TLE4_XENLA
ID TLE4_XENLA Reviewed; 772 AA.
AC O42478; Q6AX22; Q9PSX1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transducin-like enhancer protein 4;
DE AltName: Full=Enhancer of split groucho-like protein 2;
DE Short=ESG2;
DE Short=xESG2;
DE AltName: Full=Grg-4;
DE Short=XGrg-4;
DE AltName: Full=Groucho-related protein 4;
GN Name=tle4; Synonyms=esg2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TCF7L1 AND TCF7, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9783587; DOI=10.1038/26989;
RA Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H., Moerer P.,
RA van de Wetering M., Destree O., Clevers H.;
RT "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
RT transcriptional repressors.";
RL Nature 395:608-612(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 575-772, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Liver;
RX PubMed=9300818; DOI=10.1016/s0378-1119(97)00150-9;
RA Choudhury B.K., Kim J., Kung H.-F., Li S.S.-L.;
RT "Cloning and developmental expression of Xenopus cDNAs encoding the
RT Enhancer of split groucho and related proteins.";
RL Gene 195:41-48(1997).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10704855; DOI=10.1016/s0925-4773(99)00259-2;
RA Molenaar M., Brian E., Roose J., Clevers H., Destree O.;
RT "Differential expression of the Groucho-related genes 4 and 5 during early
RT development of Xenopus laevis.";
RL Mech. Dev. 91:311-315(2000).
RN [5]
RP INTERACTION WITH RIPPLY2.2.
RX PubMed=16586348; DOI=10.1387/ijdb.052138ak;
RA Kondow A., Hitachi K., Ikegame T., Asashima M.;
RT "Bowline, a novel protein localized to the presomitic mesoderm, interacts
RT with Groucho/TLE in Xenopus.";
RL Int. J. Dev. Biol. 50:473-479(2006).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH RIPPLY2.2 AND TBX6.
RX PubMed=17577580; DOI=10.1016/j.bbrc.2007.05.211;
RA Kondow A., Hitachi K., Okabayashi K., Hayashi N., Asashima M.;
RT "Bowline mediates association of the transcriptional corepressor XGrg-4
RT with Tbx6 during somitogenesis in Xenopus.";
RL Biochem. Biophys. Res. Commun. 359:959-964(2007).
RN [7]
RP INTERACTION WITH FOXD3.
RX PubMed=17138566; DOI=10.1074/jbc.m607412200;
RA Yaklichkin S., Steiner A.B., Lu Q., Kessler D.S.;
RT "FoxD3 and Grg4 physically interact to repress transcription and induce
RT mesoderm in Xenopus.";
RL J. Biol. Chem. 282:2548-2557(2007).
RN [8]
RP INTERACTION WITH DSCR6.
RX PubMed=19247927; DOI=10.1387/ijdb.082823kh;
RA Hitachi K., Danno H., Tazumi S., Aihara Y., Uchiyama H., Okabayashi K.,
RA Kondow A., Asashima M.;
RT "The Xenopus Bowline/Ripply family proteins negatively regulate the
RT transcriptional activity of T-box transcription factors.";
RL Int. J. Dev. Biol. 53:631-639(2009).
RN [9]
RP INTERACTION WITH EFNB1, AND DEVELOPMENTAL STAGE.
RX PubMed=21429299; DOI=10.5483/bmbrep.2011.44.3.199;
RA Kamata T., Bong Y.S., Mood K., Park M.J., Nishanian T.G., Lee H.S.;
RT "EphrinB1 interacts with the transcriptional co-repressor Groucho/xTLE4.";
RL BMB Rep. 44:199-204(2011).
CC -!- FUNCTION: Transcriptional corepressor. Functions with ripply2.2/bowline
CC to down regulate transcription of tbx6-dependent gene expression.
CC Represses transcription of siamois and nodal3.
CC {ECO:0000269|PubMed:9783587}.
CC -!- SUBUNIT: Interacts with tcf7, tcf7l1, ripply2.2/bowline, dscr6/ripply3
CC and foxd3. Associates with tbx6 in the presence of ripply2.2/bowline.
CC Interacts with EFNB1 through the SP domain.
CC {ECO:0000269|PubMed:16586348, ECO:0000269|PubMed:17138566,
CC ECO:0000269|PubMed:17577580, ECO:0000269|PubMed:19247927,
CC ECO:0000269|PubMed:21429299, ECO:0000269|PubMed:9783587}.
CC -!- INTERACTION:
CC O42478; Q25QX6: ripply2.2; NbExp=2; IntAct=EBI-2946644, EBI-2946647;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the spleen and ovary.
