LEF1_RAT
ID LEF1_RAT Reviewed; 397 AA.
AC Q9QXN1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Lymphoid enhancer-binding factor 1;
DE Short=LEF-1;
GN Name=Lef1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=10824856;
RA Kobielak K., Kobielak A., Trzeciak W.H.;
RT "Cloning of the lymphoid enhancer binding factor-1 (Lef-1) cDNA from rat
RT kidney: homology to the mouse sequence.";
RL Acta Biochim. Pol. 46:885-888(1999).
CC -!- FUNCTION: Transcription factor that binds DNA in a sequence-specific
CC manner (By similarity). Participates in the Wnt signaling pathway (By
CC similarity). Activates transcription of target genes in the presence of
CC CTNNB1 and EP300 (By similarity). PIASG antagonizes both Wnt-dependent
CC and Wnt-independent activation by LEF1 (By similarity). TLE1, TLE2,
CC TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1 (By
CC similarity). Regulates T-cell receptor alpha enhancer function (By
CC similarity). Required for IL17A expressing gamma-delta T-cell
CC maturation and development, via binding to regulator loci of BLK to
CC modulate expression (By similarity). May play a role in hair cell
CC differentiation and follicle morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P27782, ECO:0000250|UniProtKB:Q9UJU2}.
CC -!- SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable
CC complex. Interacts with TLE1, PIASG, ALYREF/THOC4, EP300, MDFI and
CC MDFIC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC Note=Found in nuclear bodies upon PIASG binding. {ECO:0000250}.
CC -!- DOMAIN: Proline-rich and acidic regions are implicated in the
CC activation functions of RNA polymerase II transcription factors.
CC -!- PTM: Phosphorylated at Thr-153 and/or Ser-164 by NLK. Phosphorylation
CC by NLK at these sites represses LEF1-mediated transcriptional
CC activation of target genes of the canonical Wnt signaling pathway (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR EMBL; AF198533; AAF15601.1; -; mRNA.
DR RefSeq; NP_569113.1; NM_130429.1.
DR AlphaFoldDB; Q9QXN1; -.
DR BMRB; Q9QXN1; -.
DR SMR; Q9QXN1; -.
DR BioGRID; 250906; 1.
DR IntAct; Q9QXN1; 1.
DR MINT; Q9QXN1; -.
DR STRING; 10116.ENSRNOP00000013694; -.
DR iPTMnet; Q9QXN1; -.
DR PhosphoSitePlus; Q9QXN1; -.
DR PaxDb; Q9QXN1; -.
DR GeneID; 161452; -.
DR KEGG; rno:161452; -.
DR CTD; 51176; -.
DR RGD; 620241; Lef1.
DR eggNOG; KOG3248; Eukaryota.
DR InParanoid; Q9QXN1; -.
DR OrthoDB; 807716at2759; -.
DR PhylomeDB; Q9QXN1; -.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-4641265; Repression of WNT target genes.
DR Reactome; R-RNO-8951430; RUNX3 regulates WNT signaling.
DR PRO; PR:Q9QXN1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:RGD.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; ISO:RGD.
DR GO; GO:0060033; P:anatomical structure regression; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISO:RGD.
DR GO; GO:0042100; P:B cell proliferation; ISO:RGD.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEP:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
DR GO; GO:0048468; P:cell development; ISO:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:RGD.
DR GO; GO:0071353; P:cellular response to interleukin-4; ISO:RGD.
DR GO; GO:0060710; P:chorio-allantoic fusion; ISO:RGD.
DR GO; GO:0021542; P:dentate gyrus development; ISO:RGD.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0021873; P:forebrain neuroblast division; ISO:RGD.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; ISO:RGD.
DR GO; GO:0021943; P:formation of radial glial scaffolds; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0097043; P:histone H3-K56 acetylation; ISO:RGD.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0030879; P:mammary gland development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; ISO:RGD.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:RGD.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; ISO:RGD.
DR GO; GO:0032713; P:negative regulation of interleukin-4 production; ISO:RGD.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; ISO:RGD.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030223; P:neutrophil differentiation; ISO:RGD.
DR GO; GO:0071895; P:odontoblast differentiation; IMP:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0048341; P:paraxial mesoderm formation; ISO:RGD.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; ISO:RGD.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISO:RGD.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0062009; P:secondary palate development; ISO:RGD.
DR GO; GO:0050909; P:sensory perception of taste; ISO:RGD.
DR GO; GO:0043588; P:skin development; IEP:RGD.
DR GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:RGD.
DR GO; GO:0033153; P:T cell receptor V(D)J recombination; ISO:RGD.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; ISO:RGD.
DR GO; GO:0043586; P:tongue development; ISO:RGD.
DR GO; GO:0061153; P:trachea gland development; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
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; IPR028769; LEF1.
DR InterPro; IPR024940; TCF/LEF.
DR PANTHER; PTHR10373; PTHR10373; 1.
DR PANTHER; PTHR10373:SF11; PTHR10373:SF11; 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 2: Evidence at transcript level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..397
FT /note="Lymphoid enhancer-binding factor 1"
FT /id="PRO_0000048597"
FT DNA_BIND 297..365
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..60
FT /note="CTNNB1-binding"
FT /evidence="ECO:0000250"
FT REGION 38..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU2"
FT MOD_RES 153
FT /note="Phosphothreonine; by NLK"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU2"
FT MOD_RES 164
FT /note="Phosphoserine; by NLK"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU2"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 44023 MW; D6BEFF805CB526EA CRC64;
MPQLSGGGGG GDPELCATDE MIPFKDEGDP QKEKIFAEIS HPEEEGDLAD IKSSLVNESE
IIPASNGHEV VGQTQSSQEP YHDKAREHPD DGKHPDGGLY NKGPSYSSYS GYIMMPNMNS
DPYMSNGSLS PPIPRTSNKV PVVQPSHAVH PLTPLITYSD EHFSPGSHPS HIPSEVNPKQ
GMSRHPPAPE MPTFYPLSPG GVGQITPPLG WQGQPVYPIT GGFRQAYPSS LSGDTSMSRF
SHHMIPGPPG PHTTGIPHPA IVTPQVKQEH PHTDSDLMHV KPEHEQRKEQ EPKRPHIKKP
LNAFMLYMKE MRANVVAECT LKESAAINQI LGRRWHALSR EEQAKYYELA RKERQLHMQL
YPGWSARDNY GKKKKRKREK LQESTSGTGP RMTAAYI
