VELB_EMENI
ID VELB_EMENI Reviewed; 369 AA.
AC C8VTS4; A5HMG5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Velvet complex subunit B {ECO:0000305};
GN Name=velB {ECO:0000303|PubMed:18556559}; ORFNames=ANIA_00363;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ni M., Yu J.-H.;
RT "A novel regulator couples sporogenesis and trehalose biogenesis in
RT Aspergillus nidulans.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE VELVET COMPLEX,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18556559; DOI=10.1126/science.1155888;
RA Bayram O., Krappmann S., Ni M., Bok J.W., Helmstaedt K., Valerius O.,
RA Braus-Stromeyer S., Kwon N.J., Keller N.P., Yu J.H., Braus G.H.;
RT "VelB/VeA/LaeA complex coordinates light signal with fungal development and
RT secondary metabolism.";
RL Science 320:1504-1506(2008).
RN [5]
RP INTERACTION WITH VOSA, AND FUNCTION.
RX PubMed=21152013; DOI=10.1371/journal.pgen.1001226;
RA Sarikaya Bayram O., Bayram O., Valerius O., Park H.S., Irniger S.,
RA Gerke J., Ni M., Han K.H., Yu J.H., Braus G.H.;
RT "LaeA control of velvet family regulatory proteins for light-dependent
RT development and fungal cell-type specificity.";
RL PLoS Genet. 6:E1001226-E1001226(2010).
RN [6]
RP IDENTIFICATION IN THE VELVET COMPLEX.
RX PubMed=23065618; DOI=10.1007/978-1-62703-122-6_14;
RA Bayram O., Bayram O.S., Valerius O., Joehnk B., Braus G.H.;
RT "Identification of protein complexes from filamentous fungi with tandem
RT affinity purification.";
RL Methods Mol. Biol. 944:191-205(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND INTERACTION WITH VOSA.
RX PubMed=23049895; DOI=10.1371/journal.pone.0045935;
RA Park H.S., Ni M., Jeong K.C., Kim Y.H., Yu J.H.;
RT "The role, interaction and regulation of the velvet regulator VelB in
RT Aspergillus nidulans.";
RL PLoS ONE 7:E45935-E45935(2012).
RN [8]
RP INTERACTION WITH VEA.
RX PubMed=23341778; DOI=10.1371/journal.pgen.1003193;
RA Palmer J.M., Theisen J.M., Duran R.M., Grayburn W.S., Calvo A.M.,
RA Keller N.P.;
RT "Secondary metabolism and development is mediated by LlmF control of VeA
RT subcellular localization in Aspergillus nidulans.";
RL PLoS Genet. 9:E1003193-E1003193(2013).
RN [9]
RP INTERACTION WITH VEA.
RX PubMed=26564476; DOI=10.1111/mmi.13275;
RA Rauscher S., Pacher S., Hedtke M., Kniemeyer O., Fischer R.;
RT "A phosphorylation code of the Aspergillus nidulans global regulator
RT VelvetA (VeA) determines specific functions.";
RL Mol. Microbiol. 99:909-924(2016).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25960370; DOI=10.1038/srep10199;
RA Park H.S., Yu Y.M., Lee M.K., Maeng P.J., Kim S.C., Yu J.H.;
RT "Velvet-mediated repression of beta-glucan synthesis in Aspergillus
RT nidulans spores.";
RL Sci. Rep. 5:10199-10199(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH VOSA, FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24391470; DOI=10.1371/journal.pbio.1001750;
RA Ahmed Y.L., Gerke J., Park H.S., Bayram O., Neumann P., Ni M.,
RA Dickmanns A., Kim S.C., Yu J.H., Braus G.H., Ficner R.;
RT "The velvet family of fungal regulators contains a DNA-binding domain
RT structurally similar to NF-kappaB.";
RL PLoS Biol. 11:E1001750-E1001750(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 (PubMed:18556559, PubMed:23049895). The
CC velvet complex acts as a global regulator for secondary metabolite gene
CC expression (PubMed:18556559). Component of the velB-VosA heterodimeric
CC complex that plays a dual role in activating genes associated with
CC spore maturation and repressing certain development-associated genes
CC (PubMed:21152013, PubMed:24391470). The velB-VosA complex binds DNA
CC through the DNA-binding domain of vosA that recognizes an 11-nucleotide
CC consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the
CC promoters of key developmental regulatory genes (PubMed:24391470). The
CC vosA-velB complex binds to the beta-glucan synthase fksA gene promoter
CC in asexual spores for repression (PubMed:25960370).
