Down syndrome cell adhesion molecule - O60469 (DSCAM_HUMAN)

 

Protein Feature View of PDB entries mapped to a UniProtKB sequence  

 
Function
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:10925149). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC. In spinal chord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding (PubMed:18585357, PubMed:19196994). Enhances netrin-induced phosphorylation of PAK1 and FYN (PubMed:15169762). Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (PubMed:18585357, PubMed:19196994). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions. UniProt
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Subunit Structure
Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (PubMed:15169762). Interacts (via extracellular domain) with NTN1 (PubMed:19196994). Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1. Interacts with RAC1; the interaction requires PAK1. UniProt
Domain
Ig-like C2-type domains 7 to 9 are sufficient for interaction with NTN1 and commissural axon outgrowth. The transmembrane domain is necessary for interaction with DCC. UniProt
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The PDB to UniProt mapping is based on the data provided by the EBI SIFTS project. See also Velankar et al., Nucleic Acids Research 33, D262-265 (2005).
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