TLE4_RAT
ID TLE4_RAT Reviewed; 748 AA.
AC Q07141;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Transducin-like enhancer protein 4;
DE AltName: Full=Grg-4;
DE AltName: Full=Groucho-related protein 4;
DE AltName: Full=Protein ESP2;
GN Name=Tle4; Synonyms=Esp2, Grg4;
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=Hippocampus;
RX PubMed=8245004; DOI=10.1016/s0021-9258(19)74443-3;
RA Schmidt C.J., Sladek T.E.;
RT "A rat homolog of the Drosophila enhancer of split (groucho) locus lacking
RT WD-40 repeats.";
RL J. Biol. Chem. 268:25681-25686(1993).
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-183 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 PAX5, and by CTNNB1 and TCF family members in Wnt signaling. The
CC effects of full-length TLE family members may be modulated by
CC association with dominant-negative AES. Essential for the
CC transcriptional repressor activity of SIX3 during retina and lens
CC development and for SIX3 transcriptional auto-repression (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with other family members.
CC Binds PAX5, LEF1, TCF7, TCF7L1 and TCF7L2. Interacts with ZNF703; TLE4
CC may mediate ZNF703 transcriptional repression. Interacts with SIX3 and
CC SIX6. Interacts with PAX2 (By similarity).
CC {ECO:0000250|UniProtKB:Q04727}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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: Phosphorylated. PAX5 binding increases phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37640.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L14463; AAC37640.1; ALT_INIT; mRNA.
DR PIR; B49555; B49555.
DR RefSeq; NP_062014.2; NM_019141.2.
DR AlphaFoldDB; Q07141; -.
DR SMR; Q07141; -.
DR STRING; 10116.ENSRNOP00000018272; -.
DR iPTMnet; Q07141; -.
DR PhosphoSitePlus; Q07141; -.
DR PaxDb; Q07141; -.
DR PRIDE; Q07141; -.
DR GeneID; 25565; -.
DR KEGG; rno:25565; -.
DR CTD; 7091; -.
DR RGD; 3868; Tle4.
DR eggNOG; KOG0639; Eukaryota.
DR InParanoid; Q07141; -.
DR OrthoDB; 546143at2759; -.
DR PhylomeDB; Q07141; -.
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 PRO; PR:Q07141; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
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:0016055; P:Wnt signaling pathway; ISO:RGD.
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; 1.
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..748
FT /note="Transducin-like enhancer protein 4"
FT /id="PRO_0000051285"
FT REPEAT 460..498
FT /note="WD 1"
FT REPEAT 506..545
FT /note="WD 2"
FT REPEAT 550..589
FT /note="WD 3"
FT REPEAT 592..631
FT /note="WD 4"
FT REPEAT 633..672
FT /note="WD 5"
FT REPEAT 674..713
FT /note="WD 6"
FT REPEAT 715..748
FT /note="WD 7"
FT REGION 1..112
FT /note="Q domain"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..179
FT /note="GP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT REGION 157..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..249
FT /note="CcN domain"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT REGION 250..427
FT /note="SP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT COMPBIAS 157..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT MOD_RES 225
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q04727, ECO:0000255"
FT MOD_RES 240
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62441"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62441"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62441"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
SQ SEQUENCE 748 AA; 81334 MW; E6DB66EBAECD66AD CRC64;
MIRDLSKMYR RRAHPAPHQP AQPFKFTISE SCDRIKEEFQ FLQAQYHSLK LECEKLASEK
TEMQRHYVMY YEMSYGLNIE MHKQAEIVKR LNAICAQVIP CLSQEQQQLQ AQHLLTWTWS
ACASDTTPLG FSQPFHPSGS SAGLLALSSA LGGQSHLPIK DEKKHHDNDH QRDRDSIKSS
SVSPSASFRG SEKHRNSTDY SSESKKQKTE EKEIAARYDS DGEKSDDNLV VDVSNEDPSS
PRGSPAHSPR ENGLDKTRLL KKDAPISPAS VASSSSTPSS KSKELSLNEK STTPVSKSNT
PTPRTDAPTP GSNSTPGLRP VPGKPPGVDP LASSLRTPMA VPCPYPTPFG IVPHAGMNGE
LTSPGAAYAG LHNISPQMSA AAAAAAAAAA YGRSPVVGFD PHHHMRVPAI PPNLTGIPGG
KPAYSFHVSA DGQMQPVPFP PDALIGPGIP RHARQINTLN HGEVVCAVTI SNPTRHVYTG
GKGCVKVWDI TDPGNKSPVS QLDCLNRDNY IRSCRLLPDG RTLIVGGEAS TLSIWDLAAP
TPRIKAELTS SAPACYALAI SPDSKVCFSC CSDGNIAVWD LHNQTLVRQF QGHTDGASCI
DISNDGTKLW TGGLDNTVRS WDLREGRQLQ QHDFTSQIFS LGYCPTGEWL AVGMENSNVE
VLHVTKPDKY QLHLHESCVL SLKFAHCGKW FVRPGKDNLL NAWRTPYGAS IFQSKESSSV
LSCDISADDK YIVTGSGDKK ATVYEVIY
