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VEGTB_XENLA
ID   VEGTB_XENLA             Reviewed;         455 AA.
AC   O13161;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=T-box protein VegT-B;
DE   AltName: Full=Xenopus optomotor blind {ECO:0000303|PubMed:9012520};
DE            Short=Xombi {ECO:0000312|EMBL:AAH70708.1};
GN   Name=vegt-b; Synonyms=vegt;
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:AAB50917.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RX   PubMed=9012520; DOI=10.1242/dev.122.12.4001;
RA   Lustig K.D., Kroll K.L., Sun E.E., Kirschner M.W.;
RT   "Expression cloning of a Xenopus T-related gene (Xombi) involved in
RT   mesodermal patterning and blastopore lip formation.";
RL   Development 122:4001-4012(1996).
RN   [2] {ECO:0000312|EMBL:AAH70708.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte {ECO:0000312|EMBL:AAH70708.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=10974673;
RX   DOI=10.1002/1097-0177(2000)9999:9999<::aid-dvdy1025>3.0.co;2-e;
RA   Kavka A.I., Green J.B.;
RT   "Evidence for dual mechanisms of mesoderm establishment in Xenopus
RT   embryos.";
RL   Dev. Dyn. 219:77-83(2000).
CC   -!- FUNCTION: Transcription factor required for both mesoderm and endoderm
CC       formation in the embryo; signaling determinants and concentration
CC       levels may determine which germ layer is formed. Acts together with
CC       beta-catenin to activate genes that are responsible for mesoderm
CC       induction including wnt-8, eomes t/bra, siamois, mix1 and sox17.
CC       Directly binds to promoter DNA. Patterns the mesoderm along the
CC       dorsoventral and posterior axis. Activates siamois gene transcription
CC       when alone or in combination with beta-catenin, but inhibits siamois
CC       transcription in combination with pou5f1.1/oct-25.
CC       {ECO:0000250|UniProtKB:P87377, ECO:0000269|PubMed:10974673,
CC       ECO:0000269|PubMed:9012520}.
CC   -!- SUBUNIT: Forms a repression complex on the promoters of the nodal/nr1
CC       and siamois genes with the maternal factors tcf7l1/tcf3 and
CC       pouf5.1/oct-25. Interacts (via C-terminus) with tcf7l1/tcf3 (via N-
CC       terminus). Also interacts with the other POU-domain transcription
CC       factors pou5f1.2/oct-91 and pou5f1.3/oct-60 (By similarity).
CC       {ECO:0000250|UniProtKB:P87377}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P87377,
CC       ECO:0000255|PROSITE-ProRule:PRU00201}.
CC   -!- TISSUE SPECIFICITY: Maternally localized to the vegetal hemisphere of
CC       oocytes. Zygotic expression parallels blastopore formation and shifts
CC       from dorsal expression in the marginal zone of late blastula and early
CC       gastrula stages to a ventral/lateral expression at later stages. During
CC       neurula and tailbud stages, expressed in the posterior and anterior
CC       ends of the embryo. During tailbud stages, expressed in a subset of
CC       interneurons in the neural tube. {ECO:0000269|PubMed:9012520}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expression declines considerably at the end of gastrulation but
CC       continues at a low level until the tadpole stage (stage 38).
CC       {ECO:0000269|PubMed:9012520}.
CC   -!- INDUCTION: By mesoderm-inducers including t/bra, and both FGF and TGF-
CC       beta family members. FGF signaling is not required for initial
CC       expression in the dorsal marginal zone, but is required for its
CC       continued expression during mid to late gastrula stages.
CC       {ECO:0000269|PubMed:9012520}.
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DR   EMBL; S83518; AAB50917.1; -; mRNA.
DR   EMBL; BC070708; AAH70708.1; -; mRNA.
DR   RefSeq; NP_001081671.1; NM_001088202.1.
DR   AlphaFoldDB; O13161; -.
DR   SMR; O13161; -.
DR   BioGRID; 99325; 1.
DR   IntAct; O13161; 1.
DR   DNASU; 397990; -.
DR   GeneID; 397990; -.
DR   KEGG; xla:397990; -.
DR   CTD; 397990; -.
DR   Xenbase; XB-GENE-1033836; vegt.S.
DR   OMA; PLFPYAC; -.
DR   OrthoDB; 810611at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 397990; Expressed in gastrula and 10 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; 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; 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   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..455
FT                   /note="T-box protein VegT-B"
FT                   /id="PRO_0000390488"
FT   DNA_BIND        57..230
FT                   /note="T-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT   REGION          229..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  51963 MW;  2B9C8FBCCD78E37D CRC64;
     MRNCCRERGF SVGRLEPETS FSCASDVKSS PDMDSVSSQD SLYLPNSIGA SLEDQNLWTQ
     FHQEGTEMII TKSGRRMFPQ CKIRLFGLHP YTKYMLLVDF VPLDNFRYKW NKNQWEAAGK
     AEPHPPCRTY VHPDSPASGA HWMKDPICFQ KLKLTNNTLD QQGHIILHSM HRYKPRFHVV
     QSDDMYNSPW GLVQVFSFPE TEFTAVTAYQ NEKITKLKIN HNPFAKGFRE QERSHKRDDV
     LKTLQQSPSK SQKRKKWEDS PEADISDFPK ATRIKEESIM DPAGVYQNWV SDHEANQGLT
     PHSPESEGVN QEQQVPTSSS NFYIKSQYRR SSQHLSSPYD LGEPSSRRLT PDVATVPDSD
     PDSLAVLHVI PTQNSAQERT CSMNFSMETP MKQPLRGAIY SPYGTEQWMV PAQGPYQPVS
     YTAYPTDLSA QGAVAHPHSG MSDWSQYSLF PYSCW
 
 
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