STUA_ASPFU
ID STUA_ASPFU Reviewed; 635 AA.
AC Q4X228;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Cell pattern formation-associated protein stuA {ECO:0000305};
DE AltName: Full=Stunted protein A {ECO:0000250|UniProtKB:P36011};
GN Name=stuA {ECO:0000303|PubMed:16207816}; ORFNames=AFUA_2G07900;
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 [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 [2]
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16207816; DOI=10.1091/mbc.e05-07-0617;
RA Sheppard D.C., Doedt T., Chiang L.Y., Kim H.S., Chen D., Nierman W.C.,
RA Filler S.G.;
RT "The Aspergillus fumigatus StuA protein governs the up-regulation of a
RT discrete transcriptional program during the acquisition of developmental
RT competence.";
RL Mol. Biol. Cell 16:5866-5879(2005).
RN [3]
RP FUNCTION.
RX PubMed=18490465; DOI=10.1128/iai.01483-07;
RA Gravelat F.N., Doedt T., Chiang L.Y., Liu H., Filler S.G., Patterson T.F.,
RA Sheppard D.C.;
RT "In vivo analysis of Aspergillus fumigatus developmental gene expression
RT determined by real-time reverse transcription-PCR.";
RL Infect. Immun. 76:3632-3639(2008).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19028996; DOI=10.1128/ec.00265-08;
RA Twumasi-Boateng K., Yu Y., Chen D., Gravelat F.N., Nierman W.C.,
RA Sheppard D.C.;
RT "Transcriptional profiling identifies a role for BrlA in the response to
RT nitrogen depletion and for StuA in the regulation of secondary metabolite
RT clusters in Aspergillus fumigatus.";
RL Eukaryot. Cell 8:104-115(2009).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19527167; DOI=10.1086/600070;
RA Urb M., Pouliot P., Gravelat F.N., Olivier M., Sheppard D.C.;
RT "Aspergillus fumigatus induces immunoglobulin E-independent mast cell
RT degranulation.";
RL J. Infect. Dis. 200:464-472(2009).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23925951; DOI=10.1007/s00284-013-0434-2;
RA Mulinti P., Allen N.A., Coyle C.M., Gravelat F.N., Sheppard D.C.,
RA Panaccione D.G.;
RT "Accumulation of ergot alkaloids during conidiophore development in
RT Aspergillus fumigatus.";
RL Curr. Microbiol. 68:1-5(2014).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:16207816, PubMed:19028996). Binds the StuA-response elements
CC (StRE) with the consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the
CC promoters of target genes (By similarity). Controls the expression of 6
CC secondary metabolite biosynthetic clusters including 2 involved in the
CC synthesis of alkaloids (fumigaclavine and fumitremorgen), 2 clusters of
CC the ETP class (gliotoxin and an unknown ETP-like toxin), a cluster
CC predicted to produce pseurotin A, and the product of the last cluster
CC is unknown (PubMed:19028996). Controls the production of ergot
CC alkaloids during conidiophore development (PubMed:23925951). Controls
CC expression of sspA and gliP (PubMed:18490465). Involved in the
CC induction of immunoglobulin E-independent mast cell degranulation
CC (PubMed:19527167). {ECO:0000250|UniProtKB:P36011,
CC ECO:0000269|PubMed:16207816, ECO:0000269|PubMed:18490465,
CC ECO:0000269|PubMed:19028996, ECO:0000269|PubMed:19527167,
CC ECO:0000269|PubMed:23925951}.
CC -!- INDUCTION: Induced at the onset of developmental competence and highly
CC expressed in competent hyphae (PubMed:16207816).
CC {ECO:0000269|PubMed:16207816}.
CC -!- DISRUPTION PHENOTYPE: Impairs the ability to undergo asexual
CC reproduction with abnormal morphology of conidiophores and only small
CC numbers of dysmorphic conidia exhibiting precocious germination
CC (PubMed:16207816, PubMed:19028996). Displayed reduced expression of the
CC catalase gene cat1 and hypersusceptibility to hydrogen peroxide
CC (PubMed:16207816). Impairs the production of ergot alkaloids such as
CC chanoclavine-I, festuclavine, fumigaclavine A, fumigaclavine B, and
CC fumigaclavine C (PubMed:23925951). Impairs A.fumigatus immunoglobulin
CC E-independent mast cell degranulation induction (PubMed:19527167).
CC {ECO:0000269|PubMed:16207816, ECO:0000269|PubMed:19028996,
CC ECO:0000269|PubMed:19527167, ECO:0000269|PubMed:23925951}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; AAHF01000001; EAL93087.1; -; Genomic_DNA.
DR RefSeq; XP_755125.1; XM_750032.1.
DR AlphaFoldDB; Q4X228; -.
DR SMR; Q4X228; -.
DR STRING; 746128.CADAFUBP00002335; -.
DR EnsemblFungi; EAL93087; EAL93087; AFUA_2G07900.
DR GeneID; 3513229; -.
DR KEGG; afm:AFUA_2G07900; -.
DR eggNOG; ENOG502QW2C; Eukaryota.
DR HOGENOM; CLU_016460_0_0_1; -.
DR InParanoid; Q4X228; -.
DR OMA; MDVHSSH; -.
DR OrthoDB; 311987at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
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 SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 2: Evidence at transcript level;
KW Conidiation; DNA-binding; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..635
FT /note="Cell pattern formation-associated protein stuA"
FT /id="PRO_0000435970"
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..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..605
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000250|UniProtKB:P36011"
FT COMPBIAS 246..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 67772 MW; 54FFC7CCBD9D38E9 CRC64;
MNQTQPYMDV HSSHLSSAQP YASHAATAGA MAHYPQYHQQ PPVLQPASTY GPASSYSQYA
YPSGVASSQT APPPPSTSMS SQVPAQLLPL PVNSHTVTAP GYGNTTGTPM QGFVYDTTGQ
LAPPGAKPRV TATLWEDEGS LCYQVEAKGV CVARREDNHM INGTKLLNVA GMTRGRRDGI
LKSEKVRHVV KIGPMHLKGV WIPFERALEF ANKEKITDLL YPLFVHNIGG LLYHPTNQTR
TNMVVQESQQ RRLEGPPSAR TPQASQPPAL HHHHSMQTSI PSQMPQPPTM SSQPGARPPL
DRAHTFPTPP ASASSLMGLS NQSSSYDWNN QGMNSGVPNT QPLSIDTTLS NTRSMPTTPA
TTPPGNNLQG MQSYQSQSGY DTSKPYYSTA PPSHPHYAPQ YSLSQYGQPM PPHSYIKNEM
APPAGRAPGG QSETETSDVK PADRYSQSNG HVTAGAGESA PEHESEYVQH DNTGYGASRS
SYTYTTNTSV GSLAGEHSQL TNDITGSPQQ NGSGRMTPRT GGGPPPQWAS GYASPRPTAA
SSLYNIVSDT RGSSNGAGSE NYTVASNTAP TYSMGGSLGS GKRGREDDDM GRPDSQGDYE
SKRRRTNETT VGGPVGGVLL GLQPMKAGGA MPRRR
