Detail Information for IndEnz0002016279
IED ID IndEnz0002016279
Enzyme Type ID protease016279
Protein Name Dickkopf-related protein 4
Dickkopf-4
Dkk-4
hDkk-4

Cleaved into: Dickkopf-related protein 4 short form
Gene Name DKK4
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MVAAVLLGLSWLCSPLGALVLDFNNIRSSADLHGARKGSQCLSDTDCNTRKFCLQPRDEKPFCATCRGLRRRCQRDAMCCPGTLCVNDVCTTMEDATPILERQLDEQDGTHAEGTTGHPVQENQPKRKPSIKKSQGRKGQEGESCLRTFDCGPGLCCARHFWTKICKPVLLEGQVCSRRGHKDTAQAPEIFQRCDCGPGLLCRSQLTSNRQHARLRVCQKIEKL
Enzyme Length 224
Uniprot Accession Number Q9UBT3
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (6); Chain (2); Compositional bias (1); Disulfide bond (5); Helix (1); Region (3); Sequence conflict (1); Signal peptide (1); Turn (2)
Keywords 3D-structure;Cleavage on pair of basic residues;Developmental protein;Direct protein sequencing;Disulfide bond;Reference proteome;Secreted;Signal;Wnt signaling pathway
Interact With Q96F15; P11215; Q96CV9; Q5TGU0
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification PTM: Appears to be not glycosylated.; PTM: Can be proteolytically processed by a furin-like protease. {ECO:0000269|PubMed:10570958}.
Signal Peptide SIGNAL 1..18; /evidence="ECO:0000269|PubMed:10570958, ECO:0000269|PubMed:15340161"
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 5O57;
Mapped Pubmed ID 11029007; 11137016; 11357136; 11433302; 11448771; 11701963; 11742004; 12050670; 12167704; 12205098; 12527209; 12897152; 15084453; 15459103; 17047023; 17553464; 18044981; 18408752; 18461655; 18502762; 18606139; 19059704; 19158955; 19453261; 19562778; 19659606; 19773279; 20053636; 20093360; 20650998; 21341386; 21944579; 21984209; 21994129; 22000855; 22000856; 22216841; 22249261; 22653731; 22740476; 23108157; 23256519; 23516639; 23791946; 23958302; 26419038; 26880586; 27272409; 28005267; 28450117; 28666421; 29925589; 31202458; 32713860;
Motif
Gene Encoded By
Mass 24,876
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda