Detail Information for IndEnz0002006793
IED ID IndEnz0002006793
Enzyme Type ID protease006793
Protein Name Dickkopf-related protein 2
Dickkopf-2
Dkk-2
mDkk-2
Gene Name Dkk2
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAALMRVKDSSRCLLLLAAVLMVESSQLGSSRAKLNSIKSSLGGETPAQSANRSAGMNQGLAFGGSKKGKSLGQAYPCSSDKECEVGRYCHSPHQGSSACMLCRRKKKRCHRDGMCCPGTRCNNGICIPVTESILTPHIPALDGTRHRDRNHGHYSNHDLGWQNLGRPHSKMPHIKGHEGDPCLRSSDCIDGFCCARHFWTKICKPVLHQGEVCTKQRKKGSHGLEIFQRCDCAKGLSCKVWKDATYSSKARLHVCQKI
Enzyme Length 259
Uniprot Accession Number Q9QYZ8
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. {ECO:0000269|PubMed:18524778}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Chain (1); Compositional bias (1); Disulfide bond (5); Glycosylation (1); Helix (1); Region (3); Sequence conflict (1); Signal peptide (1)
Keywords 3D-structure;Developmental protein;Disulfide bond;Glycoprotein;Reference proteome;Secreted;Signal;Wnt signaling pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification PTM: May be proteolytically processed by a furin-like protease.
Signal Peptide SIGNAL 1..33; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 2JTK;
Mapped Pubmed ID 11357136; 11742004; 12412008; 12466851; 12812787; 14681479; 15053977; 15527894; 15617677; 15759274; 15880404; 16056226; 16195809; 16521043; 16672341; 17971207; 18351675; 18367164; 18689976; 18927151; 19185060; 19282366; 19369394; 19562671; 19806668; 19924825; 20122913; 20439124; 20562862; 21078818; 21267068; 21354128; 21490069; 21531785; 21540552; 21586556; 21677750; 22407773; 22733757; 23201579; 23250216; 23364326; 23390542; 24091497; 24302887; 24496627; 24498290; 24586192; 24952961; 25044936; 25082703; 25377219; 25826080; 26273529; 26424886; 26450967; 26621269; 27053129; 27713059; 27736991; 28069742; 28250050; 28253399; 28605600; 28813421; 28893947; 29259207; 29559443; 29787744; 30478225; 30509557; 31201182; 31907354; 32580935; 33436499; 33647798; 34030936;
Motif
Gene Encoded By
Mass 28,432
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda