ID   CXXC4_XENLA             Reviewed;         217 AA.
AC   Q800L6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=CXXC-type zinc finger protein 4;
DE   AltName: Full=Inhibition of the Dvl and axin complex protein;
DE            Short=xIdax;
GN   Name=cxxc4; Synonyms=idax;
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 [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15108311; DOI=10.1002/dvdy.20037;
RA   Michiue T., Fukui A., Yukita A., Sakurai K., Danno H., Kikuchi A.,
RA   Asashima M.;
RT   "XIdax, an inhibitor of the canonical Wnt pathway, is required for anterior
RT   neural structure formation in Xenopus.";
RL   Dev. Dyn. 230:79-90(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=11113207; DOI=10.1128/mcb.21.1.330-342.2001;
RA   Hino S., Kishida S., Michiue T., Fukui A., Sakamoto I., Takada S.,
RA   Asashima M., Kikuchi A.;
RT   "Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding
RT   protein.";
RL   Mol. Cell. Biol. 21:330-342(2001).
CC   -!- FUNCTION: Acts as a negative regulator of the Wnt signaling pathway
CC       required for anterior neural structure formation
CC       (PubMed:15108311,PubMed:11113207). Ectopic expression induces
CC       ventralization(PubMed:15108311,PubMed:11113207). Binds preferentially
CC       to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over
CC       CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-
CC       hydroxymethyl-CpG (By similarity). {ECO:0000250|UniProtKB:Q9H2H0,
CC       ECO:0000269|PubMed:11113207, ECO:0000269|PubMed:15108311}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9EQC9}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neural tissues at the neurula stage,
CC       and in the restricted region of the tadpole brain.
CC       {ECO:0000269|PubMed:15108311}.
CC   -!- DOMAIN: The CXXC zinc finger mediates binding to CpG-DNA.
CC       {ECO:0000250|UniProtKB:Q9H2H0}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB085700; BAC58028.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q800L6; -.
DR   SMR; Q800L6; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR040388; CXXC4/CXXC5.
DR   InterPro; IPR002857; Znf_CXXC.
DR   PANTHER; PTHR13419; PTHR13419; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Metal-binding; Reference proteome;
KW   Wnt signaling pathway; Zinc; Zinc-finger.
FT   CHAIN           1..217
FT                   /note="CXXC-type zinc finger protein 4"
FT                   /id="PRO_0000317545"
FT   ZN_FING         122..163
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
SQ   SEQUENCE   217 AA;  23171 MW;  4F776275C7A89D14 CRC64;
     MHRNDSQRLG KPGGAPESLQ MANNNFLSTL SPEHCRPLAG ECMNKLKCGA AEAEIMNLPE
     RVGTFSAIPA LGGISLPPGV IVMTALHSPA AASAAVTDSA FQIANLADCP QNNSSGAGGN
     PAKKKRKRCG VCVPCKRLIN CGVCSSCRNR KTGHQICKFR KCEELKKKPG TSLEVRGDDS
     FFPCLASSLI PPFSPPFQCF LSPFKMHHSF SESPSRL