Tissue Specificity | Expressed in cardiac muscle (at protein level). |
Post Translational Modifications | Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence. May be phosphorylated by OBSCN. O-glycosylated on Ser and Thr residues. |
Function | Calcium-dependent cell adhesion protein.preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells. Required for proper neurite branching. Required for pre- and postsynaptic organization. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. |
Protein Name | Cadherin-2Neural CadherinN-CadherinCd Antigen Cd325 |
Database Links | Reactome: R-MMU-381426Reactome: -MMU-418990Reactome: -MMU-525793Reactome: -MMU-8957275 |
Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinSarcolemmaCell JunctionAdherens JunctionDesmosomeCell SurfaceColocalizes With Tmem65 At The Intercalated Disk In CardiomyocytesColocalizes With Obscn At The Intercalated Disk And Sarcolemma In Cardiomyocytes |
Alternative ELISA Names | Cadherin-2 ELISA kitNeural Cadherin ELISA kitN-Cadherin ELISA kitCd Antigen Cd325 ELISA kitCdh2 ELISA kit |
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Information sourced from Uniprot.org