VELB_BOTFB
ID VELB_BOTFB Reviewed; 451 AA.
AC L0PQJ9;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Velvet complex subunit 2 {ECO:0000305};
GN Name=VEL2 {ECO:0000303|PubMed:23118899};
GN Synonyms=velB {ECO:0000303|PubMed:23147398};
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.
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 (By similarity). The velvet complex acts
CC as a global regulator for secondary metabolite gene expression (By
CC similarity). Component of the VEL2-VOS1 heterodimeric complex that
CC plays a dual role in activating genes associated with spore maturation
CC and repressing certain development-associated genes (By similarity).
CC The VEL2-VOS1 complex binds DNA through the DNA-binding domain of VOS1
CC that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3'
CC consisting of two motifs in the promoters of key developmental
CC regulatory genes (By similarity). Controls the expression of the oxalic
CC acid and melanin gene clusters (PubMed:23118899, PubMed:23147398).
CC Involved in the resistance to oxidative stress (PubMed:23147398).
CC Required for full virulence (PubMed:23118899, PubMed:23147398).
CC {ECO:0000250|UniProtKB:C8VTS4, ECO:0000269|PubMed:23118899,
CC ECO:0000269|PubMed:23147398, 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). Forms a heterodimeric complex with VOS1; the
CC formation of the VEL2-VOS1 complex is light-dependent (By similarity).
CC {ECO:0000250|UniProtKB:C8VTS4, ECO:0000269|PubMed:25625818}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VTS4}. Cytoplasm
CC {ECO:0000250|UniProtKB:C8VTS4}. Note=Nuclear localization is mediated
CC by VEL1 (By similarity). {ECO:0000250|UniProtKB:C8VTS4}.
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. VelB subfamily.
CC {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; HE977591; CCK35906.1; -; Genomic_DNA.
DR AlphaFoldDB; L0PQJ9; -.
DR SMR; L0PQJ9; -.
DR VEuPathDB; FungiDB:Bcin01g02730; -.
DR OrthoDB; 1407766at2759; -.
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; -; 2.
DR InterPro; IPR021740; Velvet.
DR InterPro; IPR037525; Velvet_dom.
DR InterPro; IPR038491; Velvet_dom_sf.
DR PANTHER; PTHR33572; PTHR33572; 1.
DR Pfam; PF11754; Velvet; 1.
DR PROSITE; PS51821; VELVET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Sporulation; Transcription; Transcription regulation.
FT CHAIN 1..451
FT /note="Velvet complex subunit 2"
FT /id="PRO_0000435781"
FT DOMAIN 92..428
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48733 MW; D56A3549511BC1B3 CRC64;
MNTTAYASPP RDMHPRSTMP SLHDTTYRSG PPHQGAPYSM PQTMASQHST ISAYEQYNNS
LPVSRPPPPE HLPSSEAVSS FSIGLPGQEP SPRSITVDGR KYTLEVQQQP KRARMCGFGD
KDRRPITPPP CVKLSITEIA TGKEVDVNNI EHGMFVLNVD LWSADGERPV NLVRHSQTSP
SISATVPVSY TQIQGGAAAY SSLLPGQSQR EPTSPTYGSA PPFQGAGFSP FPGPPQVSAY
SQQQPGQQSG YGGNPNYPPP NGYQVAPQQS NYYYPQPSQS IPSHNNQDPY PSRPFTPQDL
GIGRIPISQT NPPQGMFTRN LIGSLSASAF RLTDPDDRIG IWFVLQDLSV RTEGDFRLRF
SFVNVGVPSA PQNNANSSCS VNTGKAPVLA SCFSEVFKVY SAKKFPGVVE STPLSKCFAT
QGIKIPIRKD GKDGPGKGGK DGSRGDDDDD Y
