VEA_ASPFU
ID VEA_ASPFU Reviewed; 570 AA.
AC E9RCK4; Q4WSK1; Q6MYN4;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
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:16002655}; ORFNames=AFUA_1G12490;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA Barrell B.G., Hall N.;
RT "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT region encompassing the nitrate assimilation gene cluster.";
RL Fungal Genet. Biol. 41:443-453(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=16002655; DOI=10.1128/ec.4.7.1298-1307.2005;
RA Krappmann S., Bayram O., Braus G.H.;
RT "Deletion and allelic exchange of the Aspergillus fumigatus veA locus via a
RT novel recyclable marker module.";
RL Eukaryot. Cell 4:1298-1307(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23087369; DOI=10.1128/ec.00222-12;
RA Dhingra S., Andes D., Calvo A.M.;
RT "VeA regulates conidiation, gliotoxin production, and protease activity in
RT the opportunistic human pathogen Aspergillus fumigatus.";
RL Eukaryot. Cell 11:1531-1543(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION IN THE VELVET COMPLEX.
RX PubMed=22970834; DOI=10.1111/mmi.12032;
RA Park H.S., Bayram O., Braus G.H., Kim S.C., Yu J.H.;
RT "Characterization of the velvet regulators in Aspergillus fumigatus.";
RL Mol. Microbiol. 86:937-953(2012).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24116213; DOI=10.1371/journal.pone.0077147;
RA Dhingra S., Lind A.L., Lin H.C., Tang Y., Rokas A., Calvo A.M.;
RT "The fumagillin gene cluster, an example of hundreds of genes under veA
RT control in Aspergillus fumigatus.";
RL PLoS ONE 8:E77147-E77147(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 (By similarity). The velvet complex hat
CC acts as a global regulator for secondary metabolite gene expression (By
CC similarity). Controls the expression of hundreds of genes, including
CC those comprising more than a dozen known secondary metabolite gene
CC clusters (PubMed:24116213). Controls the expression of the gliotoxin
CC gene cluster (PubMed:23087369). Controls the expression of the
CC fumagillin, fumitremorgin G, fumigaclavine C and glionitrin gene
CC clusters (PubMed:24116213). The regulation of the fumagillin gene
CC cluster and fumagillin production is performed through direct control
CC of the expression of fumR (PubMed:24116213). Negatively regulates
CC conidiation (PubMed:22970834, PubMed:23087369). Required for normal
CC protease activity (PubMed:23087369). {ECO:0000250|UniProtKB:C8VTV4,
CC ECO:0000269|PubMed:22970834, ECO:0000269|PubMed:23087369,
CC ECO:0000269|PubMed:24116213}.
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: Reduces sporulation capacities on nitrate-
CC containing medium (PubMed:16002655). Results in the abundant formation
CC of conidiophores (PubMed:22970834). Leads to a reduction of gliotoxin
CC production (PubMed:23087369). Decreases the production of fumagillin,
CC fumitremorgin G, fumigaclavine C and Glionitrin A (PubMed:24116213).
CC Reduces also protease activity (PubMed:23087369).
CC {ECO:0000269|PubMed:16002655, ECO:0000269|PubMed:22970834,
CC ECO:0000269|PubMed:23087369, ECO:0000269|PubMed:24116213}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; BX649605; CAE47975.1; -; Genomic_DNA.
DR EMBL; AAHF01000004; EAL90581.1; -; Genomic_DNA.
DR RefSeq; XP_752619.1; XM_747526.1.
DR AlphaFoldDB; E9RCK4; -.
DR SMR; E9RCK4; -.
DR STRING; 746128.CADAFUBP00001175; -.
DR EnsemblFungi; EAL90581; EAL90581; AFUA_1G12490.
DR GeneID; 3510437; -.
DR KEGG; afm:AFUA_1G12490; -.
DR VEuPathDB; FungiDB:Afu1g12490; -.
DR eggNOG; ENOG502QVY9; Eukaryota.
DR HOGENOM; CLU_022491_2_0_1; -.
DR InParanoid; E9RCK4; -.
DR OMA; NFFLYAT; -.
DR OrthoDB; 1171722at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0070787; P:conidiophore development; IMP:AspGD.
DR GO; GO:0070794; P:negative regulation of conidiophore development; IMP:AspGD.
DR GO; GO:0043942; P:negative regulation of sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0043945; P:positive regulation of asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:1900691; P:positive regulation of gliotoxin biosynthetic process; IMP:AspGD.
DR GO; GO:0009847; P:spore germination; IMP:AspGD.
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..570
FT /note="Developmental and secondary metabolism regulator
FT veA"
FT /id="PRO_0000435763"
FT DOMAIN 25..231
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..24
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 266..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..493
FT /note="PEST"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT REGION 504..541
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 273..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 63032 MW; 7A6A83213F422021 CRC64;
MATRPPLMPP ANETESSVSR ISREGKKITY KLSVMQQPER ARACGAGAKS SADRRPVDPP
PVVELRIFES DPNDDLHKTD ITFAYNANFF LFATLETARP MAQGRLTGPP TCPVLTGVPV
AGVAYLDRPQ QAGYFIFPDL SVRHEGRYRL SFHLYEEIKD IKDADKDTPM PDLNSSTNLT
KPSAPKAHLN FRLEVKSVPF TVYSAKKFPG LATSTSLSRI IAEQGCRVRI RRDVRMRRRG
EKRTDDYDFD DERAFATRSD RYTTPDMYAA NSAERARSTS ISTTADTSFP YGSDAQRRPS
AGDYGFQGAQ PYQRSMPAAS AAPAPAPVHS PATSAQTSSY QSHLSFGATQ SQYPAPQLPP
TPQSATPTNT YSPHPSYSHS RNPSNGTEYD ATSSGYPYPQ PRLPADRPSY SKAALPPLRL
EPPKAPNMQT STDSRSSDAN AYPTLSQPPV PRAPTPANHV TSLPPLKVLS GEYSHPSQPN
AQSPHHDLGS GKRLLWETNH TLSKRSHEET FGSDERPLHN GMRPDMDQYP SMGRKQPDYG
RLPFYTDSRD EMAYKRANGR MVMKILPALP
