STUA_USTMA
ID STUA_USTMA Reviewed; 624 AA.
AC A0A0D1CVS5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Cell pattern formation-associated protein ust1 {ECO:0000305};
DE AltName: Full=Stunted protein A {ECO:0000250|UniProtKB:P36011};
GN Name=ust1; ORFNames=UMAG_15042;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20064064; DOI=10.1094/mpmi-23-2-0211;
RA Garcia-Pedrajas M.D., Baeza-Montanez L., Gold S.E.;
RT "Regulation of Ustilago maydis dimorphism, sporulation, and pathogenic
RT development by a transcription factor with a highly conserved APSES
RT domain.";
RL Mol. Plant Microbe Interact. 23:211-222(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=25208341; DOI=10.1094/mpmi-07-14-0215-r;
RA Baeza-Montanez L., Gold S.E., Espeso E.A., Garcia-Pedrajas M.D.;
RT "Conserved and distinct functions of the 'Stunted' (StuA)-homolog Ust1
RT during cell differentiation in the corn smut fungus Ustilago maydis.";
RL Mol. Plant Microbe Interact. 28:86-102(2015).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:25208341). Binds the StuA-response elements (StRE) with the
CC consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of
CC target genes (By similarity). Regulates dimorphism, virulence, and the
CC sporulation program (PubMed:20064064). Required for mating, gall
CC induction, and sporogenesis in maize tissue (PubMed:20064064).
CC Regulates expression of the filament-down-regulated gene UM00205 and
CC the teliospore-specific gene ssp1 (PubMed:20064064).
CC {ECO:0000250|UniProtKB:P36011, ECO:0000269|PubMed:20064064,
CC ECO:0000269|PubMed:25208341}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25208341}.
CC Note=Accumulates in the nucleus during teliospore germination
CC (PubMed:25208341). {ECO:0000269|PubMed:25208341}.
CC -!- PTM: Phosphorylated but is not a target of cAMP signaling
CC (PubMed:25208341). {ECO:0000269|PubMed:25208341}.
CC -!- DISRUPTION PHENOTYPE: Leads to filamentous growth and abolishes mating
CC and gall induction (PubMed:20064064). In culture, produces abundant
CC thick-walled, highly pigmented cells resembling teliospores which are
CC normally produced only in planta (PubMed:20064064, PubMed:25208341).
CC {ECO:0000269|PubMed:20064064, ECO:0000269|PubMed:25208341}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; CM003142; KIS70488.1; -; Genomic_DNA.
DR RefSeq; XP_011388143.1; XM_011389841.1.
DR AlphaFoldDB; A0A0D1CVS5; -.
DR SMR; A0A0D1CVS5; -.
DR STRING; 237631.A0A0D1CVS5; -.
DR EnsemblFungi; KIS70488; KIS70488; UMAG_15042.
DR GeneID; 23568133; -.
DR KEGG; uma:UMAG_15042; -.
DR VEuPathDB; FungiDB:UMAG_15042; -.
DR OrthoDB; 839215at2759; -.
DR Proteomes; UP000000561; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein level;
KW Conidiation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Sporulation; Transcription; Transcription regulation.
FT CHAIN 1..624
FT /note="Cell pattern formation-associated protein ust1"
FT /id="PRO_0000435984"
FT DOMAIN 233..339
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 267..288
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 43..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 65238 MW; A375D02482055421 CRC64;
MSTASPLHHG HGNGSYANSP APTGVTGRDA GVAAAAVADS AVRSGSVPAS ASGSAPGSAS
GSMYGEAHTQ HHTGHHHYSA HHTHSHGALT SPVNGGHSSS WSPYGYPAAP VYGGSPSPYG
HNAYSQYASG YGYANGTAHH VATAPTTPSA TSTAYHTGVN GMMMHHGQHA GYGYSSHHLG
SHTPTHTHTH SSAYFMNGDG AHSHLNSSAH LTSPSYTTAP QYSTQLPLAG RHRVTTTLWE
DEGTLCFQVD ARGVCVARRH DNNMINGTKL LNVCGMSRGK RDGILKNEKE RIVVKVGAMH
LKGVWISFAR AKQLAEQNGI ADALYPLFEP NIQSFLYHPD NYPRTAAVIA AAQERQAQRQ
RAPGGQPSPG ANGTSQAPPL MRANTTPSNG DTSTFSSGLS SLGSWTGSHD QGHASAPTTA
QPSPSSMHNG ATQMHMSLSN HGTASPTYAQ SQQQQQQQQQ QQQQQQQQQQ QQQQQAYPMT
AAQQLARPSV GDRRQSAPIS LNNSVGHAEN PYGATNLGGA ANGGLVNGAR KVSGLKRSWN
DADDLNGSAA ASPTERDMQR SGSGGSNGLK LDGDDLHSPD SSDDRLAKKT RGMPQRGGGA
TTAMPSMSTN MLMGVGNGSG IHHE
