VOSA_EMENI
ID VOSA_EMENI Reviewed; 430 AA.
AC Q5BBX1; A0SP16; C8VL31;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Spore development regulator vosA {ECO:0000305};
DE AltName: Full=Viability of spores protein A {ECO:0000303|PubMed:17912349};
GN Name=vosA {ECO:0000303|PubMed:21152013}; ORFNames=ANIA_01959;
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], INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17912349; DOI=10.1371/journal.pone.0000970;
RA Ni M., Yu J.H.;
RT "A novel regulator couples sporogenesis and trehalose biogenesis in
RT Aspergillus nidulans.";
RL PLoS ONE 2:E970-E970(2007).
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 INDUCTION.
RX PubMed=20817115; DOI=10.1016/j.fgb.2010.08.009;
RA Kwon N.J., Shin K.S., Yu J.H.;
RT "Characterization of the developmental regulator FlbE in Aspergillus
RT fumigatus and Aspergillus nidulans.";
RL Fungal Genet. Biol. 47:981-993(2010).
RN [5]
RP INDUCTION.
RX PubMed=20624219; DOI=10.1111/j.1365-2958.2010.07282.x;
RA Kwon N.J., Garzia A., Espeso E.A., Ugalde U., Yu J.H.;
RT "FlbC is a putative nuclear C2H2 transcription factor regulating
RT development in Aspergillus nidulans.";
RL Mol. Microbiol. 77:1203-1219(2010).
RN [6]
RP INTERACTION WITH VELB, SUBCELLULAR LOCATION, 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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND INTERACTION WITH VELB.
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 VELC.
RX PubMed=24587098; DOI=10.1371/journal.pone.0089883;
RA Park H.S., Nam T.Y., Han K.H., Kim S.C., Yu J.H.;
RT "VelC positively controls sexual development in Aspergillus nidulans.";
RL PLoS ONE 9:E89883-E89883(2014).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 1-190 IN COMPLEX WITH VELB,
RP DISRUPTION PHENOTYPE, DOMAIN, MUTAGENESIS OF LYS-37; LYS-39; ARG-41 AND
RP LYS-42, FUNCTION, AND DNA-BINDING.
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 velB-VosA heterodimeric complex that plays a
CC dual role in activating genes associated with spore maturation and
CC repressing certain development-associated genes (PubMed:17912349,
CC PubMed:21152013, PubMed:23049895, PubMed:24391470). Controls primarily
CC the late process of sporulation including trehalose biogenesis
CC (PubMed:17912349). The complex binds DNA through the DNA-binding domain
CC of vosA that recognizes an 11-nucleotide consensus sequence 5'-
CC CTGGCCGCGGC-3' consisting of two motifs in the promoters of key
CC developmental regulatory genes (PubMed:24391470). The vosA-velB complex
CC binds to the beta-glucan synthase fksA gene promoter in asexual spores
CC for repression (PubMed:25960370). {ECO:0000250|UniProtKB:A0SP16,
CC ECO:0000269|PubMed:17912349, ECO:0000269|PubMed:21152013,
CC ECO:0000269|PubMed:23049895, ECO:0000269|PubMed:25960370}.
CC -!- SUBUNIT: Forms a heterodimeric complex with VelB; the formation of the
CC velB-vosA complex is light-dependent (PubMed:21152013,
CC PubMed:23049895). Interacts also with velC (PubMed:24587098).
CC {ECO:0000269|PubMed:21152013, ECO:0000269|PubMed:23049895,
CC ECO:0000269|PubMed:24587098}.
CC -!- INTERACTION:
CC Q5BBX1; C8VTS4: velB; NbExp=5; IntAct=EBI-16088812, EBI-16088850;
CC Q5BBX1; Q5BBX1: vosA; NbExp=3; IntAct=EBI-16088812, EBI-16088812;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17912349,
CC ECO:0000269|PubMed:21152013}. Note=Localizes in the nucleus of mature
CC conidia (PubMed:17912349). {ECO:0000269|PubMed:17912349}.
CC -!- INDUCTION: Expression is induced in conidia, ascospores and during the
CC late phase of conidiation when conidia differentiate and become mature
CC (PubMed:17912349). During vegetative growth, expression quickly drops
CC and continues to be undetectable (or low) until 24 hours post induction
CC of conidiation (PubMed:17912349). Expression is positively regulated by
CC abaA (PubMed:23049895). Expression is under the regulation of the flbE
CC transcription factor (PubMed:20817115). Expression is also under the
CC regulation of the flbC transcription factor (PubMed:20624219).
