TB1RA_XENLA
ID TB1RA_XENLA Reviewed; 519 AA.
AC Q7SZM9;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=F-box-like/WD repeat-containing protein TBL1XR1-A;
DE AltName: Full=Nuclear receptor corepressor/HDAC3 complex subunit TBLR1-A;
DE AltName: Full=TBL1-related protein 1-A;
DE Short=xTBLR1;
DE AltName: Full=Transducin beta-like 1X-related protein 1-A;
GN Name=tbl1xr1-a; Synonyms=tblr1;
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], AND INTERACTION WITH NCOR1; RARA AND RXRA.
RX PubMed=12794076; DOI=10.1074/jbc.m303309200;
RA Tomita A., Buchholz D.R., Obata K., Shi Y.-B.;
RT "Fusion protein of retinoic acid receptor-alpha with promyelocytic leukemia
RT protein or promyelocytic leukemia zinc finger protein recruits N-CoR-TBLR1
RT corepressor complex to repress transcription in vivo.";
RL J. Biol. Chem. 278:30788-30795(2003).
RN [2]
RP INTERACTION WITH NCOR1; RXRA AND THRB, AND DEVELOPMENTAL STAGE.
RX PubMed=15060155; DOI=10.1128/mcb.24.8.3337-3346.2004;
RA Tomita A., Buchholz D.R., Shi Y.-B.;
RT "Recruitment of N-CoR/SMRT-TBLR1 corepressor complex by unliganded thyroid
RT hormone receptor for gene repression during frog development.";
RL Mol. Cell. Biol. 24:3337-3346(2004).
CC -!- FUNCTION: F-box-like protein which acts as an integral component of the
CC N-CoR transcriptional corepressor complex. Probably regulates
CC transcription activation mediated by nuclear receptors. May mediate the
CC recruitment of the 19S proteasome complex, leading to the subsequent
CC proteasomal degradation of the N-CoR complex, thereby allowing cofactor
CC exchange and transcription activation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with heterodimers of rxra and thrb, and this
CC interaction is abrogated by thyroid hormone binding to thrb. Interacts
CC with ncor1. {ECO:0000269|PubMed:12794076, ECO:0000269|PubMed:15060155}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing intestine both prior
CC to and during remodeling (stages NF54 to NF66).
CC {ECO:0000269|PubMed:15060155}.
CC -!- DOMAIN: The F-box-like domain is related to the F-box domain, and also
CC functions to recruit ubiquitin E3 ligase complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat EBI family. {ECO:0000305}.
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DR EMBL; AY225088; AAP20646.1; -; mRNA.
DR RefSeq; NP_001082621.1; NM_001089152.1.
DR AlphaFoldDB; Q7SZM9; -.
DR SMR; Q7SZM9; -.
DR BioGRID; 99938; 5.
DR IntAct; Q7SZM9; 2.
DR GeneID; 398608; -.
DR KEGG; xla:398608; -.
DR CTD; 398608; -.
DR Xenbase; XB-GENE-6255786; tbl1xr1.L.
DR OrthoDB; 1463197at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398608; Expressed in lung and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045183; Ebi-like.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
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; PTHR22846; PTHR22846; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..519
FT /note="F-box-like/WD repeat-containing protein TBL1XR1-A"
FT /id="PRO_0000051268"
FT DOMAIN 4..36
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 41..86
FT /note="F-box-like"
FT REPEAT 172..211
FT /note="WD 1"
FT REPEAT 228..267
FT /note="WD 2"
FT REPEAT 269..308
FT /note="WD 3"
FT REPEAT 311..349
FT /note="WD 4"
FT REPEAT 352..391
FT /note="WD 5"
FT REPEAT 394..442
FT /note="WD 6"
FT REPEAT 445..484
FT /note="WD 7"
FT REPEAT 486..519
FT /note="WD 8"
FT REGION 115..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56043 MW; 5E998EDC8C892296 CRC64;
MSISSDEVNF LVYRYLQESG FSHSAFTFGI ESHISQSNIN GALAPPAALI SIIQKGLQYV
EAEVSINEDG TLFDGRPIES LSLIDAVMPD VVQTRQQAYR DKLAQQQTAA AAAAAAAAAA
TPNNQQPPAK NGENTANGEE NGGHALANNH TDMMEVDGDV EIPSSKAVVL RGHESEVFIC
AWNPVSDLLA SGSGDSTARI WNLSENSTSG STQLVLRHCI REGGQDVPSN KDVTSLDWNS
EGTLLATGSY DGFARIWTKD GNLASTLGQH KGPIFALKWN KKGNFILSAG VDKTTIIWDA
HTGEAKQQFP FHSAPALDVD WQSNNTFASC STDMCIHVCK LGQDRPIKTF QGHTNEVNAI
KWDPTGNLLA SCSDDMTLKI WSMKHDTCVH DLQAHNKEIY TIKWSPTGPG TNNPNANLML
ASASFDSTVR LWDVDRGICI HTLTKHQEPV YSVAFSPDGR YLASGSFDKC VHIWNTQTGA
LVHSYRGTGG IFEVCWNAAG DKVGASASDG SVCVLDLRK
