STUA_EMENI
ID STUA_EMENI Reviewed; 622 AA.
AC P36011; C8V024; Q5B0U4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Cell pattern formation-associated protein stuA {ECO:0000305};
DE AltName: Full=Stunted protein A {ECO:0000303|PubMed:2062309};
GN Name=stuA {ECO:0000303|PubMed:2062309}; ORFNames=AN5836;
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 [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=1516832; DOI=10.1101/gad.6.9.1770;
RA Miller K.Y., Wu J., Miller B.L.;
RT "StuA is required for cell pattern formation in Aspergillus.";
RL Genes Dev. 6:1770-1782(1992).
RN [2]
RP SEQUENCE REVISION.
RA Miller B.L.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RX PubMed=2062309; DOI=10.1007/bf00259682;
RA Miller K.Y., Toennis T.M., Adams T.H., Miller B.L.;
RT "Isolation and transcriptional characterization of a morphological
RT modifier: the Aspergillus nidulans stunted (stuA) gene.";
RL Mol. Gen. Genet. 227:285-292(1991).
RN [6]
RP FUNCTION.
RX PubMed=8722771; DOI=10.1093/genetics/143.1.155;
RA Busby T.M., Miller K.Y., Miller B.L.;
RT "Suppression and enhancement of the Aspergillus nidulans medusa mutation by
RT altered dosage of the bristle and stunted genes.";
RL Genetics 143:155-163(1996).
RN [7]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9312029; DOI=10.1093/emboj/16.18.5710;
RA Dutton J.R., Johns S., Miller B.L.;
RT "StuAp is a sequence-specific transcription factor that regulates
RT developmental complexity in Aspergillus nidulans.";
RL EMBO J. 16:5710-5721(1997).
RN [8]
RP INDUCTION, AND FUNCTION.
RX PubMed=9315680; DOI=10.1128/mcb.17.10.6191;
RA Wu J., Miller B.L.;
RT "Aspergillus asexual reproduction and sexual reproduction are
RT differentially affected by transcriptional and translational mechanisms
RT regulating stunted gene expression.";
RL Mol. Cell. Biol. 17:6191-6201(1997).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9379904; DOI=10.1046/j.1365-2958.1997.5131873.x;
RA Suelmann R., Sievers N., Fischer R.;
RT "Nuclear traffic in fungal hyphae: in vivo study of nuclear migration and
RT positioning in Aspergillus nidulans.";
RL Mol. Microbiol. 25:757-769(1997).
RN [10]
RP FUNCTION.
RX PubMed=12455692; DOI=10.1128/ec.1.5.725-735.2002;
RA Scherer M., Wei H., Liese R., Fischer R.;
RT "Aspergillus nidulans catalase-peroxidase gene (cpeA) is transcriptionally
RT induced during sexual development through the transcription factor StuA.";
RL Eukaryot. Cell 1:725-735(2002).
RN [11]
RP INDUCTION.
RX PubMed=17630328; DOI=10.1128/ec.00189-07;
RA Breakspear A., Momany M.;
RT "Aspergillus nidulans conidiation genes dewA, fluG, and stuA are
RT differentially regulated in early vegetative growth.";
RL Eukaryot. Cell 6:1697-1700(2007).
RN [12]
RP INDUCTION.
RX PubMed=23516554; DOI=10.1371/journal.pone.0058762;
RA Kang E.H., Kim J.A., Oh H.W., Park H.M.;
RT "LAMMER Kinase LkhA plays multiple roles in the vegetative growth and
RT asexual and sexual development of Aspergillus nidulans.";
RL PLoS ONE 8:E58762-E58762(2013).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RX PubMed=25359270; DOI=10.1007/s12275-014-4517-y;
RA Park B.C., Park Y.H., Yi S., Choi Y.K., Kang E.H., Park H.M.;
RT "Transcriptional regulation of fksA, a beta-1,3-glucan synthase gene, by
RT the APSES protein StuA during Aspergillus nidulans development.";
RL J. Microbiol. 52:940-947(2014).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=25550299; DOI=10.3852/14-079;
RA Chung D., Upadhyay S., Bomer B., Wilkinson H.H., Ebbole D.J., Shaw B.D.;
RT "Neurospora crassa ASM-1 complements the conidiation defect in a stuA
RT mutant of Aspergillus nidulans.";
RL Mycologia 107:298-306(2015).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:1516832, PubMed:8722771, PubMed:9312029, PubMed:25550299).