CC {ECO:0000269|PubMed:17912349, ECO:0000269|PubMed:20624219,
CC ECO:0000269|PubMed:20817115, ECO:0000269|PubMed:23049895}.
CC -!- DOMAIN: The N-terminal velvet domain contains a NF-kappa-B-like fold
CC and is involved in DNA-binding (PubMed:24391470).
CC {ECO:0000269|PubMed:24391470}.
CC -!- DISRUPTION PHENOTYPE: Results in the lack of trehalose in spores, a
CC rapid loss of the cytoplasm, organelles and viability of spores, and a
CC dramatic reduction in tolerance of conidia to heat and oxidative stress
CC (PubMed:17912349). Down-regulates genes associated with spore
CC maturation and up-regulates certain development-associated genes
CC (PubMed:24391470). Results in elevated accumulation of beta-glucan in
CC asexual spores (PubMed:25960370). {ECO:0000269|PubMed:24391470,
CC ECO:0000269|PubMed:25960370}.
CC -!- SIMILARITY: Belongs to the velvet family. VosA subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF85898.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA65124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ856465; ABI51618.1; -; mRNA.
DR EMBL; BN001307; CBF85898.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000029; EAA65124.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_659563.1; XM_654471.1.
DR PDB; 4N6Q; X-ray; 1.79 A; A=1-190.
DR PDB; 4N6R; X-ray; 2.20 A; A=1-190.
DR PDBsum; 4N6Q; -.
DR PDBsum; 4N6R; -.
DR AlphaFoldDB; Q5BBX1; -.
DR SMR; Q5BBX1; -.
DR DIP; DIP-60679N; -.
DR IntAct; Q5BBX1; 1.
DR STRING; 162425.CADANIAP00008619; -.
DR EnsemblFungi; EAA65124; EAA65124; AN1959.2.
DR GeneID; 2875240; -.
DR KEGG; ani:AN1959.2; -.
DR VEuPathDB; FungiDB:AN1959; -.
DR eggNOG; ENOG502RYQD; Eukaryota.
DR HOGENOM; CLU_034766_1_0_1; -.
DR InParanoid; Q5BBX1; -.
DR OrthoDB; 1407766at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0005992; P:trehalose biosynthetic process; 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 3D-structure; Nucleus; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..430
FT /note="Spore development regulator vosA"
FT /id="PRO_0000435787"
FT DOMAIN 14..185
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 314..321
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:M2TGT8"
FT COMPBIAS 313..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 37
FT /note="K->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:24391470"
FT MUTAGEN 39
FT /note="K->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:24391470"
FT MUTAGEN 41
FT /note="R->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:24391470"
FT MUTAGEN 42
FT /note="K->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:24391470"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4N6R"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4N6Q"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4N6R"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:4N6Q"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:4N6Q"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 71..85
FT /evidence="ECO:0007829|PDB:4N6Q"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 127..139
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:4N6Q"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4N6Q"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4N6Q"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:4N6Q"
SQ SEQUENCE 430 AA; 47330 MW; 7EF43AD3427B9202 CRC64;
MSAANYPDPS LPRPSTSDDF ELIVRQNPNR ARVAGGKEKE RKPVDPPPIV QIRVREEGTY
LAQHYLQSPY FFMSCSLYDA QEDAPASIPP STALTGTLVS SLHRLKDVDN TDGGFFVWGD
LSIKVEGDFR LKFSLFEMRK TDVVFLKSIV SERFTVSPPK SFPGMAESTF LSRSFADQGV
KLRIRKEPRT LIKRTAPRPE EYPQAAIPRS PSDRTAMQIP GSSYPAPPYQ PTSRDYSYYA
PVKRQRTSVD YGARGMYDAD GRMRQMETYP QTATLYGQPG GYPTPMMGYP SGHGGVPDYA
MSYGLPPSAQ VPQMQDPAAQ SRSSQQATMQ SLGMVNPPGT PTPDSARAMM QQAYPRPQYS
ASTAVLPPLQ QSRNYPQGTN GATRGYYEQS PQATPILPSQ PLGTSEAERY GVPPGHTGYD
HTGSANGTPR
