ID   VEGT_XENBO              Reviewed;         454 AA.
AC   Q98UD2;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=T-box protein VegT {ECO:0000250|UniProtKB:P87377, ECO:0000312|EMBL:AAK00596.1};
GN   Name=vegt {ECO:0000312|EMBL:AAK00596.1};
OS   Xenopus borealis (Kenyan clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8354;
RN   [1] {ECO:0000312|EMBL:AAK00596.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bubunenko M., Vempati U.D., King M.L.;
RT   "Characterization of the RNA signal that directs vegetal localization of
RT   VegT, the primary germ layer determinant in Xenopus.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor required for both mesoderm and endoderm
CC       formation in the embryo; signaling determinants and concentration
CC       levels may determine which germ layer is formed. Acts together with
CC       beta-catenin to activate genes that are responsible for mesoderm
CC       induction including wnt-8, eomes t/bra, siamois, mix1 and sox17.
CC       Directly binds to promoter DNA. Patterns the mesoderm along the
CC       dorsoventral and posterior axis. Activates siamois gene transcription
CC       when alone or in combination with beta-catenin, but inhibits siamois
CC       transcription in combination with pou5f1.1/oct-25 (By similarity).
CC       {ECO:0000250|UniProtKB:P87377}.
CC   -!- SUBUNIT: Forms a repression complex on the promoters of the nodal/nr1
CC       and siamois genes with the maternal factors tcf7l1/tcf3 and
CC       pouf5.1/oct-25. Interacts (via C-terminus) with tcf7l1/tcf3 (via N-
CC       terminus). Also interacts with the other POU-domain transcription
CC       factors pou5f1.2/oct-91 and pou5f1.3/oct-60 (By similarity).
CC       {ECO:0000250|UniProtKB:P87377}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P87377,
CC       ECO:0000255|PROSITE-ProRule:PRU00201}.
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; AF180351; AAK00596.1; -; mRNA.
DR   AlphaFoldDB; Q98UD2; -.
DR   SMR; Q98UD2; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00182; TBOX; 1.
DR   Gene3D; 2.60.40.820; -; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR046360; T-box_DNA-bd.
DR   InterPro; IPR036960; T-box_sf.
DR   InterPro; IPR001699; TF_T-box.
DR   InterPro; IPR018186; TF_T-box_CS.
DR   PANTHER; PTHR11267; PTHR11267; 2.
DR   Pfam; PF00907; T-box; 1.
DR   PRINTS; PR00937; TBOX.
DR   SMART; SM00425; TBOX; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   PROSITE; PS01283; TBOX_1; 1.
DR   PROSITE; PS01264; TBOX_2; 1.
DR   PROSITE; PS50252; TBOX_3; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..454
FT                   /note="T-box protein VegT"
FT                   /id="PRO_0000390493"
FT   DNA_BIND        57..230
FT                   /note="T-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT   REGION          229..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  51855 MW;  4623D860475AD6AC CRC64;
     MRNCCRERGF SVGCLEPETS FSCASDVKPS PDMDSVSSQD SLYLPNSIGA SLQDQDLWSQ
     FHQEGTEMII TKSGRRMFPQ CKIRLFGLHL YAKYMLLVDF VPLDNFRYKW NKNQWEAAGK
     AEPHPPCRTY VHPDSPASGA HWMKDPICFQ KLKLTNNTLD QQGHIILHSM HRYKPRFHVV
     QSDDMYNSPW GLVQVFSFPE TEFTAVTAYQ NEKITKLKIN HNPFAKGFRE QERSHKRDDV
     LRTLQQSPGK RQKRKKWEDS PEADISDFPK ATRVKEESVM DPAVVYQNWV SDHEANQGLT
     PHSPESEGVN QEQQVPTSSL NFYNKSQHRS SQHLSSPYDL GEPSSRRLTP DVATVPDSDQ
     DSLAVLHGIP TQDSAQERTC SMNISMETPV KQPLRGTIYS SYGTEQWMVP AQGQYQPVGY
     TAYQTDLSTQ GAVAHQHSGM SDWSQYSLFP YSCW