TBXT_XENLA
ID TBXT_XENLA Reviewed; 432 AA.
AC P24781; Q6IP86;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=T-box transcription factor T {ECO:0000305};
DE AltName: Full=Brachyury protein {ECO:0000305};
DE Short=xBRA;
DE AltName: Full=Protein T;
GN Name=tbxt {ECO:0000250|UniProtKB:O15178}; Synonyms=bra, t;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neurula;
RX PubMed=1717160; DOI=10.1016/0092-8674(91)90573-h;
RA Smith J.C., Price B.M., Green J.B., Weigel D., Herrmann B.G.;
RT "Expression of a Xenopus homolog of Brachyury (T) is an immediate-early
RT response to mesoderm induction.";
RL Cell 67:79-87(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=7906224; DOI=10.1002/j.1460-2075.1994.tb06268.x;
RA Cunliffe V., Smith J.C.;
RT "Specification of mesodermal pattern in Xenopus laevis by interactions
RT between Brachyury, noggin and Xwnt-8.";
RL EMBO J. 13:349-359(1994).
RN [4]
RP INDUCTION.
RX PubMed=10068640; DOI=10.1242/dev.126.7.1467;
RA Sun B.I., Bush S.M., Collins-Racie L.A., LaVallie E.R.,
RA DiBlasio-Smith E.A., Wolfman N.M., McCoy J.M., Sive H.L.;
RT "derriere: a TGF-beta family member required for posterior development in
RT Xenopus.";
RL Development 126:1467-1482(1999).
RN [5]
RP INDUCTION.
RX PubMed=10375512; DOI=10.1242/dev.126.14.3229;
RA Osada S., Wright C.V.E.;
RT "Xenopus nodal-related signaling is essential for mesendodermal patterning
RT during early embryogenesis.";
RL Development 126:3229-3240(1999).
RN [6]
RP FUNCTION.
RX PubMed=11111039; DOI=10.1016/s0378-1119(00)00417-0;
RA Sinha S., Abraham S., Gronostajski R.M., Campbell C.E.;
RT "Differential DNA binding and transcription modulation by three T-box
RT proteins, T, TBX1 and TBX2.";
RL Gene 258:15-29(2000).
RN [7]
RP FUNCTION.
RX PubMed=11869292; DOI=10.1046/j.1440-169x.2002.00624.x;
RA Kitaguchi T., Mizugishi K., Hatayama M., Aruga J., Mikoshiba K.;
RT "Xenopus Brachyury regulates mesodermal expression of Zic3, a gene
RT controlling left-right asymmetry.";
RL Dev. Growth Differ. 44:55-61(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-222, AND SUBUNIT.
RX PubMed=9349824; DOI=10.1038/39929;
RA Mueller C.W., Herrmann B.G.;
RT "Crystallographic structure of the T domain-DNA complex of the Brachyury
RT transcription factor.";
RL Nature 389:884-888(1997).
CC -!- FUNCTION: Involved in the transcriptional regulation of genes required
CC for mesoderm formation and differentiation (PubMed:11869292). Binds to
CC the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence
CC (PubMed:11111039). Causes dorsal mesodermal differentiation of animal
CC cap ectoderm when co-expressed with wnt8 and noggin (PubMed:7906224).
CC None of these molecules causes dorsal mesoderm formation when expressed
CC alone (PubMed:7906224). Establishes the left/right axis at early
CC gastrula stage by directly up-regulating mesodermal expression of zic3
CC (PubMed:11869292). {ECO:0000269|PubMed:11111039,
CC ECO:0000269|PubMed:11869292, ECO:0000269|PubMed:7906224}.
CC -!- SUBUNIT: When not bound to DNA, exists as a monomer (PubMed:9349824).
CC Binds DNA as a dimer (PubMed:9349824). {ECO:0000269|PubMed:9349824,
CC ECO:0000303|PubMed:9349824}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15178}.
CC -!- TISSUE SPECIFICITY: Expressed in presumptive mesodermal cells around
CC the blastopore, and then in the notochord.
CC -!- DEVELOPMENTAL STAGE: During gastrula and neurula stages in involuting
CC mesoderm and in the notochord.
CC -!- INDUCTION: By the natural signal and in response to the mesoderm-
CC inducing factors activin A, basic FGF/bFGF, derriere, nodal/nr-1,
CC nodal2/nr-2 and nodal4/nr-4. {ECO:0000269|PubMed:10068640,
CC ECO:0000269|PubMed:10375512}.
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DR EMBL; M77243; AAA49663.1; -; mRNA.
DR EMBL; BC072031; AAH72031.1; -; mRNA.
DR PIR; A41056; A41056.
DR RefSeq; NP_001084047.1; NM_001090578.1.
DR PDB; 1XBR; X-ray; 2.50 A; A/B=39-222.
DR PDBsum; 1XBR; -.
DR AlphaFoldDB; P24781; -.
DR SMR; P24781; -.
DR IntAct; P24781; 1.
DR DNASU; 399275; -.
DR GeneID; 399275; -.
DR KEGG; xla:399275; -.
DR CTD; 399275; -.
DR Xenbase; XB-GENE-865212; tbxt.S.
DR OMA; RNDHKDM; -.
DR OrthoDB; 1201455at2759; -.
DR EvolutionaryTrace; P24781; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 399275; Expressed in gastrula and 6 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IGI:BHF-UCL.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:UniProtKB.
DR GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
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; IPR002070; TF_Brachyury.
DR InterPro; IPR001699; TF_T-box.
DR InterPro; IPR018186; TF_T-box_CS.
DR PANTHER; PTHR11267; PTHR11267; 1.
DR Pfam; PF00907; T-box; 1.
DR PRINTS; PR00938; BRACHYURY.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Developmental protein; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..432
FT /note="T-box transcription factor T"
FT /id="PRO_0000184417"
FT DNA_BIND 49..217
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 274..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1XBR"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 84..97
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1XBR"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1XBR"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 160..177
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1XBR"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1XBR"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1XBR"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:1XBR"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1XBR"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:1XBR"
SQ SEQUENCE 432 AA; 47599 MW; 2F91D942D86EE60A CRC64;
MSATESCAKN VQYRVDHLLS AVENELQAGS EKGDPTEKEL KVSLEERDLW TRFKELTNEM
IVTKNGRRMF PVLKVSMSGL DPNAMYTVLL DFVAADNHRW KYVNGEWVPG GKPEPQAPSC
VYIHPDSPNF GAHWMKDPVS FSKVKLTNKM NGGGQIMLNS LHKYEPRIHI VRVGGTQRMI
TSHSFPETQF IAVTAYQNEE ITALKIKHNP FAKAFLDAKE RNDYKDILDE GIDSQHSNFS
QLGTWLIPNG GSLCSPNPHT QFGAPLSLSS PHGCERYSSL RNHRSAPYPS PYTHRNNSPN
NLADNSSACL SMLQSHDNWS TLQMPAHTGM LPMSHSTGTP PPSSQYPSLW SVSNSAITPV
SQSGGITNGI SSQYLLGSTP HYSSLSHAVP SPSTGSPLYE HGAQTEIAEN QYDVTAHSRL
SSTWTPVAPP SV