CC Binds the StuA-response elements (StRE) with the consensus sequence 5'-
CC (A/T)CGCG(T/A)N(A/C)-3' at the promoters of target genes
CC (PubMed:9312029, PubMed:25359270). Required from the very earliest
CC events of asexual reproduction until completion of conidiophore
CC development, but is not specifically required for differentiation of
CC conidia (PubMed:1516832). Represses transcription of the abaA
CC developmental regulatory gene and of the developmentally regulated
CC awh11 gene (PubMed:9312029). Controls the expression of the catalase-
CC peroxidase gene cpeA (PubMed:12455692). Plays an important role in cell
CC wall biogenesis during the development by controlling the transcription
CC level of fksA (PubMed:25359270). {ECO:0000269|PubMed:12455692,
CC ECO:0000269|PubMed:1516832, ECO:0000269|PubMed:25359270,
CC ECO:0000269|PubMed:25550299, ECO:0000269|PubMed:8722771,
CC ECO:0000269|PubMed:9312029}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25550299,
CC ECO:0000269|PubMed:9379904}.
CC -!- INDUCTION: Expression is increased 50-fold during the establishment of
CC developmental competence (PubMed:1516832, PubMed:2062309,
CC PubMed:17630328). Expression is positively controlled by brlA
CC (PubMed:1516832). Expression is also regulated by the LAMMER kinase
CC lkhA (PubMed:23516554). {ECO:0000269|PubMed:1516832,
CC ECO:0000269|PubMed:2062309, ECO:0000269|PubMed:23516554}.
CC -!- DISRUPTION PHENOTYPE: Leads to defective conidiophore morphology and
CC impairs conidia production (PubMed:25550299). Affects cell wall beta-
CC 1,3-glucan biosynthesis (PubMed:25359270).
CC {ECO:0000269|PubMed:25359270, ECO:0000269|PubMed:25550299}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M83569; AAA33325.2; -; Genomic_DNA.
DR EMBL; AACD01000100; EAA58345.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70741.1; -; Genomic_DNA.
DR PIR; A44068; A44068.
DR RefSeq; XP_663440.1; XM_658348.1.
DR AlphaFoldDB; P36011; -.
DR SMR; P36011; -.
DR STRING; 162425.CADANIAP00007206; -.
DR EnsemblFungi; CBF70741; CBF70741; ANIA_05836.
DR EnsemblFungi; EAA58345; EAA58345; AN5836.2.
DR GeneID; 2870743; -.
DR KEGG; ani:AN5836.2; -.
DR VEuPathDB; FungiDB:AN5836; -.
DR eggNOG; ENOG502QW2C; Eukaryota.
DR HOGENOM; CLU_016460_0_0_1; -.
DR InParanoid; P36011; -.
DR OMA; MDVHSSH; -.
DR OrthoDB; 311987at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:AspGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0070787; P:conidiophore development; IMP:AspGD.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0070795; P:positive regulation of conidiophore development; IMP:AspGD.
DR GO; GO:0075307; P:positive regulation of conidium formation; IMP:AspGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:AspGD.
DR GO; GO:0000905; P:sporocarp development involved in asexual reproduction; IMP:AspGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR029790; EFG1/Phd1/StuA.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR47792; PTHR47792; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 1: Evidence at protein level;
KW Conidiation; DNA-binding; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..622
FT /note="Cell pattern formation-associated protein stuA"
FT /id="PRO_0000072296"
FT DOMAIN 129..235
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 163..184
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..590
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000303|PubMed:1516832"
FT COMPBIAS 258..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 66956 MW; 05D8AE2FAF497083 CRC64;
MASMNQPQPY MDVHSHLSSG QTYASHPATA GALTHYQYPQ QPPVLQPTST YGPASSYSQY
PYPNSVASSQ SVPPPTTSIS SQVPAQLLPL PVTNHPVPTH GYGNNSGTPM QGYVYDPTGQ
MAPPGAKPRV TATLWEDEGS LCYQVEAKGV CVARREDNGM INGTKLLNVA GMTRGRRDGI
LKSEKVRNVV KIGPMHLKGV WIPFDRALEF ANKEKITDLL YPLFVQHISN LLYHPANQNQ
RNMTVPDSRR LEGPQPVVRT PQAQQPPSLH HHSLQTPVPS HMSQPGGRPS LDRAHTFPTP
PASASSLIGI TSQNNSYDWN PGMNSSVPNT QPLSIDTSLS NARSMPTTPA TTPPGNNLQG
MQSYQPQSGY DSKPYYSAAP STHPQYAPQQ PLPQQSMAQY GHSMPTSSYR DMAPPSSQRG
SVTEIESDVK TERYGQGTVA KTEPEQEQEY AQPDSGYNTG RGSYYTTNPS VGGLAHDHSQ
LTPDMTGSPQ QNGSGRMTPR TSNTAPQWAP GYTTPPRPAA ASSLYNIVSD TRGTSGANGS
TSDNYSVASN SGYSTGMNGS MGSNKRMRDD DDDRIVPPDS RGEFDTKRRK TLTETPVGGP
VGGVPLGLQP MKAGGSLISA RR
