity). Controls the expression of the oxalic acid and melanin
CC gene clusters (PubMed:23118899, PubMed:23147398). Controls also the
CC expression of proteases and carbohydrate-active enzymes
CC (PubMed:25625818). Involved in the resistance to oxidative stress
CC (PubMed:23147398). Required for full virulence (PubMed:23118899,
CC PubMed:23147398). {ECO:0000250|UniProtKB:C8VTV4,
CC ECO:0000269|PubMed:23118899, ECO:0000269|PubMed:23147398,
CC ECO:0000269|PubMed:25625818}.
CC -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC LAE1, VEL1 and VEL2; VEL1 acting as a bridging protein between LAE1 and
CC VEL2 (PubMed:25625818). {ECO:0000269|PubMed:25625818}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23118899}. 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: Leads to light-independent conidiation, loss of
CC sclerotial development and oxalic acid production, and reduced
CC virulence on several host plants (PubMed:23118899, PubMed:25625818).
CC Increases conidiation and melanin biosynthesis (PubMed:23147398).
CC {ECO:0000269|PubMed:23118899, ECO:0000269|PubMed:23147398}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE977589; CCK35904.1; -; Genomic_DNA.
DR AlphaFoldDB; L0PQS5; -.
DR SMR; L0PQS5; -.
DR VEuPathDB; FungiDB:Bcin15g03390; -.
DR OrthoDB; 1171722at2759; -.
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; Sporulation; Transcription; Transcription regulation.
FT CHAIN 1..575
FT /note="Developmental and secondary metabolism regulator
FT VEL1"
FT /id="PRO_0000435775"
FT DOMAIN 21..225
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..509
FT /note="PEST"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT REGION 513..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..40
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT COMPBIAS 231..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63594 MW; EEEE33E3B33486C3 CRC64;
MAASIGPKSI PETITRQTKG GRKLKYTLTV IQQPERARAC GSGAKSSADR RPVDPPPVVQ
LRIYDETDPR QEKEITFHYN ANFFLFATLE VARNIAQGRV QTSAPQAPVL TGMPVSGMAY
LDRPNEAGYF IFPDLSVRHE GQYKLSFNLY EETKEEKDTD IEPSNDSSMR QMSSAAAAAE
SSFDWRMELK SDQFTVYSAK KFPGLSESTD LSRTVAEQGC RVRIRRDVRM RRRDTKPGGD
FGEKEDEYQQ GRATSPPFDY NIQAARQRAL SASVHEDPQQ RRGSGEISPY HSPVVNTPFR
TPSISPSTPN APLPPGNQLG WIPNGPGYAA APSIQPPHPP PPPPSSYPQS MPATHHNQGP
STQFRQQPPQ GPPPAPIGYD ERRSSYSQFR PPTNPSQQQS YESDYRRMSF GYQIPASSQG
PQPIAPAVQN PAYNQQSMEP TYSRNPPAYS TSFQDSVALA PLRAAEQPLA MSPLASVTSI
SRGTQNSAPM PSHNYNKLER SGSYSQYAPI EAEAPKSTNK RSFNDVFSTP TESLSNGRRP
SAIGIDIEEN TRKQEQMIYR RANGNIQNKP APGLN