TBX6_XENLA
ID TBX6_XENLA Reviewed; 506 AA.
AC Q8AV66; Q2I0I2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=T-box transcription factor TBX6;
DE Short=T-box protein 6;
DE Short=XTbx6;
GN Name=tbx6 {ECO:0000312|EMBL:BAC20262.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC20262.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Neurula {ECO:0000269|PubMed:11737146};
RX PubMed=11737146; DOI=10.1046/j.1440-169x.2001.00606.x;
RA Uchiyama H., Kobayashi T., Yamashita A., Ohno S., Yabe S.;
RT "Cloning and characterization of the T-box gene Tbx6 in Xenopus laevis.";
RL Dev. Growth Differ. 43:657-669(2001).
RN [2]
RP ERRATUM OF PUBMED:11737146.
RA Uchiyama H., Kobayashi T., Yamashita A., Ohno S., Yabe S.;
RL Dev. Growth Differ. 44:95-96(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC20262.1}
RP SEQUENCE REVISION TO 405 AND 424.
RA Uchiyama H.;
RT "T-box gene Tbx6 in Xenopus laevis.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAC20262.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fang P.-F., Ding X.-Y.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP INDUCTION.
RX PubMed=15188053; DOI=10.1093/abbs/36.6.390;
RA Fang P.-F., Hu R.-Y., He X.-Y., Ding X.-Y.;
RT "Multiple signaling pathways control Tbx6 expression during Xenopus
RT myogenesis.";
RL Acta Biochim. Biophys. Sin. 36:390-396(2004).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=16953215; DOI=10.1038/sj.cr.7310093;
RA Lou X., Fang P.-F., Li S., Hu R.-Y., Kuerner K.-M., Steinbeisser H.,
RA Ding X.-Y.;
RT "Xenopus Tbx6 mediates posterior patterning via activation of Wnt and FGF
RT signalling.";
RL Cell Res. 16:771-779(2006).
RN [7] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16343478; DOI=10.1016/j.ydbio.2005.11.020;
RA Li H.-Y., Bourdelas A., Carron C., Gomez C., Boucaut J.-C., Shi D.-L.;
RT "FGF8, Wnt8 and Myf5 are target genes of Tbx6 during anteroposterior
RT specification in Xenopus embryo.";
RL Dev. Biol. 290:470-481(2006).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RIPPLY2.2, AND IDENTIFICATION IN A COMPLEX WITH
RP RIPPLY2.2 AND TLE4.
RX PubMed=17577580; DOI=10.1016/j.bbrc.2007.05.211;
RA Kondow A., Hitachi K., Okabayashi K., Hayashi N., Asashima M.;
RT "Bowline mediates association of the transcriptional corepressor XGrg-4
RT with Tbx6 during somitogenesis in Xenopus.";
RL Biochem. Biophys. Res. Commun. 359:959-964(2007).
CC -!- FUNCTION: Transcriptional activator. Plays a role in ventral mesoderm
CC specification and acts together with nog during muscle differentiation.
CC Mediates posterior pattern formation of the embryo, including
CC specification of posterior mesoderm, via activation of the Wnt and Fgf
CC signaling pathways. {ECO:0000269|PubMed:11737146,
CC ECO:0000269|PubMed:16343478, ECO:0000269|PubMed:16953215,
CC ECO:0000269|PubMed:17577580}.
CC -!- SUBUNIT: Interacts with ripply2.2/bowline. Associates with tle4 in the
CC presence of ripply2.2/bowline. {ECO:0000269|PubMed:17577580}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
CC -!- TISSUE SPECIFICITY: At gastrulation, expressed in the lateral and
CC ventral mesoderm. Expressed around the blastopore except at the dorsal
CC midline. As gastrulation proceeds, expression extends anteriorly and
CC ventrally. At the tailbud stage, expression then retracts caudally
CC becoming restricted to the tip of the tailbud.
CC {ECO:0000269|PubMed:11737146, ECO:0000269|PubMed:16343478}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in early gastrula embryos,
CC reaches a peak in late gastrula to early neurula embryos (stages 13-16)
CC and then declines until stage 30. {ECO:0000269|PubMed:11737146}.
CC -!- INDUCTION: By activin and vegt signaling, both acting via nodal. By bmp
CC signaling in a dose-dependent manner. Fgf is necessary but not
CC sufficient for induction. {ECO:0000269|PubMed:15188053}.
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DR EMBL; AB091393; BAC20262.1; -; mRNA.
DR EMBL; DQ355794; ABC75836.1; -; mRNA.
DR RefSeq; NP_001081165.1; NM_001087696.1.
DR AlphaFoldDB; Q8AV66; -.
DR SMR; Q8AV66; -.
DR GeneID; 394428; -.
DR KEGG; xla:394428; -.
DR CTD; 394428; -.
DR Xenbase; XB-GENE-6254214; tbx6.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IPI: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:0009952; P:anterior/posterior pattern specification; IMP:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IPI:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; 1.
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 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..506
FT /note="T-box transcription factor TBX6"
FT /id="PRO_0000302091"
FT DNA_BIND 105..278
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 276..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..364
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 405
FT /note="Missing (in Ref. 1; BAC20262)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="P -> S (in Ref. 1; BAC20262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 56559 MW; 53B8D1BF1D624D44 CRC64;
MYHSELFQQY GTSYTMRPPH ALAPTYPSAG GHHDSYRYSE LDVPSQRFDG LFPALEPSQR
ILGAPPLTPL SLPPGPALGF GQVQPPCETP QLPGNVKMKL ENKELWKQFH SIGTEMIITK
SGRRMFPQCK VSVSGLEADG KYLLLADLLP VDNSRYKWQE DHWEASGRAE PRLPERVYIH
PDSPAPGSHW MKQPISFHKI KLTNNTLDQM GHIILHSMHK YQPRFHIVRA QDVFSRRWGG
CSSFTFPETL FLTVTAYQNE KITQLKIQTN PFAKGFREDG MKSKRDRSIR GKRKVISVEQ
EQEEEEQFQP EGECKRPPLY SGPCDSTLSE ELDIGRSLGI PSPNCSFHPI TPPTQTPPST
ETPNPSLPAN QEQGAPLQMS SQTPGTFLQT YPEPPRGASS LYSCSPTDAA QNQTLRPSAQ
RLPPGYQESP HISHSQGELK IYGTEMGPPG NFNPPSCAVT PSVRLSDEPM GRGFSMNFPH
FLPNNKIGLQ ISGAQLQRMY NGGGWM