CC {ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:21152013,
CC ECO:0000269|PubMed:23049895, ECO:0000269|PubMed:24391470,
CC ECO:0000269|PubMed:25960370}.
CC -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC laeA, veA and velB; VeA acting as a bridging protein between laeA and
CC velB (PubMed:18556559, PubMed:23065618). Interacts directly with veA
CC (PubMed:23341778, PubMed:26564476). Forms a heterodimeric complex with
CC vosA; the formation of the velB-vosA complex is light-dependent
CC (PubMed:21152013, PubMed:23049895, PubMed:24391470).
CC {ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:21152013,
CC ECO:0000269|PubMed:23049895, ECO:0000269|PubMed:23065618,
CC ECO:0000269|PubMed:23341778, ECO:0000269|PubMed:24391470,
CC ECO:0000269|PubMed:26564476}.
CC -!- INTERACTION:
CC C8VTS4; Q5BBX1: vosA; NbExp=5; IntAct=EBI-16088850, EBI-16088812;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18556559}. Cytoplasm
CC {ECO:0000269|PubMed:18556559}. Note=VeA increases the nuclear
CC localization of VelB. {ECO:0000269|PubMed:18556559}.
CC -!- INDUCTION: Expression is positively regulated by abaA
CC (PubMed:23049895). {ECO:0000269|PubMed:23049895}.
CC -!- DISRUPTION PHENOTYPE: Reduces the number of conidia, and decreased and
CC delayed mRNA accumulation of the key asexual regulatory genes brlA,
CC abaA and vosA during asexual spore formation (PubMed:23049895). Down-
CC regulates genes associated with spore maturation and up-regulates
CC certain development-associated genes (PubMed:24391470). Results in
CC elevated accumulation of beta-glucan in asexual spores
CC (PubMed:25960370). {ECO:0000269|PubMed:23049895,
CC ECO:0000269|PubMed:24391470, ECO:0000269|PubMed:25960370}.
CC -!- SIMILARITY: Belongs to the velvet family. VelB subfamily.
CC {ECO:0000305}.
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DR EMBL; EF540815; ABQ17967.1; -; mRNA.
DR EMBL; BN001308; CBF89638.1; -; Genomic_DNA.
DR PDB; 4N6R; X-ray; 2.20 A; B=1-369.
DR PDBsum; 4N6R; -.
DR AlphaFoldDB; C8VTS4; -.
DR SMR; C8VTS4; -.
DR DIP; DIP-60680N; -.
DR IntAct; C8VTS4; 1.
DR STRING; 162425.CADANIAP00002340; -.
DR EnsemblFungi; CBF89638; CBF89638; ANIA_00363.
DR VEuPathDB; FungiDB:AN0363; -.
DR eggNOG; ENOG502S1B4; Eukaryota.
DR HOGENOM; CLU_022491_0_0_1; -.
DR InParanoid; C8VTS4; -.
DR OMA; KIGVWFI; -.
DR OrthoDB; 1407766at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:AspGD.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0075308; P:negative regulation of conidium formation; IMP:AspGD.
DR GO; GO:0043941; P:positive regulation of sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0010914; P:positive regulation of sterigmatocystin biosynthetic process; IMP:AspGD.
DR GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:AspGD.
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 3D-structure; Cytoplasm; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..369
FT /note="Velvet complex subunit B"
FT /id="PRO_0000435778"
FT DOMAIN 53..345
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:4N6R"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4N6R"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 271..281
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:4N6R"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:4N6R"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:4N6R"
SQ SEQUENCE 369 AA; 40040 MW; 46D2F22E50F30ACB CRC64;
MYAVEDRAHS GHHPPPLSMD RIPPPSTMYP SSAGPSAMVS PAGQPEPESL STVHDGRIWS
LQVVQQPIRA RMCGFGDKDR RPITPPPCIR LIVKDAQTQK EVDINSLDSS FYVVMADLWN
ADGTHEVNLV KHSATSPSIS TAMSSSYPPP PHPTSSDYPA SYQTNPYGQP VGQPVGQPVG
YAGVGNYYGG STQLQYQNAY PNPQAQYYQP MYGGMAQPQM PAAQPVTPGP GGMFTRNLIG
CLSASAYRLY DTEDKIGVWF VLQDLSVRTE GIFRLKFSFV NVGKSVSDLP QSDIAEVINK
GTAPILASTF SEPFQVFSAK KFPGVIESTP LSKVFANQGI KIPIRKDGVK GQGSRGRHSD
EDDGLDNEY
