CXXC4_MOUSE
ID CXXC4_MOUSE Reviewed; 198 AA.
AC Q6NXI8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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 via
CC its interaction with DVL1 (PubMed:11113207). Binds preferentially to
CC 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}.
CC -!- SUBUNIT: Interacts with the PDZ domain of DVL1.
CC {ECO:0000250|UniProtKB:Q9EQC9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9EQC9}.
CC -!- DEVELOPMENTAL STAGE: Highest expression at embryonic day 11.
CC {ECO:0000269|PubMed:11113207}.
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; BC067052; AAH67052.1; -; mRNA.
DR EMBL; BC082332; AAH82332.1; -; mRNA.
DR AlphaFoldDB; Q6NXI8; -.
DR SMR; Q6NXI8; -.
DR STRING; 10090.ENSMUSP00000138000; -.
DR PhosphoSitePlus; Q6NXI8; -.
DR MaxQB; Q6NXI8; -.
DR PaxDb; Q6NXI8; -.
DR PRIDE; Q6NXI8; -.
DR ProteomicsDB; 277933; -.
DR Antibodypedia; 45113; 129 antibodies from 20 providers.
DR Ensembl; ENSMUST00000166288; ENSMUSP00000128574; ENSMUSG00000044365.
DR MGI; MGI:2442112; Cxxc4.
DR VEuPathDB; HostDB:ENSMUSG00000044365; -.
DR eggNOG; ENOG502QQVJ; Eukaryota.
DR GeneTree; ENSGT00940000154108; -.
DR HOGENOM; CLU_104023_0_0_1; -.
DR InParanoid; Q6NXI8; -.
DR OMA; HHRNESQ; -.
DR PhylomeDB; Q6NXI8; -.
DR TreeFam; TF326617; -.
DR ChiTaRS; Cxxc4; mouse.
DR PRO; PR:Q6NXI8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6NXI8; protein.
DR Bgee; ENSMUSG00000044365; Expressed in vas deferens and 221 other tissues.
DR ExpressionAtlas; Q6NXI8; baseline and differential.
DR Genevisible; Q6NXI8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IPI:MGI.
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..198
FT /note="CXXC-type zinc finger protein 4"
FT /id="PRO_0000317543"
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:0000250|UniProtKB:Q9EQC9"
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
