VEA_HYPJQ
ID VEA_HYPJQ Reviewed; 573 AA.
AC G0RL42;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 31.
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:23390613};
GN Synonyms=VeA {ECO:0000303|PubMed:23390613}; ORFNames=TRIREDRAFT_122284;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a;
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [2]
RP INDUCTION, AND INTERACTION WITH LAE1.
RC STRAIN=QM6a;
RX PubMed=23390613; DOI=10.1534/g3.112.005140;
RA Karimi-Aghcheh R., Bok J.W., Phatale P.A., Smith K.M., Baker S.E.,
RA Lichius A., Omann M., Zeilinger S., Seiboth B., Rhee C., Keller N.P.,
RA Freitag M., Kubicek C.P.;
RT "Functional analyses of Trichoderma reesei LAE1 reveal conserved and
RT contrasting roles of this regulator.";
RL G3 (Bethesda) 3:369-378(2013).
RN [3]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25386652; DOI=10.1371/journal.pone.0112799;
RA Karimi Aghcheh R., Nemeth Z., Atanasova L., Fekete E., Paholcsek M.,
RA Sandor E., Aquino B., Druzhinina I.S., Karaffa L., Kubicek C.P.;
RT "The VELVET A orthologue VEL1 of Trichoderma reesei regulates fungal
RT development and is essential for cellulase gene expression.";
RL PLoS ONE 9:E112799-E112799(2014).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26481618; DOI=10.1007/s00253-015-7059-2;
RA Liu K., Dong Y., Wang F., Jiang B., Wang M., Fang X.;
RT "Regulation of cellulase expression, sporulation, and morphogenesis by
RT velvet family proteins in Trichoderma reesei.";
RL Appl. Microbiol. Biotechnol. 100:769-779(2016).
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:25386652). The velvet complex
CC hat acts as a global regulator for secondary metabolite gene expression
CC (By similarity). Regulates expression of the carbohydrate-active enzyme
CC gene clusters (PubMed:25386652). {ECO:0000250|UniProtKB:C8VTV4,
CC ECO:0000269|PubMed:25386652}.
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 (By similarity). Interacts with LAE1 (PubMed:23390613).
CC {ECO:0000250|UniProtKB:C8VTV4, ECO:0000269|PubMed:23390613}.
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 -!- INDUCTION: Expression is regulated by light and darkness, but this
CC regulation is further modulated by the carbon source in relation to the
CC growth rate (PubMed:25386652). Expression is under the control of LAE1
CC (PubMed:23390613). {ECO:0000269|PubMed:23390613,
CC ECO:0000269|PubMed:25386652}.
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 loss of conidiation
CC and impairs formation of perithecia (PubMed:25386652). Completely
CC impairs the expression of cellulases, xylanases and the cellulase
CC regulator XYR1 (PubMed:25386652). {ECO:0000269|PubMed:25386652}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; GL985066; EGR48103.1; -; Genomic_DNA.
DR RefSeq; XP_006966146.1; XM_006966084.1.
DR AlphaFoldDB; G0RL42; -.
DR SMR; G0RL42; -.
DR EnsemblFungi; EGR48103; EGR48103; TRIREDRAFT_122284.
DR GeneID; 18483372; -.
DR KEGG; tre:TRIREDRAFT_122284; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_122284; -.
DR eggNOG; ENOG502S0HV; Eukaryota.
DR HOGENOM; CLU_022491_2_0_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
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..573
FT /note="Developmental and secondary metabolism regulator
FT VEL1"
FT /id="PRO_0000435772"
FT DOMAIN 26..220
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 222..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..504
FT /note="PEST"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT MOTIF 40..45
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT COMPBIAS 226..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..355
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 62878 MW; 7C5C3B5DD93A538E CRC64;
MATPSSVASS SSRDQVQRIH RVTRENRHLW YQLTVLQQPE RARACGSGMK ANSDRRPVDP
PPVVELRIIE GPSVEEGKDI TFDYNANFFL YASLEQARTI AHGRVQNGAT NNPPILTGVP
ASGMAYLDRP TEAGYFIFPD LSVRHEGYFR LSFSLYETTK EPKDFDLEPA DSDLPPGVDW
RMEIKTQPFN VFSAKKFPGL MESTSLSKTV ADQGCRVRIR RDVRMRKRDG KGSGFDRRGE
EEYSRRRTVT PAPAEDPNLR ARSVSNASEH RGPYMPQEPP RRPSAAESYH APPPLPPPPP
SSYDAPPPAA RPGHLGFGGD HNMPPQYGAP AARPYGHPQS APIPPATPTG PYPTSSAAPS
PYAKQDHHHQ QQYSYNSRPP APSASPAPPM KHAMYDNRPS EPYVPHSSPS VYASTERRPS
YANYSAPAPY STPASQPTYS TPASQPTYST PASQPTYSAP PPAPYSAPAP PPPRPSMSQS
SLAPLKIASL VSPLPPIEAQ TEPLPPPPML STGGKRKHDH VFSQNHKPLY NGQRQLDAHY
GHGYRGLTPE PDQGLYSRAD GQIGVVTFNQ YQV
