TLE3_RAT
ID TLE3_RAT Reviewed; 764 AA.
AC Q9JIT3;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transducin-like enhancer protein 3;
DE Short=rTLE3;
GN Name=Tle3; Synonyms=Esp3;
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=Brain cortex;
RX PubMed=10800926; DOI=10.1046/j.1471-4159.2000.0741838.x;
RA Feldman J.D., Vician L., Crispino M., Hoe W., Baudry M., Herschman H.R.;
RT "rTLE3, a newly identified transducin-like enhancer of split, is induced by
RT depolarization in brain.";
RL J. Neurochem. 74:1838-1847(2000).
RN [2]
RP REVIEW.
RX PubMed=18254933; DOI=10.1186/gb-2008-9-1-205;
RA Jennings B.H., Ish-Horowicz D.;
RT "The Groucho/TLE/Grg family of transcriptional co-repressors.";
RL Genome Biol. 9:R205.1-R205.7(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-217; SER-245;
RP THR-259; SER-263 AND SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits the transcriptional activation mediated
CC by CTNNB1 and TCF family members in Wnt signaling. The effects of full-
CC length TLE family members may be modulated by association with
CC dominant-negative AES (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer and heterooligomer with other family members.
CC Binds LEF1, TCF7, TCF7L1, TCF7L2 and FOXA2. Interacts with XIAP/BIRC4
CC and TCF7L2/TCF4. Interacts with TBX18 (via engrailed homology 1
CC repressor motif), leading to decreased of TBX18 transcriptional
CC activity. {ECO:0000250|UniProtKB:Q04726, ECO:0000250|UniProtKB:Q08122}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highly expressed in adrenal gland, small intestine,
CC kidney, lung, ovary and thyroid. Detected at lower levels in pituitary,
CC hippocampus, cortex, cerebellum and testis.
CC -!- INDUCTION: By kainic acid in the dentate gyrus.
CC -!- DOMAIN: WD repeat Groucho/TLE family members are characterized by 5
CC regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a
CC central CcN domain, containing a nuclear localization signal, and a
CC serine/proline-rich SP domain. The most highly conserved are the N-
CC terminal Q domain and the C-terminal WD-repeat domain.
CC {ECO:0000305|PubMed:18254933}.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. This ubiquitination does not affect
CC its stability, nuclear localization, or capacity to tetramerize but
CC inhibits its interaction with TCF7L2/TCF4 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
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; AF186092; AAF75590.1; -; mRNA.
DR RefSeq; NP_445852.1; NM_053400.1.
DR AlphaFoldDB; Q9JIT3; -.
DR SMR; Q9JIT3; -.
DR STRING; 10116.ENSRNOP00000018467; -.
DR iPTMnet; Q9JIT3; -.
DR PhosphoSitePlus; Q9JIT3; -.
DR PaxDb; Q9JIT3; -.
DR PRIDE; Q9JIT3; -.
DR GeneID; 84424; -.
DR KEGG; rno:84424; -.
DR UCSC; RGD:620292; rat.
DR CTD; 7090; -.
DR RGD; 620292; Tle3.
DR VEuPathDB; HostDB:ENSRNOG00000013013; -.
DR eggNOG; KOG0639; Eukaryota.
DR HOGENOM; CLU_007612_3_0_1; -.
DR InParanoid; Q9JIT3; -.
DR OMA; FDTQMRQ; -.
DR OrthoDB; 546143at2759; -.
DR PhylomeDB; Q9JIT3; -.
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-4641265; Repression of WNT target genes.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q9JIT3; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000013013; Expressed in thymus and 19 other tissues.
DR Genevisible; Q9JIT3; RN.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR005617; Groucho/TLE_N.
DR InterPro; IPR009146; Groucho_enhance.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10814; PTHR10814; 1.
DR Pfam; PF03920; TLE_N; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR01850; GROUCHOFAMLY.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation;
KW WD repeat; Wnt signaling pathway.
FT CHAIN 1..764
FT /note="Transducin-like enhancer protein 3"
FT /id="PRO_0000051282"
FT REPEAT 476..514
FT /note="WD 1"
FT REPEAT 522..561
FT /note="WD 2"
FT REPEAT 566..605
FT /note="WD 3"
FT REPEAT 608..647
FT /note="WD 4"
FT REPEAT 649..688
FT /note="WD 5"
FT REPEAT 690..729
FT /note="WD 6"
FT REPEAT 731..763
FT /note="WD 7"
FT REGION 1..131
FT /note="Q domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 130..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..199
FT /note="GP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 184..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..268
FT /note="CcN domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 269..444
FT /note="SP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT MOTIF 225..228
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 141..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 321
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
SQ SEQUENCE 764 AA; 82644 MW; 7C5EAAEC9AA1A2DB CRC64;
MYPQGRHPAP HQPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYDKL ANEKTEMQRH
YVMYYEMSYG LNIEMHKQTE IAKRLNTILA QIMPFLSQEH QQQVAQAVER AKQVTMTELN
AIIGQQQLQA QHLSHATHGP PVQLPPHPSG LQPPGIPPVT GSSSGLLALG ALGSQAHLAV
KDEKNHHELD HRERESSTNN SVSPSESLRA SEKHRGSADY SMEAKKRKAE EKDSLSRYDS
DGDKSDDLVV DVSNEDPATP RVSPAHSPPE NGLDKARGLK KDAPTSPASV ASSSSTPSSK
TKDLGHNDKS STPGLKSNTP TPRNDAPTPG TSTTPGLRSM PGKPPGMDPI ASALRTPISL
TSSYAAPFAM MSHHEMNGSL TSPSAYAGLH NIPSQMSAAA AAAAAAYGRS PMVGFDPHPP
MRATGLPSSL ASIPGGKPAY SFHVSADGQM QPVPFPHDAL AGPGIPRHAR QINTLSHGEV
VCAVTISNPT RHVYTGGKGC VKIWDISQPG SKSPISQLDC LNRDNYIRSC KLLPDGRTLI
VGGEASTLTI WDLASPTPRI KAELTSSAPA CYALAISPDA KVCFSCCSDG NIAVWDLHNQ
TLVRQFQGHT DGASCIDISH DGTKLWTGGL DNTVRSWDLR EGRQLQQHDF TSQIFSLGYC
PTGEWLAVGM ESSNVEVLHH TKPDKYQLHL HESCVLSLKF AYCGKWFVST GKDNLLNAWR
TPYGASIFQS KESSSVLSCD ISADDKYIVT GSGDKKATVY EVIY
