VEA_ASPFN
ID VEA_ASPFN Reviewed; 574 AA.
AC B8NIF0;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Developmental and secondary metabolism regulator veA {ECO:0000305};
DE AltName: Full=Velvet complex subunit A {ECO:0000305};
GN Name=veA {ECO:0000303|PubMed:16988822}; ORFNames=AFLA_066460;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16988822; DOI=10.1007/s00253-006-0581-5;
RA Duran R.M., Cary J.W., Calvo A.M.;
RT "Production of cyclopiazonic acid, aflatrem, and aflatoxin by Aspergillus
RT flavus is regulated by veA, a gene necessary for sclerotial formation.";
RL Appl. Microbiol. Biotechnol. 73:1158-1168(2007).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17646985; DOI=10.1007/s00253-007-1081-y;
RA Cary J.W., O'Brian G.R., Nielsen D.M., Nierman W., Harris-Coward P., Yu J.,
RA Bhatnagar D., Cleveland T.E., Payne G.A., Calvo A.M.;
RT "Elucidation of veA-dependent genes associated with aflatoxin and
RT sclerotial production in Aspergillus flavus by functional genomics.";
RL Appl. Microbiol. Biotechnol. 76:1107-1118(2007).
RN [4]
RP INDUCTION.
RX PubMed=18667168; DOI=10.1016/j.fgb.2008.06.009;
RA Kale S.P., Milde L., Trapp M.K., Frisvad J.C., Keller N.P., Bok J.W.;
RT "Requirement of LaeA for secondary metabolism and sclerotial production in
RT Aspergillus flavus.";
RL Fungal Genet. Biol. 45:1422-1429(2008).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19411623; DOI=10.1128/ec.00088-09;
RA Amaike S., Keller N.P.;
RT "Distinct roles for VeA and LaeA in development and pathogenesis of
RT Aspergillus flavus.";
RL Eukaryot. Cell 8:1051-1060(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION IN THE VELVET COMPLEX.
RX PubMed=23994319; DOI=10.1016/j.fgb.2013.08.009;
RA Chang P.K., Scharfenstein L.L., Li P., Ehrlich K.C.;
RT "Aspergillus flavus VelB acts distinctly from VeA in conidiation and may
RT coordinate with FluG to modulate sclerotial production.";
RL Fungal Genet. Biol. 58:71-79(2013).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24584515; DOI=10.1007/s00253-014-5598-6;
RA Duran R.M., Gregersen S., Smith T.D., Bhetariya P.J., Cary J.W.,
RA Harris-Coward P.Y., Mattison C.P., Grimm C., Calvo A.M.;
RT "The role of Aspergillus flavus veA in the production of extracellular
RT proteins during growth on starch substrates.";
RL Appl. Microbiol. Biotechnol. 98:5081-5094(2014).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24951443; DOI=10.1128/ec.00099-14;
RA Baidya S., Duran R.M., Lohmar J.M., Harris-Coward P.Y., Cary J.W.,
RA Hong S.Y., Roze L.V., Linz J.E., Calvo A.M.;
RT "VeA is associated with the response to oxidative stress in the aflatoxin
RT producer Aspergillus flavus.";
RL Eukaryot. Cell 13:1095-1103(2014).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24412484; DOI=10.1016/j.fgb.2014.01.001;
RA Cary J.W., Harris-Coward P.Y., Ehrlich K.C., Di Mavungu J.D.,
RA Malysheva S.V., De Saeger S., Dowd P.F., Shantappa S., Martens S.L.,
RA Calvo A.M.;
RT "Functional characterization of a veA-dependent polyketide synthase gene in
RT Aspergillus flavus necessary for the synthesis of asparasone, a sclerotium-
RT specific pigment.";
RL Fungal Genet. Biol. 64:25-35(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26209694; DOI=10.1128/ec.00092-15;
RA Cary J.W., Han Z., Yin Y., Lohmar J.M., Shantappa S., Harris-Coward P.Y.,
RA Mack B., Ehrlich K.C., Wei Q., Arroyo-Manzanares N., Uka V., Vanhaecke L.,
RA Bhatnagar D., Yu J., Nierman W.C., Johns M.A., Sorensen D., Shen H.,
RA De Saeger S., Diana Di Mavungu J., Calvo A.M.;
RT "Transcriptome analysis of Aspergillus flavus reveals veA-dependent
RT regulation of secondary metabolite gene clusters, including the novel
RT aflavarin cluster.";
RL Eukaryot. Cell 14:983-997(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 hat
CC acts as a global regulator for secondary metabolite gene expression
CC (PubMed:16988822, PubMed:26209694). Controls the expression of the
CC cyclopiazonic acid, aflatrem, and aflatoxin gene clusters
CC (PubMed:16988822, PubMed:17646985). Controls the expression of the
CC sclerotium-specific pigment asparasone A gene cluster (PubMed:16988822,
CC PubMed:17646985). Controls the expression of the aflavarin gene cluster
CC (PubMed:26209694). controls also the production of hydrolases and other
CC extracellular proteins during growth on natural starch-based substrates
CC (PubMed:24584515). Regulates genes involved in the High Osmolarity
CC Glycerol (HOG) signaling pathway (PubMed:24951443). Required for the
CC conidial and sclerotial density-dependent production (PubMed:23994319,
CC PubMed:24412484). {ECO:0000250|UniProtKB:C8VTV4,
CC ECO:0000269|PubMed:16988822, ECO:0000269|PubMed:17646985,
CC ECO:0000269|PubMed:19411623, ECO:0000269|PubMed:23994319,
CC ECO:0000269|PubMed:24412484, ECO:0000269|PubMed:24584515,
CC ECO:0000269|PubMed:24951443, ECO:0000269|PubMed:26209694}.
