TBX2_CAEEL
ID TBX2_CAEEL Reviewed; 423 AA.
AC Q19691;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=T-box protein 2;
GN Name=tbx-2 {ECO:0000312|WormBase:F21H11.3};
GN ORFNames=F21H11.3 {ECO:0000312|WormBase:F21H11.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7774921; DOI=10.1016/0888-7543(95)80128-9;
RA Agulnik S.I., Bollag R.J., Silver L.M.;
RT "Conservation of the T-box gene family from Mus musculus to Caenorhabditis
RT elegans.";
RL Genomics 25:214-219(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, SUMOYLATION, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16701625; DOI=10.1016/j.ydbio.2006.04.001;
RA Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G.;
RT "The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required
RT for ABa-derived pharyngeal muscle in C. elegans.";
RL Dev. Biol. 295:664-677(2006).
RN [4]
RP FUNCTION.
RX PubMed=18505863; DOI=10.1534/genetics.108.088948;
RA Singhvi A., Frank C.A., Garriga G.;
RT "The T-box gene tbx-2, the homeobox gene egl-5 and the asymmetric cell
RT division gene ham-1 specify neural fate in the HSN/PHB lineage.";
RL Genetics 179:887-898(2008).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF HIS-145.
RX PubMed=23933492; DOI=10.1016/j.ydbio.2013.08.001;
RA Milton A.C., Packard A.V., Clary L., Okkema P.G.;
RT "The NF-Y complex negatively regulates Caenorhabditis elegans tbx-2
RT expression.";
RL Dev. Biol. 382:38-47(2013).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP HIS-145.
RX PubMed=25873636; DOI=10.1534/g3.115.018101;
RA Milton A.C., Okkema P.G.;
RT "Caenorhabditis elegans TBX-2 Directly Regulates Its Own Expression in a
RT Negative Autoregulatory Loop.";
RL G3 (Bethesda) 5:1177-1186(2015).
CC -!- FUNCTION: Involved in the transcriptional regulation of genes required
CC for the development of pharyngeal muscles derived from the ABa lineage
CC (PubMed:16701625, PubMed:23933492). Acts as a transcriptional repressor
CC and binds to T-box binding sites in its own promoter to negatively
CC autoregulate its own expression in neurons, seam cells and the gut in
CC order to restrict its expression to certain tissues (PubMed:25873636).
CC May function together with the nfya-1-NF-Y complex to repress its own
CC expression (PubMed:25873636). Plays a role in neural fate specification
CC in the hermaphrodite-specific neuron (HSN)/PHB neuron lineage, acting
CC in concert with homeobox protein egl-5 and the asymmetric cell division
CC protein ham-1. {ECO:0000269|PubMed:16701625,
CC ECO:0000269|PubMed:18505863, ECO:0000269|PubMed:23933492,
CC ECO:0000269|PubMed:25873636}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201,
CC ECO:0000269|PubMed:16701625}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles and a subset of
CC pharyngeal neurons. Expressed in head neurons and occassionally tail
CC neurons (PubMed:23933492, PubMed:25873636). Not expressed in the
CC pharynx (PubMed:23933492). {ECO:0000269|PubMed:16701625,
CC ECO:0000269|PubMed:23933492, ECO:0000269|PubMed:25873636}.
CC -!- DEVELOPMENTAL STAGE: First expressed in embryos at the 100-cell stage
CC (PubMed:16701625). First expressed in pharyngeal precursors at the 100-
CC 200 cell stage and expression continues in the pharynx until near
CC hatching, when expression becomes restricted to several neurons in the
CC head (PubMed:23933492, PubMed:25873636). In larval stages, expressed in
CC head neurons and occasionally tail neurons (PubMed:23933492). In L4
CC larvae, expressed in the gut and seam cells (PubMed:23933492). In
CC larval stages, not expressed in the pharynx (PubMed:23933492).
CC {ECO:0000269|PubMed:16701625, ECO:0000269|PubMed:23933492,
CC ECO:0000269|PubMed:25873636}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:16701625}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in 70% lethality
CC at the larval stages (PubMed:23933492). RNAi-mediated knockdown
CC enhances the larval lethality phenotype of the nfyb-1 cu13 mutant
CC (PubMed:23933492). {ECO:0000269|PubMed:23933492}.
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DR EMBL; BX284603; CCD69847.1; -; Genomic_DNA.
DR PIR; B88450; B88450.
DR PIR; D56530; D56530.
DR RefSeq; NP_498088.1; NM_065687.3.
DR AlphaFoldDB; Q19691; -.
DR SMR; Q19691; -.
DR BioGRID; 40929; 3.
DR STRING; 6239.F21H11.3; -.
DR EPD; Q19691; -.
DR PaxDb; Q19691; -.
DR PeptideAtlas; Q19691; -.
DR EnsemblMetazoa; F21H11.3.1; F21H11.3.1; WBGene00006543.
DR UCSC; F21H11.3.2; c. elegans.
DR WormBase; F21H11.3; CE01245; WBGene00006543; tbx-2.
DR eggNOG; KOG3585; Eukaryota.
DR GeneTree; ENSGT00940000163374; -.
DR HOGENOM; CLU_024824_3_0_1; -.
DR InParanoid; Q19691; -.
DR OMA; LMYSTFR; -.
DR OrthoDB; 995977at2759; -.
DR PhylomeDB; Q19691; -.
DR PRO; PR:Q19691; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006543; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005667; C:transcription regulator complex; ISS:WormBase.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0042694; P:muscle cell fate specification; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0042048; P:olfactory behavior; IMP:WormBase.
DR GO; GO:0043282; P:pharyngeal muscle development; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:WormBase.
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 Developmental protein; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..423
FT /note="T-box protein 2"
FT /id="PRO_0000184469"
FT DNA_BIND 70..243
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 238..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 145
FT /note="H->Y: In bx59; results in 44-50% lethality at the
FT larval stages. Morphological defects in the pharynx.
FT Increases tbx-2 expression in head neurons and in the
FT syncytial head hypodermal cell hyp6. 98% lethality at the
FT L1 larval stage in a nfyb-1 mutant (cu13) background, which
FT may be due to increased tbx-2 promoter activity."
FT /evidence="ECO:0000269|PubMed:23933492,
FT ECO:0000269|PubMed:25873636"
SQ SEQUENCE 423 AA; 46997 MW; 91FD17596F213F40 CRC64;
MAFNPFALGR PDLLLPFMGA GVGGPGAGGP PPNLFFSMLQ AGFPPGPVGS PPEDDGVTDD
PKVELDEREL WQQFSQCGTE MVITKSGRRI FPAYRVKISG LDKKSQYFVM MDLVPADEHR
YKFNNSRWMI AGKADPEMPK TLYIHPDSPS TGEHWMSKGA NFHKLKLTNN ISDKHGYTIL
NSMHKYQPRL HVVRCADRHN LMYSTFRTFV FRETEFIAVT AYQNEKVTEL KIENNPFAKG
FRDAGAGKRE KKRQLHRMNG DATQSPPGKT ASLPTHSPHP SESNSEDDEP TLKKCKPEPS
QTPTTSSLST STTPTLSAHH PLRSPQFCIP PPIDMMYQNM PMDLLAHWQM ATLFPQFSMA
LNSPAAAASL LSKHLAKASS ECKVEATSED SEEAEKPEVK KEQKSVTPPK KGGFDVLDLL
SKP
