TBX1A_XENLA
ID TBX1A_XENLA Reviewed; 463 AA.
AC Q8AX98;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=T-box transcription factor TBX1-A;
DE Short=T-box protein 1-A;
GN Name=tbx1-a;
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], FUNCTION, DOMAIN, AND DEVELOPMENTAL STAGE.
RX PubMed=15736267; DOI=10.1002/dvdy.20276;
RA Ataliotis P., Ivins S., Mohun T.J., Scambler P.J.;
RT "XTbx1 is a transcriptional activator involved in head and pharyngeal arch
RT development in Xenopus laevis.";
RL Dev. Dyn. 232:979-991(2005).
RN [2]
RP INTERACTION WITH DSCR6.
RX PubMed=19247927; DOI=10.1387/ijdb.082823kh;
RA Hitachi K., Danno H., Tazumi S., Aihara Y., Uchiyama H., Okabayashi K.,
RA Kondow A., Asashima M.;
RT "The Xenopus Bowline/Ripply family proteins negatively regulate the
RT transcriptional activity of T-box transcription factors.";
RL Int. J. Dev. Biol. 53:631-639(2009).
RN [3]
RP FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22354841; DOI=10.1242/dev.071456;
RA Janesick A., Shiotsugu J., Taketani M., Blumberg B.;
RT "RIPPLY3 is a retinoic acid-inducible repressor required for setting the
RT borders of the pre-placodal ectoderm.";
RL Development 139:1213-1224(2012).
CC -!- FUNCTION: Probable transcriptional regulator involved in developmental
CC processes (By similarity). Binds to the palindromic T site 5'-
CC TTCACACCTAGGTGTGAA-3' DNA sequence (By similarity). Induces pre-
CC placodal ectoderm (PPE) gene expression in regions where RIPPLY3 is
CC absent. Plays a role in the formation of the anteroposterior (AP) axis
CC during embryonic development; required to establish the posterolateral
CC border of the pre-placodal ectoderm (PPE) acting downstream of the
CC retinoic acid receptor (RAR) signaling. {ECO:0000250|UniProtKB:O43435,
CC ECO:0000250|UniProtKB:P70323, ECO:0000269|PubMed:15736267,
CC ECO:0000269|PubMed:22354841}.
CC -!- SUBUNIT: Binds DNA as a dimer (By similarity). Interacts with
CC dscr6/ripply3 (PubMed:19247927). {ECO:0000250|UniProtKB:O43435,
CC ECO:0000269|PubMed:19247927}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
CC -!- DEVELOPMENTAL STAGE: First detected shortly after the mid-blastula
CC transition and is localized to the presumptive mesoderm at mid-gastrula
CC stages. Expression persists in the lateral plate mesoderm at neurula
CC stages and is found in the pharyngeal arches and otic vesicles from
CC early tail bud stages onward. Expressed in the pre-placodal ectoderm
CC domain at stage 18. {ECO:0000269|PubMed:15736267,
CC ECO:0000269|PubMed:22354841}.
CC -!- INDUCTION: Up-regulated by retinoc acid (RA) in the pre-placodal
CC ectoderm (PPE) during post-gastrulation development. Up-regulated by
CC retinoc acid (RA) before, but inhibited after, neurogenesis
CC development. {ECO:0000269|PubMed:22354841}.
CC -!- DOMAIN: The C-terminus acts as a transcriptional activation domain.
CC {ECO:0000269|PubMed:15736267}.
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DR EMBL; AF526274; AAN77134.1; -; mRNA.
DR RefSeq; NP_001083914.1; NM_001090445.1.
DR AlphaFoldDB; Q8AX98; -.
DR SMR; Q8AX98; -.
DR GeneID; 399188; -.
DR KEGG; xla:399188; -.
DR CTD; 399188; -.
DR Xenbase; XB-GENE-6254396; tbx1.S.
DR OrthoDB; 1185429at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 399188; Expressed in internal ear and 8 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0060788; P:ectodermal placode formation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; 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; 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 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..463
FT /note="T-box transcription factor TBX1-A"
FT /id="PRO_0000262460"
FT DNA_BIND 119..297
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 39..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 51290 MW; 73AE0347C8B5A8B3 CRC64;
MISAISSPWL TQLSHFCDVA AFTANSLSSL NATGGYHLSP SPGDPYSQHE PHYEPCSASQ
HSYSFGHACP EPESGASSSS CASSTPGSGS TGSSSSNKAP VKKNPKVANI NVQLEMKALW
DEFNQLGTEM IVTKAGRRMF PTFQVKIFGM DPMADYMLLM DFVPVDDKRY RYAFHSSSWL
VAGKADPATP GRVHYHPDSP AKGAQWMKQI VSFDKLKLTN NLLDDNGHII LNSMHRYQPR
FHVVYVDPRK DSEKYAEENF KTFVFEETRF TAVTAYQNHR ITQLKIASNP FAKGFRDCDP
EDWPRNHRPG SLPLMNAFAR SRNPVSSPTQ NGSDKDGDGR REYERDASGT PLHGDAAHQQ
LMSRVLSLSL PVPGGLVPLS TGRPSPPHEL RLDPHSQGSE PLHHHPYKYP TSYDRYLGAK
TRPAPYPLPT IRGHGYHHHH MNPAAANMYS GAGAPGSYEY GPR
