KAISO_XENLA
ID KAISO_XENLA Reviewed; 701 AA.
AC Q8UVQ4; Q90X05;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transcriptional regulator Kaiso;
DE AltName: Full=Zinc finger and BTB domain-containing protein 33;
DE Short=xKaiso;
GN Name=zbtb33; Synonyms=kaiso;
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, SELF-ASSOCIATION, INTERACTION WITH
RP CTNND1, AND DEVELOPMENTAL STAGE.
RX PubMed=11751886; DOI=10.1074/jbc.m109508200;
RA Kim S.-W., Fang X., Ji H., Paulson A.F., Daniel J.M., Ciesiolka M.,
RA van Roy F., McCrea P.D.;
RT "Isolation and characterization of XKaiso, a transcriptional repressor that
RT associates with the catenin Xp120(ctn) in Xenopus laevis.";
RL J. Biol. Chem. 277:8202-8208(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DNA-BINDING.
RC TISSUE=Lung;
RX PubMed=15548582; DOI=10.1242/dev.01549;
RA Ruzov A., Dunican D.S., Prokhortchouk A., Pennings S., Stancheva I.,
RA Prokhortchouk E., Meehan R.R.;
RT "Kaiso is a genome-wide repressor of transcription that is essential for
RT amphibian development.";
RL Development 131:6185-6194(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=15543138; DOI=10.1038/ncb1191;
RA Kim S.-W., Park J.-I., Spring C.M., Sater A.K., Ji H., Otchere A.A.,
RA Daniel J.M., McCrea P.D.;
RT "Non-canonical Wnt signals are modulated by the Kaiso transcriptional
RT repressor and p120-catenin.";
RL Nat. Cell Biol. 6:1212-1220(2004).
RN [5]
RP FUNCTION, DNA-BINDING, SELF-ASSOCIATION, INTERACTION WITH NCOR1 AND
RP TCF7L1-A, AND MUTAGENESIS OF ASP-33 AND ARG-47.
RX PubMed=15935774; DOI=10.1016/j.devcel.2005.04.010;
RA Park J.-I., Kim S.-W., Lyons J.P., Ji H., Nguyen T.T., Cho K., Barton M.C.,
RA Deroo T., Vleminckx K., Moon R.T., McCrea P.D.;
RT "Kaiso/p120-catenin and TCF/beta-catenin complexes coordinately regulate
RT canonical Wnt gene targets.";
RL Dev. Cell 8:843-854(2005).
RN [6]
RP ERRATUM OF PUBMED:15935774.
RA Park J.-I., Kim S.-W., Lyons J.P., Ji H., Nguyen T.T., Cho K., Barton M.C.,
RA Deroo T., Vleminckx K., Moon R.T., McCrea P.D.;
RL Dev. Cell 9:305-305(2005).
CC -!- FUNCTION: Transcriptional regulator with bimodal DNA-binding
CC specificity. Binds to methylated CpG dinucleotides in the consensus
CC sequence 5'-CGCG-3' and also binds to the non-methylated consensus
CC sequence 5'-CTGCNA-3'. May recruit the N-CoR repressor complex to
CC promote histone deacetylation and the formation of repressive chromatin
CC structures in target gene promoters. Contributes to the repression of
CC target genes of the Wnt signaling pathway and to the methylation-
CC dependent repression of zygotic transcription prior to the mid-blastula
CC transition (MBT). Also required for gastrulation movements.
CC {ECO:0000269|PubMed:11751886, ECO:0000269|PubMed:15543138,
CC ECO:0000269|PubMed:15548582, ECO:0000269|PubMed:15935774}.
CC -!- SUBUNIT: Self associates. Interacts with tcf7l1-A, leading to
CC repression of tcf7l1-A target genes. Interacts with ctnnd1, and this
CC interaction may inhibit DNA-binding. Interacts with ncor1.
CC {ECO:0000269|PubMed:11751886, ECO:0000269|PubMed:15935774}.
