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TF7L1_MOUSE
ID   TF7L1_MOUSE             Reviewed;         584 AA.
AC   Q9Z1J1; O70450; O70573;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Transcription factor 7-like 1;
DE   AltName: Full=HMG box transcription factor 3;
DE            Short=TCF-3;
DE            Short=mTCF-3;
GN   Name=Tcf7l1; Synonyms=Tcf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CTNNB1.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=9488439; DOI=10.1128/mcb.18.3.1248;
RA   Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G.,
RA   Markman M., Lamers W., Destree O., Clevers H.;
RT   "Two members of the Tcf family implicated in Wnt/b-catenin signaling during
RT   embryogenesis in the mouse.";
RL   Mol. Cell. Biol. 18:1248-1256(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-584.
RC   STRAIN=CD-1; TISSUE=Limb;
RA   Melchionna R., Murphy P., La Valle R., Borello U., Cossu G.;
RT   "Cloning of murine Tcf-3: a possible role in muscle development.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 173-584.
RA   Sussman D.J.;
RT   "Partial mRNA sequence of mouse transcription factor mTCF-3.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=10498690; DOI=10.1242/dev.126.20.4557;
RA   DasGupta R., Fuchs E.;
RT   "Multiple roles for activated LEF/TCF transcription complexes during hair
RT   follicle development and differentiation.";
RL   Development 126:4557-4568(1999).
RN   [5]
RP   FUNCTION, AND MUTAGENESIS OF LEU-383 AND PRO-407.
RX   PubMed=11445543; DOI=10.1101/gad.891401;
RA   Merrill B.J., Gat U., DasGupta R., Fuchs E.;
RT   "Tcf3 and Lef1 regulate lineage differentiation of multipotent stem cells
RT   in skin.";
RL   Genes Dev. 15:1688-1705(2001).
CC   -!- FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA and
CC       acts as a repressor in the absence of CTNNB1, and as an activator in
CC       its presence. Necessary for the terminal differentiation of epidermal
CC       cells, the formation of keratohyalin granules and the development of
CC       the barrier function of the epidermis. {ECO:0000269|PubMed:11445543}.
CC   -!- SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable
CC       complex.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Detected in the basal layer of epidermis and in
CC       outer root sheath and bulge of hair follicles.
CC       {ECO:0000269|PubMed:10498690}.
CC   -!- DOMAIN: The putative Groucho interaction domain between the N-terminal
CC       CTNNB1 binding domain and the HMG-box is necessary for repression of
CC       the transactivation mediated by TCF7L1 and CTNNB1.
CC   -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR   EMBL; AJ223069; CAA11070.1; -; mRNA.
DR   EMBL; AJ223233; CAA11201.1; -; mRNA.
DR   EMBL; AF057691; AAC13696.1; -; mRNA.
DR   RefSeq; NP_033358.2; NM_009332.3.
DR   AlphaFoldDB; Q9Z1J1; -.
DR   SMR; Q9Z1J1; -.
DR   BioGRID; 204008; 3.
DR   DIP; DIP-49605N; -.
DR   IntAct; Q9Z1J1; 5.
DR   STRING; 10090.ENSMUSP00000109687; -.
DR   iPTMnet; Q9Z1J1; -.
DR   PhosphoSitePlus; Q9Z1J1; -.
DR   MaxQB; Q9Z1J1; -.
DR   PaxDb; Q9Z1J1; -.
DR   PRIDE; Q9Z1J1; -.
DR   ProteomicsDB; 263296; -.
DR   DNASU; 21415; -.
DR   GeneID; 21415; -.
DR   KEGG; mmu:21415; -.
DR   CTD; 83439; -.
DR   MGI; MGI:1202876; Tcf7l1.
DR   eggNOG; KOG3248; Eukaryota.
DR   InParanoid; Q9Z1J1; -.
DR   Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-4641265; Repression of WNT target genes.
DR   Reactome; R-MMU-8853884; Transcriptional Regulation by VENTX.
DR   Reactome; R-MMU-8951430; RUNX3 regulates WNT signaling.
DR   BioGRID-ORCS; 21415; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Tcf7l1; mouse.
DR   PRO; PR:Q9Z1J1; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9Z1J1; protein.
DR   GO; GO:1990907; C:beta-catenin-TCF complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:MGI.
DR   GO; GO:0048319; P:axial mesoderm morphogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:1904672; P:regulation of somatic stem cell population maintenance; IMP:MGI.
DR   GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0043588; P:skin development; IGI:MGI.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR013558; CTNNB1-bd_N.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR024940; TCF/LEF.
DR   InterPro; IPR028778; Tcf7l1.
DR   PANTHER; PTHR10373; PTHR10373; 1.
DR   PANTHER; PTHR10373:SF25; PTHR10373:SF25; 1.
DR   Pfam; PF08347; CTNNB1_binding; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Wnt signaling pathway.
FT   CHAIN           1..584
FT                   /note="Transcription factor 7-like 1"
FT                   /id="PRO_0000048615"
FT   DNA_BIND        342..410
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..71
FT                   /note="CTNNB1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          159..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           417..423
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        76..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..229
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         383
FT                   /note="L->P: Abolishes DNA-binding and
FT                   transactivator/repressor activity; when associated with I-
FT                   407."
FT                   /evidence="ECO:0000269|PubMed:11445543"
FT   MUTAGEN         407
FT                   /note="P->I: Abolishes DNA-binding and
FT                   transactivator/repressor activity; when associated with P-
FT                   383."
FT                   /evidence="ECO:0000269|PubMed:11445543"
FT   CONFLICT        114
FT                   /note="G -> P (in Ref. 2; CAA11201)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="I -> M (in Ref. 2; CAA11201)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404..405
FT                   /note="QL -> HV (in Ref. 2; CAA11201)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463
FT                   /note="S -> I (in Ref. 2; CAA11201)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="A -> T (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   584 AA;  62298 MW;  BA8B4F570AFC72CB CRC64;
     MPQLGGGRGG AGGGGGGSGA GATSGGDDLG ANDELIPFQD EGGEEQEPSS DTASAQRDLD
     EVKSSLVNES ENQSSSSDSE AERRPQPARD AFQKPRDYFA EVRRPQDGAF FKGGAYPGYP
     FLMIPDLSSP YLSNGPLSPG GARTYLQMKW PLLDVPSSAT VKDTRSPSPA HLSNKVPVVQ
     HPHHMHPLTP LITYSNDHFS PASPPTHLSP EIDPKTGIPR PPHPSELSPY YPLSPGAVGQ
     IPHPLGWLVP QQGQPMYSLP PGGFRHPYPA LAMNASMSSL VSSRFPHMVA PAHPGLPTSG
     IPHPAIVSPI VKQEPAAPSL SPAVSAKSPV TVKKEEEKKP HVKKPLNAFM LYMKEMRAKV
     VAECTLKESA AINQILGRKW HNLSREEQAK YYELARKERQ LHAQLYPTWS ARDNYGKKKK
     RKREKQLSQT QSQQQIQEAE GALASKSKKP CIQYLPPEKP CDSPASSHGS ALDSPATPSA
     ALASPAAPAA THSEQAQPLS LTTKPEARAQ LALHSAAFLS AKAAASNSSQ MGSQPPLLSR
     PLPLGSMPAA LLTSPPTFPA TLHAHQALPV LQAQPLSLVT KSAH
 
 
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