ID   VEA_ASPPA               Reviewed;         574 AA.
AC   Q69B22;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 31.
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:15294809};
OS   Aspergillus parasiticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15294809; DOI=10.1128/aem.70.8.4733-4739.2004;
RA   Calvo A.M., Bok J., Brooks W., Keller N.P.;
RT   "veA is required for toxin and sclerotial production in Aspergillus
RT   parasiticus.";
RL   Appl. Environ. Microbiol. 70:4733-4739(2004).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19889978; DOI=10.1073/pnas.0907416106;
RA   Chanda A., Roze L.V., Kang S., Artymovich K.A., Hicks G.R., Raikhel N.V.,
RA   Calvo A.M., Linz J.E.;
RT   "A key role for vesicles in fungal secondary metabolism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19533-19538(2009).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20735852; DOI=10.1186/1471-2091-11-33;
RA   Roze L.V., Chanda A., Laivenieks M., Beaudry R.M., Artymovich K.A.,
RA   Koptina A.V., Awad D.W., Valeeva D., Jones A.D., Linz J.E.;
RT   "Volatile profiling reveals intracellular metabolic changes in Aspergillus
RT   parasiticus: veA regulates branched chain amino acid and ethanol
RT   metabolism.";
RL   BMC Biochem. 11:33-33(2010).
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:15294809). Controls the expression of the aflatoxin gene
CC       cluster (PubMed:15294809, PubMed:19889978). Required for the expression
CC       of aflR and aflJ (PubMed:15294809). Mediates the coordination of
CC       aflatoxigenic vesicles (aflatoxisomes) development with aflatoxin gene
CC       expression (PubMed:19889978). Regulates branched chain amino acid and
CC       ethanol metabolism and acts as a positive regulator of mitochondrial
CC       and peroxisomal beta-oxidation (PubMed:20735852).
CC       {ECO:0000250|UniProtKB:C8VTV4, ECO:0000269|PubMed:15294809,
CC       ECO:0000269|PubMed:19889978, ECO:0000269|PubMed:20735852}.
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 (By similarity). {ECO:0000250|UniProtKB:C8VTV4}.
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   -!- 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: Blocks sclerotial formation, reduces conidiation
CC       both on the culture medium and on peanut seeds, and abolishes
CC       production of the visible orange aflatoxin intermediate versicolorin A
CC       (PubMed:15294809). Fails to accumulate aflatoxisomes under aflatoxin-
CC       inducing conditions in the dark (PubMed:19889978). Enhances
CC       accumulation of metabolites in branched chain amino acid catabolism and
CC       increases ethanol production (PubMed:20735852).
CC       {ECO:0000269|PubMed:15294809, ECO:0000269|PubMed:19889978,
CC       ECO:0000269|PubMed:20735852}.
CC   -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR   EMBL; AY445513; AAS07022.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69B22; -.
DR   SMR; Q69B22; -.
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   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..574
FT                   /note="Developmental and secondary metabolism regulator
FT                   veA"
FT                   /id="PRO_0000435762"
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..501
FT                   /note="PEST"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   REGION          513..548
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..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  62948 MW;  6C86E3F53CDB6C3F CRC64;
     MATRAPLAPP PNETEASVSR ITREGKKLTY KLNVMQQPER ARACGAGAKS SADRRPVDPP
     PVVELRVYES DPNDDLNKTD ITFAYNANFF LYATLETARP MAQGRFAPNP TCPVLTGVPV
     AGVAYLDRPS QAGYFIFPDL SVRHEGVYRL NFHLYEETKE SKDANENAPI QSMSNPMPAK
     PMAPKSFLEF RLEVVSVPFT VFSAKKFPGL ATSTSLSRVI AEQGCRVRIR RDVRMRRRGE
     KRTDDYDYDE ERVYRSSDRF STPDTHGYAG TPVERPRSTS TSTVDPSFPY GADAQRRSSG
     ATEHGFQGAQ PYQRPMPPAP VPAPVAVSTP APPAPPAPPS HNPGYQSHLS FGSTQTQYPA
     PQLPPTPQSA STLAAPYSPH PSYSHARNPS TSAEYETPGY SYPSSRVSTE RSSYPKNGLP
     PLRLEPPKPL NMPSGEPRSS DPNAYHSVAQ SAGPRSQTPS SSLVPSLPPL KALSGDYPNN
     LSQPSSSISQ SPSHDLGAGK KFLWDTGASL SKRSYEDSFG HDDRPLYNGM RPDTESHPRR
     LSDAGRNFYN ETRDEMAYKR ANGRMATKIS PALQ