CC -!- INTERACTION:
CC Q8UVQ4; Q8AXM9: ctnnd1; NbExp=2; IntAct=EBI-6261609, EBI-6260685;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and throughout development.
CC Expressed in the animal hemisphere of eggs and cleavage stage embryos.
CC Expressed in the ectodermal region of blastula and gastrula stage
CC embryos and in the anterior and dorsal regions of neurula stage
CC embryos. Expressed in the brain, ear, eye, branchial arches and spinal
CC cord of tailbud stage embryos. {ECO:0000269|PubMed:11751886}.
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DR EMBL; AF420316; AAL66228.1; -; mRNA.
DR EMBL; AY044336; AAK95689.1; -; mRNA.
DR EMBL; BC070994; AAH70994.1; -; mRNA.
DR RefSeq; NP_001082143.1; NM_001088674.1.
DR AlphaFoldDB; Q8UVQ4; -.
DR SMR; Q8UVQ4; -.
DR BioGRID; 99582; 3.
DR IntAct; Q8UVQ4; 1.
DR GeneID; 398248; -.
DR KEGG; xla:398248; -.
DR CTD; 398248; -.
DR Xenbase; XB-GENE-865623; zbtb33.S.
DR OrthoDB; 567120at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 398248; Expressed in blastula and 18 other tissues.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..701
FT /note="Transcriptional regulator Kaiso"
FT /id="PRO_0000046990"
FT DOMAIN 32..94
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 501..523
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 529..551
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 557..580
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 128..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..609
FT /note="Required for methylation dependent DNA-binding"
FT REGION 519..701
FT /note="Required for sequence specific DNA-binding"
FT REGION 644..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 33
FT /note="D->N: Abrogates interaction with NCOR1 and
FT transcriptional repression; when associated with Q-47."
FT /evidence="ECO:0000269|PubMed:15935774"
FT MUTAGEN 47
FT /note="R->Q: Abrogates interaction with NCOR1 and
FT transcriptional repression; when associated with N-33."
FT /evidence="ECO:0000269|PubMed:15935774"
FT CONFLICT 333
FT /note="I -> L (in Ref. 1; AAL66228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 77347 MW; 7556FC6F1049855F CRC64;
METKKLITAT DTQYSGILLN ALNDQRIQGL YCDVTVIVED RKFRAHRNIL SACSTYFHQL
FSVAGQVVEL NFVKADIFAE ILNYIYSSKI VRVRCDMLEE LIKSGKLLGV PFIAELGIPL
SQVKSISGAG GKDGGTDAPS NPDHKAPEPQ KSSDSPLPCT VKIKADVKTE MPVITESFSL
SSDDYKDKKA SGSQDHNSEK EDDDDDVIFC SEIVSSKQAP AERKEAAQTQ IPPDNEQVPE
VKKVTPSSQV QLTQNSLPTN QQSSKNTSST TQKFTPPVNA NISKNPTPAA NGFLSPTAQK
QGTPNAVQNQ HSQNITSGNA LPQQKPVVNF SSIKPQQISA IKPKTEVIIH GNGLSPPSSS
VIPLGQQPVT PKHISFDGVQ KKQVVTFTQG SPSKPGEFKI KIADVVSGSS LDSFKDSEPR
RIIDGKKIIT LDTASEIEGL STGCKVYANI GEDTYDIVIP IKEDPEEGEA KLDLDGLPNR
KRMKLKHDDH YELIVDGRVY YICIVCKRSY VCLTSLRRHF NVHSWEKKYP CRYCERVFPL
AEYRTKHEIH HTGERRYQCL TCGSSFINYQ VMASHIRSVH SLDPSGDSKL YRLNPCKTLQ
IRQYAYVNNS TNGTVINDGA INVPVITDGG INVPVINDGG IVYDIDPDEP QQPASEGNHA
NSATKPVNWD NIFIQQSNQN MFKLNTSEGG TEFEFVIPES Y