CC {ECO:0000269|PubMed:10704855, ECO:0000269|PubMed:9300818}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. At end of gastrulation,
CC expressed in the prospective neural plate region. In neurula stages,
CC shows highest expression in the sensorial layer of the neurectoderm,
CC decreasing from anterior to posterior. Shows localized expression
CC within the anterior neural plate, including the floor of the neural
CC groove. Expressed in the cement gland anlage at stage 14. At stage 16,
CC expressed in the neural groove, rhombomeres, forebrain and branchial
CC arches. At stage 22, abundant in the eye vesicles, ear placodes,
CC prospective branchial arches, pronephric anlage, prospective pronephric
CC duct, presomitic mesoderm and the somites. In the developing brain,
CC expression is dynamic, being most abundant in the mesencephalon and
CC posterior rhombencephalon. At stage 30, expressed in cephalic ganglia V
CC and VII and in stage 35, also IX and X. Also expressed in the future
CC endocardium and pericardium. At stage 32, expressed in the neural
CC groove, rhombomeres, forebrain and branchial arches. At stage 35,
CC expressed in the future choroid plexus of the telencephalon and in the
CC ependymal layer. Throughout the neural tube, expressed in a dorsal to
CC ventral gradient. In the developing eye, expressed in the prospective
CC ganglion cell layer, the ciliary marginal zone and the lens.
CC {ECO:0000269|PubMed:10704855, ECO:0000269|PubMed:21429299,
CC ECO:0000269|PubMed:9783587}.
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. The SP domain is
CC involved in EFNB1-binding. {ECO:0000269|PubMed:21429299}.
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=CAA12236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ224945; CAA12236.1; ALT_INIT; mRNA.
DR EMBL; BC079799; AAH79799.1; -; mRNA.
DR EMBL; U63516; AAC60273.1; -; mRNA.
DR RefSeq; NP_001084260.1; NM_001090791.1.
DR AlphaFoldDB; O42478; -.
DR SMR; O42478; -.
DR IntAct; O42478; 1.
DR DNASU; 399397; -.
DR GeneID; 399397; -.
DR CTD; 399397; -.
DR Xenbase; XB-GENE-481770; tle4.S.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 399397; Expressed in blastula and 19 other tissues.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0017053; C:transcription repressor complex; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IGI:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
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; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..772
FT /note="Transducin-like enhancer protein 4"
FT /id="PRO_0000051291"
FT REPEAT 484..522
FT /note="WD 1"
FT REPEAT 530..569
FT /note="WD 2"
FT REPEAT 574..613
FT /note="WD 3"
FT REPEAT 616..655
FT /note="WD 4"
FT REPEAT 657..696
FT /note="WD 5"
FT REPEAT 698..737
FT /note="WD 6"
FT REPEAT 739..772
FT /note="WD 7"
FT REGION 1..137
FT /note="Q domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..205
FT /note="GP domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 183..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..275
FT /note="CcN domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 276..452
FT /note="SP domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT COMPBIAS 183..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 17
FT /note="P -> A (in Ref. 1; CAA12236)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="N -> D (in Ref. 1; CAA12236)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="G -> GQ (in Ref. 1; CAA12236)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="D -> S (in Ref. 1; CAA12236)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="V -> R (in Ref. 1; CAA12236)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="C -> V (in Ref. 1; CAA12236)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="N -> S (in Ref. 3; AAC60273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 83706 MW; 47E4C2420CBF89FA CRC64;
MIRDLSKMYP QTRHPAPPHQ PAQPFKFTIS ESCDRIKEEF QFLQAQYHSL KLECEKLASE
KTEMQRHYVM YYEMSYGLNI EMHKQAEIVK RLNAICAQVI PFLSQEHQQQ VVQAVERAKQ
VTMAELNAII GQQLQAQHLS HAHGLPVPLT PHPSGLQPPA IPSIGSSAGL LALSSALGGQ
SHLPIKDEKK HHDSDHQRDR DSIKSSSVSP SASFRAAEKH RNSTDYSSES KKQKTEEKDI
AARYDSDGEK SDDNLVVDVS NEDPSSPRGS PAHSPRENGL DKPRLLKKDA PISPASIASS
SSTPSSKSKE HSHNEKSTTP VSKSNTPTPR TDAPTPGSNS SGLRPVPGKP PGVDPLTGLR
TPMAVPCPYP TPFGIVPHAG MNGDLTSPGP AYASLHSISP QMSAAAAAAA AAAAYGRSPV
VGFDPHHHMR VPGIPPNLTG IPGGKPAYSF HVSADGQMQP VPFPPDALIG PGIPRHARQI
NTLNHGEVVC AVTISNPTRH VYTGGKGCVK VWDISHPGNK SPVSQLDCLN RDNYIRSCRL
LPDGRTLIVG GEASTLSIWD LAAPTPRIKA ELTSSAPACY ALAISPDSKV CFSCCSDGNI
AVWDLHNQTL VRQFQGHTDG ASCIDISNDG TKLWTGGLDN TVRSWDLREG RQLQQHDFTS
QIFSLGYCPT GEWLAVGMEN SNVEVLHVTK PDKYQLHLHE SCVLSLKFAH CGKWFVSTGK
DNLLNAWRTP YGASIFQSKE SSSVLSCDIS VDDKYIVTGS GDKKATVYEV IY
