ID   BRC2_HALRO              Reviewed;         681 AA.
AC   O01409;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=T-box-containing protein 2;
DE   AltName: Full=AS-T2;
GN   Name=T2;
OS   Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Pyuridae; Halocynthia.
OX   NCBI_TaxID=7729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=8954744; DOI=10.1006/dbio.1996.0345;
RA   Yasuo H., Kobayashi M., Shimauchi Y., Satoh N.;
RT   "The ascidian genome contains another T-domain gene that is expressed in
RT   differentiating muscle and the tip of the tail of the embryo.";
RL   Dev. Biol. 180:773-779(1996).
CC   -!- FUNCTION: Involved in the transcriptional regulation of genes required
CC       for muscle differentiation. Binds to a palindromic site (called T site)
CC       and activates gene transcription when bound to such a site (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
CC   -!- TISSUE SPECIFICITY: Differentiating muscle and tailbud tip.
CC   -!- DEVELOPMENTAL STAGE: First detected in the vegetal hemisphere at the
CC       32-cell stage. Expression continues in endothelial lineage until 110-
CC       cell stage when it declines here and becomes evident in muscle lineage
CC       cells. Expression increases throughout gastrulation and neurulation in
CC       differentiating muscle cells until late tailbud stage. Expression also
CC       detected in the tailbud tip from mid-gastrulation to tail elongation.
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; D83265; BAA19689.1; -; mRNA.
DR   AlphaFoldDB; O01409; -.
DR   SMR; O01409; -.
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; 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   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..681
FT                   /note="T-box-containing protein 2"
FT                   /id="PRO_0000184465"
FT   DNA_BIND        149..323
FT                   /note="T-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT   REGION          316..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  76430 MW;  0DD8C8C0CD54A2E5 CRC64;
     MSAFPISDIG GSWEYSHAPP TATSATGIPG FPEQSVGGLQ LPFPGYTYVG ASPLTQPRRH
     FPNSTPVLGN YAGLSSDREV IATSLNPYIS KFSANAEWPI SDIHQSKKSV YIPEERDVSN
     QFQTDKQQQQ QFMKLPDPQM QVQLCDKELW DQFSRAGTEM IVTKTGRRMF PGYRIKISGL
     DPTAKYCVML DIVNVDDHRY KFQHGEWTVA GRGEPHLPQR FFLHPNSPAN GSKWMSEIIS
     FHKVKLTNSI GRDVDGKIVL NSMHRYQPRV HIVRTDDISS VHMQRLCTFA FPQTVFITVT
     AYQNSEVTKL KIDNNPFAKG FREDGARAKK PRNQHNHFSD NDTSPYSEQR RSYYEPGSYT
     HLPYYNNSPM NVPSHHHYDN QTMNREFLPE AKRNRIMPES NSIHAPSLSV FHPGNENAVS
     QWQDVPDLNE MYNANDNNYN SVANQSIHNV QYTQNGITSH SPVQPVPHDN SFTYYNSSSP
     SSSDSNQSNV NASFSVMTTT HASHSINDIM RISEHADVTS PNINIPNTVE TNVHSSDSGI
     GSSPPTPSDD DASNLIPGTE EIFKDDGKVL DGENLPDMSD LISLTERKES GEANANSHTE
     DFSRNPACQS GDTIESKDIQ TLQVASVTDT YSYQKNYVEN SSHQSYNNSQ EFSYHSNAMP
     ESNCESSVDP NLDWESNLLT M