TLE3A_DANRE
ID TLE3A_DANRE Reviewed; 761 AA.
AC O13166;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transducin-like enhancer protein 3-A {ECO:0000305};
DE AltName: Full=Groucho-related protein grg2 {ECO:0000303|PubMed:16326386};
DE AltName: Full=Protein groucho-2 {ECO:0000303|PubMed:27747413};
GN Name=tle3a {ECO:0000305};
GN Synonyms=grg2 {ECO:0000303|PubMed:16326386},
GN gro2 {ECO:0000303|PubMed:27747413}, groucho2 {ECO:0000303|PubMed:27747413};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=27747413; DOI=10.1007/s004270050103;
RA Wuelbeck C., Campos-Ortega J.A.;
RT "Two zebrafish homologues of the Drosophila neurogenic gene groucho and
RT their pattern of transcription during early embryogenesis.";
RL Dev. Genes Evol. 207:156-166(1997).
RN [2]
RP FUNCTION, AND INTERACTION WITH PNX.
RX PubMed=12642490; DOI=10.1242/dev.00418;
RA Bae Y.B., Shimizu T., Yabe T., Kim C., Hirata T., Nojima H., Muraoka O.,
RA Hirano T., Hibi M.;
RT "A homeobox gene, pnx, is involved in the formation of posterior neurons in
RT zebrafish.";
RL Development 130:1853-1865(2003).
RN [3]
RP INTERACTION WITH RIPPLY1.
RX PubMed=16326386; DOI=10.1016/j.devcel.2005.09.021;
RA Kawamura A., Koshida S., Hijikata H., Ohbayashi A., Kondoh H., Takada S.;
RT "Groucho-associated transcriptional repressor ripply1 is required for
RT proper transition from the presomitic mesoderm to somites.";
RL Dev. Cell 9:735-744(2005).
RN [4]
RP INTERACTION WITH TCF7L1A AND LBX2.
RX PubMed=25371059; DOI=10.1038/ncomms6368;
RA Lu F.I., Sun Y.H., Wei C.Y., Thisse C., Thisse B.;
RT "Tissue-specific derepression of TCF/LEF controls the activity of the
RT Wnt/beta-catenin pathway.";
RL Nat. Commun. 5:5368-5368(2014).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Enhances the transcriptional repression activity
CC of pnx. {ECO:0000269|PubMed:12642490}.
CC -!- SUBUNIT: Interacts with pnx (PubMed:12642490). Interacts with the WRPW
CC motif of ripply1 (PubMed:16326386). Interacts with tcf7l1a
CC (PubMed:25371059). Interacts (via C-terminus) with lbx2 (via N-
CC terminus) (PubMed:25371059). {ECO:0000269|PubMed:12642490,
CC ECO:0000269|PubMed:16326386, ECO:0000269|PubMed:25371059}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously during gastrulation.
CC Expressed in the entire presomitic mesoderm, including the tailbud,
CC throughout somitogenesis. Also expressed diffusely within whole somites
CC in young stages. In older stages, expression is restricted to
CC boundaries between somites. Also expressed in a dynamic manner within
CC the neural plate. {ECO:0000269|PubMed:27747413}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression decreases from the mid-blastula stages onwards before
CC increasing again at the start of gastrulation.
CC {ECO:0000269|PubMed:27747413}.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
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DR EMBL; Y12466; CAA73069.1; -; mRNA.
DR EMBL; U96340; AAB57807.1; -; mRNA.
DR AlphaFoldDB; O13166; -.
DR SMR; O13166; -.
DR STRING; 7955.ENSDARP00000045678; -.
DR PaxDb; O13166; -.
DR PRIDE; O13166; -.
DR ZFIN; ZDB-GENE-990415-86; tle3a.
DR eggNOG; KOG0639; Eukaryota.
DR InParanoid; O13166; -.
DR PRO; PR:O13166; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:1900052; P:regulation of retinoic acid biosynthetic process; IGI:ZFIN.
DR GO; GO:0061056; P:sclerotome development; IMP:ZFIN.
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 Nucleus; Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..761
FT /note="Transducin-like enhancer protein 3-A"
FT /id="PRO_0000051289"
FT REPEAT 473..511
FT /note="WD 1"
FT REPEAT 519..558
FT /note="WD 2"
FT REPEAT 563..602
FT /note="WD 3"
FT REPEAT 605..644
FT /note="WD 4"
FT REPEAT 646..685
FT /note="WD 5"
FT REPEAT 687..726
FT /note="WD 6"
FT REPEAT 728..761
FT /note="WD 7"
FT REGION 1..140
FT /note="Q domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 139..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..204
FT /note="GP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 205..274
FT /note="CcN domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 275..441
FT /note="SP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT MOTIF 231..234
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 187..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 82460 MW; 836A81E36527655F CRC64;
MYPQGRHPAP QTPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYIKL ANEKTEMQRH
YIMYYEMSYG LNIEMHKQTE IAKRLNAILA QIMPFLSQEH QQQVAQAVER AKQVTMTELN
AIIGVRGLPN LPLTQQLQAQ HLSHTHGPVA LTPPHPSGLQ PPGIPPVTGS GSGLLALGAL
GSQPHLPAKD EKNHHDLEHR ESTNNSISPS DSLRTTSEKH RGSSDYSLDS KKRKVEDKDS
MSRYDSDGDK SDDLVVDVSN EDPATPRGSP AHSPPENGID KPRPAKKDTP RRPASVASSG
STPSSKTKPP EHNDKSSTPG LKSKAPTPRN DAPTPGTSTT PGLRPILGKP PMEALAAPAL
RTPLTCPTPF AMMSHHEMNG SLTNPGVYAG LHISPQMSAA AAAAYGRSPM AGFEPPHMRA
PGLPASLTSI SGGKPAYSFH VSADGQMQPV PFPPDALIGP GIPRHARQIN TLSHGEVVCA
VTISNPTRHV YTGGKGCVKI WDISQPGSKS PVSQLDCLNR DNYIRSCKLL PDGRTLIVGG
EASTLTIWDL ASQTPRIKAE LTSSAPACYA LAISPDAKVC FSCCSDGNIA VWDLHNQTLV
RQFQGHTDGA SCIDISHDGT KLWTGGLDNT VRSWDLREGR QLQQHDFASQ IFSLGYCPTG
EWLAVGMESS NVEVLHHTKP DKYQLHLHES CVLSLKFAYC GKWFVSTGKD NLLNAWSTPY
GASIFQSKES SSVLSCDISA DDKYIVTGSG DKKATVYEVI Y