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:23994319). {ECO:0000269|PubMed:23994319}.
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 positively regulated by laeA
CC (PubMed:18667168). {ECO:0000269|PubMed:18667168}.
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 expression of aflR and sclerotia
CC production (PubMed:19411623, PubMed:23994319). Unables metabolization
CC of host cell lipid reserves and is inhibited by oleic acid in growth
CC assays (PubMed:19411623). Blocks the production of aflatrem and
CC aflatoxin; and strongly decreases cyclopiazonic acid production
CC (PubMed:16988822, PubMed:17646985). Down-regulates transcription of
CC ps27, a polyketide synthase gene belonging to the asparasone A gene
CC cluster (PubMed:24412484). Down-regulates five genes found within the
CC aflavarin cluster (PubMed:26209694). Results in a reduction in
CC transcription levels of oxidative stress response genes after exposure
CC to hydrogen peroxide (PubMed:24951443). Alters the starch-degradation
CC profile (PubMed:24584515). {ECO:0000269|PubMed:16988822,
CC ECO:0000269|PubMed:17646985, ECO:0000269|PubMed:19411623,
CC ECO:0000269|PubMed:23994319, ECO:0000269|PubMed:24412484,
CC ECO:0000269|PubMed:24584515, ECO:0000269|PubMed:24951443,
CC ECO:0000269|PubMed:26209694}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; EQ963479; EED49824.1; -; Genomic_DNA.
DR RefSeq; XP_002380205.1; XM_002380164.1.
DR AlphaFoldDB; B8NIF0; -.
DR SMR; B8NIF0; -.
DR STRING; 5059.CADAFLAP00008070; -.
DR EnsemblFungi; EED49824; EED49824; AFLA_066460.
DR eggNOG; ENOG502QVY9; Eukaryota.
DR HOGENOM; CLU_022491_2_0_1; -.
DR Proteomes; UP000001875; 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; Sporulation; Transcription; Transcription regulation.
FT CHAIN 1..574
FT /note="Developmental and secondary metabolism regulator
FT veA"
FT /id="PRO_0000435760"
FT DOMAIN 25..230
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..498
FT /note="PEST"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT REGION 513..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..44
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 63034 MW; 6862B50391F2EBF6 CRC64;
MATRAPLAPP PNETEASVSR ITREGKKLTY KLNVMQQPER ARACGAGAKS SADRRPVDPP
PVVELRVYES DPNDDLNKTD ITFAYNANFF LYATLETARP MAQGRFAPNP TCPVLTGVPV
AGVAYLDRPS QAGYFIFPDL SVRHEGVYRL NFHLYEETKE SKDANENAPI QSMSNPMPSK
PMAPKSFLEF RLEVVSVPFT VFSAKKFPGL ATSTSLSRVI AEQGCRVRIR RDVRMRRRGE
KRTDDYDYDE ERVYRSSDRI STPDTHGYAG TPVERPRSTS TSTVDPSFPY GVDAQRRSSG
ATEYGFQGAQ PYQRPLPPAP GPAPAAVSTP APPAPPAPPS HNPGYQSHLS FGSTQTQYPA
PQLPPTPQTA STLAAPYSPH PSYSHARNPS TSAEYETPGY SYPPSRMSTE RSSYPKNGLP
PLRLEPPKPL NMPSGEPRSS DPNAYHSVAQ SAAPRSQTPS SSLVPSLPPL KALSGDYPNN
LSQSSSSTSQ SPSHDLGAGK KFFWDTGASL SKRSYEDSFG HDDRPLYNGM RPDTESYPRR
LSDASRNFYN ETRDEMAYKR ANGRMATKIS PALQ
