DKK4_MOUSE
ID DKK4_MOUSE Reviewed; 221 AA.
AC Q8VEJ3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Dickkopf-related protein 4;
DE Short=Dickkopf-4;
DE Short=Dkk-4;
DE Flags: Precursor;
GN Name=Dkk4;
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=Czech II; TISSUE=Mammary tumor;
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 REVIEW OF THE DKK FAMILY.
RX PubMed=17143291; DOI=10.1038/sj.onc.1210054;
RA Niehrs C.;
RT "Function and biological roles of the Dickkopf family of Wnt modulators.";
RL Oncogene 25:7469-7481(2006).
CC -!- FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6
CC interaction with Wnt and by forming a ternary complex with the
CC transmembrane protein KREMEN that promotes internalization of LRP5/6.
CC DKKs play an important role in vertebrate development, where they
CC locally inhibit Wnt regulated processes such as antero-posterior axial
CC patterning, limb development, somitogenesis and eye formation. In the
CC adult, Dkks are implicated in bone formation and bone disease, cancer
CC and Alzheimer disease (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LRP5 and LRP6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: The C-terminal cysteine-rich domain mediates interaction with
CC LRP5 and LRP6. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dickkopf family. {ECO:0000305}.
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DR EMBL; BC018400; AAH18400.1; -; mRNA.
DR CCDS; CCDS22180.1; -.
DR RefSeq; NP_663567.1; NM_145592.2.
DR RefSeq; XP_006509161.1; XM_006509098.2.
DR AlphaFoldDB; Q8VEJ3; -.
DR SMR; Q8VEJ3; -.
DR STRING; 10090.ENSMUSP00000033936; -.
DR iPTMnet; Q8VEJ3; -.
DR PhosphoSitePlus; Q8VEJ3; -.
DR PaxDb; Q8VEJ3; -.
DR PRIDE; Q8VEJ3; -.
DR Antibodypedia; 24127; 414 antibodies from 33 providers.
DR DNASU; 234130; -.
DR Ensembl; ENSMUST00000033936; ENSMUSP00000033936; ENSMUSG00000031535.
DR GeneID; 234130; -.
DR KEGG; mmu:234130; -.
DR UCSC; uc009ldj.1; mouse.
DR CTD; 27121; -.
DR MGI; MGI:2385299; Dkk4.
DR VEuPathDB; HostDB:ENSMUSG00000031535; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000161614; -.
DR HOGENOM; CLU_080459_1_0_1; -.
DR InParanoid; Q8VEJ3; -.
DR OMA; RKFCLQP; -.
DR OrthoDB; 1139517at2759; -.
DR PhylomeDB; Q8VEJ3; -.
DR TreeFam; TF330916; -.
DR Reactome; R-MMU-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR BioGRID-ORCS; 234130; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dkk4; mouse.
DR PRO; PR:Q8VEJ3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VEJ3; protein.
DR Bgee; ENSMUSG00000031535; Expressed in renal cortex interstitium and 56 other tissues.
DR Genevisible; Q8VEJ3; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0039706; F:co-receptor binding; IBA:GO_Central.
DR GO; GO:0048019; F:receptor antagonist activity; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0061170; P:negative regulation of hair follicle placode formation; IDA:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR InterPro; IPR006796; Dickkopf_N.
DR InterPro; IPR039863; DKK-like.
DR InterPro; IPR023569; Prokineticin_domain.
DR PANTHER; PTHR12113; PTHR12113; 1.
DR Pfam; PF04706; Dickkopf_N; 1.
DR Pfam; PF06607; Prokineticin; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Reference proteome; Secreted;
KW Signal; Wnt signaling pathway.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..221
FT /note="Dickkopf-related protein 4"
FT /id="PRO_0000007227"
FT REGION 41..90
FT /note="DKK-type Cys-1"
FT REGION 101..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..218
FT /note="DKK-type Cys-2"
FT COMPBIAS 129..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 145..157
FT /evidence="ECO:0000250"
FT DISULFID 151..166
FT /evidence="ECO:0000250"
FT DISULFID 156..194
FT /evidence="ECO:0000250"
FT DISULFID 176..202
FT /evidence="ECO:0000250"
FT DISULFID 196..218
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 24261 MW; 670AD9F750BF1715 CRC64;
MVLVTLLGLS WFCSPLAALV LDFNNIKSSA DVQGAGKGSL CASDRDCSEG KFCLAFHDER
SFCATCRRVR RRCQRSAVCC PGTVCVNDVC TAVEDTRPVM DRNTDGQDGA YAEGTTKWPA
EENRPQGKPS TKKSQSSKGQ EGESCLRTSD CGPGLCCARH FWTKICKPVL REGQVCSRRG
HKDTAQAPEI FQRCDCGPGL TCRSQVTSNR QHSRLRVCQR I