CXXC4_RAT
ID CXXC4_RAT Reviewed; 198 AA.
AC Q9EQC9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=CXXC-type zinc finger protein 4;
DE AltName: Full=Inhibition of the Dvl and axin complex protein;
GN Name=Cxxc4; Synonyms=Idax;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH DVL1.
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).
RN [2]
RP INTERACTION WITH DVL1.
RX PubMed=15313210; DOI=10.1016/j.bbrc.2004.07.113;
RA London T.B.C., Lee H.-J., Shao Y., Zheng J.;
RT "Interaction between the internal motif KTXXXI of Idax and mDvl PDZ
RT domain.";
RL Biochem. Biophys. Res. Commun. 322:326-332(2004).
CC -!- FUNCTION: Acts as a negative regulator of the Wnt signaling pathway via
CC its interaction with DVL1 (By similarity). Binds preferentially to DNA
CC containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH
CC (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-
CC CpG (By similarity). {ECO:0000250|UniProtKB:Q6NXI8,
CC ECO:0000250|UniProtKB:Q9H2H0}.
CC -!- SUBUNIT: Interacts with the PDZ domain of DVL1.
CC {ECO:0000269|PubMed:11113207, ECO:0000269|PubMed:15313210}.
CC -!- INTERACTION:
CC Q9EQC9; O14640: DVL1; Xeno; NbExp=5; IntAct=EBI-9344960, EBI-723489;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11113207}.
CC -!- TISSUE SPECIFICITY: Highest expression in cerebrum, cerebellum and
CC heart, and lower expression in thymus and testis.
CC {ECO:0000269|PubMed:11113207}.
CC -!- DOMAIN: The CXXC zinc finger mediates binding to CpG-DNA.
CC {ECO:0000250|UniProtKB:Q9H2H0}.
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DR EMBL; AF272158; AAG42071.1; -; mRNA.
DR AlphaFoldDB; Q9EQC9; -.
DR SMR; Q9EQC9; -.
DR IntAct; Q9EQC9; 3.
DR STRING; 10116.ENSRNOP00000067828; -.
DR PaxDb; Q9EQC9; -.
DR RGD; 69228; Cxxc4.
DR eggNOG; ENOG502QQVJ; Eukaryota.
DR InParanoid; Q9EQC9; -.
DR PhylomeDB; Q9EQC9; -.
DR TreeFam; TF326617; -.
DR PRO; PR:Q9EQC9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Reference proteome;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..198
FT /note="CXXC-type zinc finger protein 4"
FT /id="PRO_0000317544"
FT ZN_FING 132..173
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 114..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..166
FT /note="Interaction with DVL1"
FT /evidence="ECO:0000269|PubMed:11113207"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 154
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 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
SQ SEQUENCE 198 AA; 20978 MW; 9D9F7FAD11A9B759 CRC64;
MHHRNDSQRL GKAGCPPEPS LQMANTNFLS TLSPEHCRPL AGECMNKLKC GAAEAEIMNL
PERVGTFSAI PALGGISLPP GVIVMTALHS PAAASAAVTD SAFQIANLAD CPQNHSSSSS
SSSGGAGGAN PAKKKRKRCG VCVPCKRLIN CGVCSSCRNR KTGHQICKFR KCEELKKKPG
TSLERTPVPS AEAFRWFF
